PMCCPMCCPMCC

Search tips
Search criteria 

Advanced

 
Logo of ijmsMDPIhomeThis articleThis journalInstructions for authorsSubscribeIJMS
 
Int J Mol Sci. 2017 July; 18(7): 1544.
Published online 2017 July 17. doi:  10.3390/ijms18071544
PMCID: PMC5536032

Correlation between Oxidative Stress, Nutrition, and Cancer Initiation

Abstract

Inadequate or excessive nutrient consumption leads to oxidative stress, which may disrupt oxidative homeostasis, activate a cascade of molecular pathways, and alter the metabolic status of various tissues. Several foods and consumption patterns have been associated with various cancers and approximately 30–35% of the cancer cases are correlated with overnutrition or malnutrition. However, several contradictory studies are available regarding the association between diet and cancer risk, which remains to be elucidated. Concurrently, oxidative stress is a crucial factor for cancer progression and therapy. Nutritional oxidative stress may be induced by an imbalance between antioxidant defense and pro-oxidant load due to inadequate or excess nutrient supply. Oxidative stress is a physiological state where high levels of reactive oxygen species (ROS) and free radicals are generated. Several signaling pathways associated with carcinogenesis can additionally control ROS generation and regulate ROS downstream mechanisms, which could have potential implications in anticancer research. Cancer initiation may be modulated by the nutrition-mediated elevation in ROS levels, which can stimulate cancer initiation by triggering DNA mutations, damage, and pro-oncogenic signaling. Therefore, in this review, we have provided an overview of the relationship between nutrition, oxidative stress, and cancer initiation, and evaluated the impact of nutrient-mediated regulation of antioxidant capability against cancer therapy.

Keywords: nutrition, oxidative stress, reactive oxygen species, cancer progression

1. Introduction

Nutrition is proposed to play an essential role in cancer progression. Cancer is the second leading cause of deaths in people from developed countries, whereas it is the most leading cause of death in people from developing or underdeveloped countries [1,2]. According to the International Agency for Research on Cancer (IARC), more than 10 million new cases and about 10 million fatal cases have occurred due to cancer onset worldwide [3]. In western countries, more than 65% of all the cancers occur upon exposure to numerous harmful substances, such as those present in western-style diet, alcohol, and smoking, that do not exist naturally in the environment [4].

Nutrition can also cause oxidative stress, augment a cascade of molecular reactions in cells, and alter the metabolic state of tissues [5]. Oxidative metabolism and redox homeostasis are suggested to be an essential part of aerobic life [6]. Living organisms cannot survive without these processes. Under such unfavorable conditions, oxygen derivatives can damage nucleic acids, lipids, and proteins; alter oxidative equilibrium; and regulate cell viability [7]. Oxidative stress induces the formation of excess antioxidants to protect the human body from antioxidant deficiency [8]. Moreover, nutrition can induce oxidative stress even in normal physiological conditions in the human body, and dietary factors can also serve as inflammatory and pro-oxidant factors [9]. Thus, nutritional oxidative stress might be described as a postprandial imbalance between the antioxidant defense and the pro-oxidant load as a consequence of inadequate or excess supply of nutrients [10].

Oxidative stress is known as a physiological state in which high levels of reactive oxygen species (ROS) and free radicals are generated due to antioxidant metabolism [11]. Normal cellular metabolism produces ROS and free radicals and plays a crucial role in cell signaling pathways [12]. Mechanically, mitochondria, the largest powerhouse of cells, generate ROS when generating adenosine triphosphate (ATP), whereby electrons react with oxygen (O2) and subsequently form the superoxide anion (O2) [13]. There are several studies confirming that oxidative stress may have a core relationship with human pathophysiological diseases [14,15,16]. Specifically, oxidative stress is prominently known to damage the DNA molecule, alter signaling pathways, and regulate progression of various cancers, including those of the breast, lung, liver, colon, prostate, ovary, and brain [17,18,19,20,21,22,23]. Moreover, it is reported that the whole DNA molecule can bind with hydroxyl radicals, and consequently, damage the deoxyribose backbone, including purine and pyrimidine bases. During these damaging processes, 8-OH deoxyguanosine (8-OHdG) can be produced, which may markedly increase the risk of mutagenesis [24]. The 8-OHdG molecules are also used as indicators to detect free radicals during DNA mutagenesis and are widely implicated as an early detection tool for cancer progression [24,25]. Importantly, 8-OHdG can transform GC pairs to TA pairs upon DNA replication, which might induce mutagenesis if oxidative lesions exist, subsequently causing cancer initiation [26].

The precise mechanisms underlying induction of oxidative stress by nutrition followed by cancer initiation are the current research topics, and the probable mechanisms include alterations in epigenetic events and induction of genomic instability, which alter gene expression, cause resistance to apoptosis, and induce tumor invasion and metastasis [12,14,15,16,24,26]. Therefore, in this review, we have provided an overview of the correlation between nutrition, oxidative stress, and carcinogenesis.

2. Correlation between Nutrition and Oxidative Stress

It is known that overnutrition may generate free radicals, and subsequently elevate oxidative stress [27] and ROS-mediated modulation of various molecular pathways [28,29,30]; therefore, scientists have directed increasing attention towards investigation of the function of oxidative stress in various pathophysiological diseases and normal body metabolism [16,31,32,33,34,35]. Therefore, the antioxidant capability of the human body is considered a crucial factor for overcoming free radical-mediated oxidative stress and the subsequent pathophysiological processes.

2.1. Nutrition Induces Oxidative Stress during Early Human Development

There are various crucial environmental factors, including nutrition, involved in epigenetic modifications [36]. For instance, undernutrition or malnutrition and low birth weight in utero due to early infant growth deficiency may be closely linked to risk factors, such as insulin resistance, obesity, reproductive dysregulation, and cardiovascular disease, in adulthood [37,38]. Similarly, offspring grown in a prenatally rich nutritional circumstance is at an increased risk of compromised fertility and cardiometabolic disorders later in life [39,40]. A recent study proposed that oxidative stress has a potent effect in nutrition-mediated epigenetic changes in various experimental models [41].

Obesity, maternal malnutrition, or obesogenic maternal diet upon gestation, but not in the post-weaning period [42], is associated with augmented oxidative stress markers and diminished antioxidant capability in the offspring, resulting in diabetogenic effects [43,44]. Concurrently, antioxidant supplementation could significantly attenuate obesity in their offspring [45]. Nutrition may trigger epigenetic changes in perinatal development into adulthood via different pathways, such as metabolic risk factor progression and oxidative stress generation.

2.2. Nutrition Triggers Oxidative Stress at the Cellular Level

A previous study demonstrated that after glucose intake, mononuclear (MNC) and polymorphonuclear (PMN) leukocytes of normal subjects generate ROS and induce inflammation due to excess micronutrients [46]. Similarly, after lipid intake, leukocytes in normal subjects may also significantly induce ROS generation and inflammation; protein intake can trigger ROS generation, but to a much lesser degree than glucose and lipid intake can [47]. Moreover, upon assessing a mixed meal in well-fit subjects, severe inflammatory alterations were identified, with a reduction in inhibitor κBα (IκBα), and upregulation of binding of nuclear factor κB (NF-κB) and expression of inhibitory proteins p47phox subunit, IκB kinase α (IKKα), IκB kinase β (IKKβ), and plasma C-reactive protein (CRP) [48].

Postprandial oxidative stress might increase due to excessive caloric intake, which abnormally increases blood glucose, free fatty acids (FFA), and triglycerides circulating in the blood. These high concentrations of FFA and glucose outpace the entire capability of mitochondria for oxidative phosphorylation, ultimately leading to improved transfer from single electrons to molecular oxygen; consequently, O2 enters the circulation [49,50]. Besides mitochondria, ROS production by leukocytes is also induced by the caloric amount, as previous studies indicated that caloric limit led to a decent reduction in ROS production via lipid peroxidation and protein carboxylation [51,52,53].

Inappropriate lifestyle patterns of an individual, including physical inactivity or obesity, can also cause ROS production in the postprandial state. As a result, obese individuals experience pernicious and acute oxidative stress after a fatty meal, compared to responses of the non-obese well-fitted individuals [54]. Inconsistent data exist regarding the outcome of exercise in postprandial oxidative stress. Although exercise is thought as a tool to increase endogenous antioxidant defenses, numerous researchers have been unsuccessful in showing a positive effect of physical activity on postprandial oxidative stress [55,56,57].

Cooking method can also have a postprandial impact on oxidative metabolism. Protein- and fat-rich food cooked quickly under high temperatures lead to the formation of dietary advanced glycation end products (AGEs) [58]. Studies showed that a single oral challenge by AGEs (coke) caused severe postprandial endothelial dysfunction, as illustrated by a significant reduction in flow-mediated dilatation both in diabetic and in healthy subjects [59]. Nutritive AGEs appear to affect reproductively challenged women as well. A study in women with polycystic ovarian syndrome (PCOS) showed that low-AGE meals in combination with six-month treatment with orlistat (a lipase inhibitor) led to a significant improvement of their hormonal profile and body mass index (BMI) [60].

Taken together, increasing evidence demonstrates that nutrition triggers major oxidative and inflammatory imbalances in the postprandial state. Indeed, postprandial hyperlipidemia and hyperglycemia, or so-called postprandial dysfunction in the body, are gradually gaining vital consideration as major risk factors for some diseases. Continuous accumulation of all these imbalances during the constant postprandial state that symbolizes current lifestyles may contribute to the pathophysiology of reproductive and metabolic disorders (Figure 1).

Figure 1
Overnutrition and decreased physical activity lead to overloaded glucose and free fatty acid (FFA) levels in cells. Their conversion into energy is supplemented by augmented free radical generation (oxidative stress). The muscle adipocytes can defend ...

2.3. Nutrition Increases Oxidative Stress during Tissue Metabolism

Nutrient consumption elicits a major oxidative and inflammatory effect at the cellular level, which alters tissue metabolism. Nutritional oxidative stress after carbohydrate, protein, and lipid intake results in a domino of metabolic alterations in various tissues, including the liver, adipose tissue, pancreatic β-cells, and skeletal muscle. These active but metabolically distressed tissues interacting with nutrients further augment oxidative stress, eventually resulting in an infinite vicious cycle (Figure 2).

Figure 2
Nutrition mediates oxidative stress at the metabolic tissue level. Dietary fat (lipids) induces intracellular lipid accumulation in the liver and subsequently causes the inflammatory response and ER stress, which ultimately results in oxidative stress- ...

2.3.1. Liver

Dietary fat intake or overfeeding augments free fatty acid (FFA) supply in the liver, which can affect liver metabolism by the accumulation of intracellular lipids. In the liver tissue, increased malonyl-CoA levels stimulate de novo FA production and prevent carnitine palmitoyltransferase-1 (CPT-1) function. Consequently, fatty acids (FAs) cannot be broken down in the mitochondria and are diverted to other metabolic pathways, resulting in the formation of ceramides, diacylglycerol (DAG), and triacylglycerol (TAG) [61]. In a rat model, fat-rich meal administration for only three days led to a three-fold increase in liver lipid accumulation, without any significant growth in the skeletal muscle or visceral fat content, suggesting that liver insulin resistance may precede systemic insulin resistance (Figure 2) [62]. As stated above, these lipids recruit numerous inflammatory factors that derestrict insulin signaling, including the c-Jun N-terminal kinase (JNK) and protein kinase C (PKC) pathways. Additionally, in an investigational model, FFA-containing cultured hepatocytes exhibited augmented levels of prothrombotic and oxidative markers, such as nitric oxide (NO), plasminogen activator inhibitor-1 (PAI-1), and malondialdehyde (MDA) [63]. Concurrently, massive substrate supply and liver overfeeding expose the ER to a substantial anabolic load that accordingly stimulates ER stress and protein misfolding, which can induce inflammatory signaling activation and ROS generation (Figure 2) [61]. Lastly, lipid accumulation in the hepatic cells affects hepatic glucose production in impaired insulin-mediated suppression and hyperlipidemia, categorized by elevated hepatic clearance of high-density lipoprotein (HDL)-cholesterol combined with elevated secretion of very low-density lipoproteins (VLDL) [64].

2.3.2. Adipose Tissue

In the adipose tissue, ROS production and oxidative metabolism play major roles in adipogenesis [65]. Various sources are involved in producing intracellular ROS in adipocytes. Although adipocytes are not thought to be pure energy-producing cells, ROS may be generated from electron transport chain (ETC) substrate overload as well as from mitochondria [66]. Moreover, several enzymes can induce ROS generation in adipocytes, including nicotinamide adenine dinucleotide phosphate (NADPH) oxidase. In adipocytes, NADPH oxidase 4 (NOX4) is the core isoform and its expression is augmented in the fat cells upon exposure to enriched nutrient derivatives, including glucose or palmitate [67]. Knockdown of NOX4 in adipocytes (3T3-L1 cells) prevented glucose- and palmitate-stimulated ROS production, indicating the significance of non-mitochondrial ROS in adipocytes [68].

Upon intake of a meal, an inflammatory response occurs in the adipose tissue [69]. A study conducted on rat visceral adipose tissue showed that rats fed with a fatty meal showed an acute postprandial stimulation of inflammatory signaling [70]. Similarly, in humans, 6 h after the feeding of a mixed meal, a similar upregulation of MCP-1 and IL-6 was noted within the adipose tissue in normal-weight, overweight, and obese subjects, independent of the grade of adiposity (Figure 2) [71]. In addition, the change in postprandial inflammatory effects in the adipose tissue due to the specific quantity and quality of dietary fat was studied by various scientific groups, but their results are conflicting. A study involving 75 subjects with metabolic syndrome revealed that as compared to long-term ingestion of saturated fat diet, that of high-monounsaturated fat diet led to a weakened postprandial inflammatory effect in the adipose tissue [72], whereas another study indicated that individuals with metabolic syndrome displayed impaired postprandial adipose tissue inflammation, regardless of the quantity and the quality of fat ingested [73]. From the direct stimulation of inflammatory pathways by nutrient consumption, a high-fat diet may prompt native inflammation in the adipose tissue through the discharge of unnecessary FFAs. The responses of FFAs in the inflammatory pathways are facilitated through the Toll-like receptor (TLR-4), which further induces the secretion of different cytokines and macrophage aggregation in the adipose tissue (Figure 2) [74].

Overall, oxidative stress can also be identified postprandially in adipocytes. In cultured adipocytes, elevated FFA levels augmented oxidative stress via NADPH oxidase stimulation, and oxidative stress directly caused dysfunctional secretion of adipokines. Additionally, increased ROS generation caused by increased expression of NADPH oxidase and decreased expression of antioxidative enzymes was investigated in the adipose tissue of overweight mice [75]. Thus, nutrition-activated oxidative stress likely leads to a contrary native redox status that could affect the role of free radicals in the adipose tissue (Figure 2) [76].

2.3.3. Pancreas

Oxidative stress can also likely compromise pancreatic β-cell function, as β-cells are inherently sensitive to oxidative stress. In a previous study, β-cells exposed to H2O2 generated cyclin- and p21-dependent kinase inhibitors and downregulated insulin mRNA, calcium flux, and ATP reduction in the cytosol and mitochondria [77]. Moreover, β-cells express low levels of antioxidant enzymes, such as catalase, superoxide dismutase (SOD), and glutathione peroxidase, and are more sensitive to detrimental ROS actions [78]. Hence, oxidative stress, induced by elevated FFA and glucose levels, insulin resistance, and long-term inflammation through the above-stated mechanisms, clearly plays a role in pancreatic cells and alters insulin secretion (Figure 2) [16].

In patients with diabetes, long-term induction of plasma FFA and glucose levels has damaging effects on the pancreatic cell function [16]. An in vitro study showed that the islets or HIT-T15 cells cultured in high concentrations of FFA and glucose exhibited reduced levels of insulin mRNA and gene function and altered glucose-induced insulin secretion pathway [79]. Aberrant free radical production and oxidative stress could be one of the crucial mechanisms underlying these instabilities (Figure 2). Moreover, hyperglycemia by itself can augment intracellular mitochondrial ROS generation in pancreatic β-cells, triggering a native oxidative microenvironment, which incidentally alters several metabolic signaling pathways that further intensify oxidative stress [80], including long-term low-grade AGE and inflammation generation, consequently collapsing β-cell function (Figure 2) [81].

2.3.4. Skeletal Muscle

Regarding metabolic circulation, the skeletal muscle can also be characterized as a pathway controller. This tissue represents a crucial source of energy generation and accounts for approximately 80% of the postprandial insulin-induced glucose dumping [82]. As a pure energy-generating organ, skeletal muscle is packed with mitochondria that control energy homeostasis.

After nutrient feeding, insulin induces glucose entry in the skeletal muscle through glucose transporter type 4 (GLUT4) [83]. This is a cardinal phase in the body’s metabolic pathways as fuel consumption should be attuned to fuel obtainability. The capability of skeletal muscle to mainly shift from lipid oxidation and high amounts of FA utilization in fasting situations to glucose ingestion, oxidation, and storage under insulin-prompted circumstances is recognized as metabolic flexibility. The inability to shift from lipid to carbohydrate use (metabolic inflexibility) was investigated in obese patients and is accompanied with intra-myocellular lipid aggregation and insulin resistance (Figure 2) [84]. Numerous factors regulate the metabolic flexibility of a subject, including nutrient presence, plasma FFA levels, the accessibility of the adipose tissue for lipid storage, and their level of physical activity [85]. Another factor that may be associated with metabolic flexibility is mitochondrial oxidative capability. Although a study showed contradictory data, it was suggested that mitochondrial aberrations in the muscle could stimulate metabolic flexibility to lipids and prompt insulin resistance (Figure 2) [85].

In the skeletal muscle, dietary habits may also disturb physiological metabolic developments and their role through direct changes in the mitochondrial biology [86]. Together, increased dietary fat and overfeeding appeared to induce mitochondrial inactivity, with declined ATP synthesis, altered mitochondrial gene expression, and augmented ROS generation. Consequently, a vicious cycle occurs as these mitochondrial dysfunctions further intensify the metabolic abnormalities of the skeletal muscle (Figure 2).

2.4. Nutrition Induces Oxidative Homeostasis

Nutrition-stimulated inflammatory and oxidative status in severe settings can alter extracellular and intracellular physiological activities. When these instabilities are recurrent, they execute a persistent inflammatory and oxidative response, which, in some cases, can prompt multiple diseases.

Limited-calorie dietary patterns can provoke the precise reverse effect, promoting cell longevity and securing oxidative balance. For instance, six months of caloric limitation significantly diminished oxidative stress and declined fasting insulin levels and body core temperature in healthy subjects [87]. Moreover, the study showed improved basal endothelial function and augmented plasma antioxidant capability in patients with diabetes, who followed a Mediterranean diet for three months in comparison with those patients on control diets [88].

Overall, evidence suggests that diet regulates oxidative stability both in an acute and in a chronic state. Nutritional variance can easily interrupt this cellular stability, initiate unfavorable pathophysiological pathways, and stimulate the incidence of numerous diseases in humans.

3. The Relationship between Nutrition and Oxidative Stress Following Carcinogenesis

The worldwide cancer burden is anticipated to increase by more than two-fold over the next two decades [89], therefore worsening a massive public health and medical care problem. Physical activity, nutrition, and diet rank high among the most important risk factors for human cancer, in part because of their influences on obesity, which is a recognized risk factor for various malignancies [90,91,92,93,94,95]. The role of some specific nutrients in cancer etiology has been proposed based on associations stated in epidemiological studies, further supported by biological credibility. The ultimate carcinogen is known as chemically reactive and activated form of a pro-carcinogen or carcinogen that is capable of a direct covalent binding to protein and/or nucleic acid macromolecules. The ultimate carcinogen directly binds with a cell component (probably DNA) to initiate carcinogenesis. These factors are linked to the antioxidant status of selected nutrients, impact on epigenetic functions, DNA adducts, DNA repair, regulation of gene expression, inflammation, stimulation of growth factors, or influence on circulating intensities of endogenous hormones (Figure 3) [96,97,98]. Incessant exposure to environmental carcinogens and inhalation chemicals is assumed to induce the amount of cytochrome P450 CYP1A1 expression in extrahepatic tissues via the aryl hydrocarbon receptor (AhR) [99,100,101,102]. Though the latter has long been identified as a ligand-activated transcription factor (TF), which is accountable for the xenobiotic inducing pathway of numerous phase I and phase II metabolizing enzymes, recent studies propose that AhR is associated with several cell signaling pathways critical to cell cycle modulation and normal homeostasis [101,102]. Alteration of these pathways is associated with tumor progression. Moreover, it is increasingly evident that P450 plays a vital role in the detoxification of environmental carcinogens, following the metabolic activation of dietary compounds (nutrition) with cancer preventative activity (Figure 3) [102]. Along with other crucial factors, such as diet, energy balance, BMI, physical activity, and metabolic rate, nutrition may also influence DNA replication of cancer cells following cancer progression. Therefore, nutrition-mediated oxidative stress plays a crucial role in carcinogenesis. Some of the vital dietary components that have an association with oxidative stress following different aspects of carcinogenesis have been discussed in this section (Table 1 and Figure 4).

Figure 3
Nutrition as a mediator of cancer suppression at the molecular level. A chemically reactive and activated form of pro-carcinogen or carcinogen (ultimate carcinogen) is capable of direct covalent binding to protein and/or nucleic acid macromolecules. It ...
Figure 4
Some vital dietary factors have been associated with various aspects of cancer progression. Arrows represent activation of cancer and T bar represent inhibition.
Table 1
The role of various dietary components in oxidative stress and carcinogenesis.

3.1. Alcohol

Alcohol is a prominent carcinogen linked with breast, oropharyngeal, colorectal, liver, and esophageal cancers [103]. Excessive consumption of alcohol also leads to fibrotic changes in the liver [104,105]. Moreover, it leads to the production of ROS following oxidative stress, which, consequently, causes severe dysfunction and damage to the biological signaling molecules [106]. Additionally, it disrupts intra- and extra-cellular network and functions, which ultimately cause chromosomal abnormalities, DNA damage, DNA methylation modification, signaling pathway alteration, tumor necrosis factor α (TNF-α) release, and retinoid metabolism impairment, consequently, leading to cancer initiation [107,108,109,110]. Functional diversity in the genes associated with alcohol metabolism can result in varying exposure to the carcinogenic metabolites of alcohol; therefore, identifying genetic intolerance to alcohol can aid in cancer prognosis [111]. For instance, people with a common genetic mutation in the alcohol dehydrogenase gene that suppresses enzyme activity have a higher risk of esophageal cancer than those who have a fully active enzyme [103]. Alcohol facilitates its mutagenic effects by the derivation of acetaldehyde adducts, induction of the activity of Kupffer cells, and enhancing oxidative stress by augmenting formation of gut-derived endotoxins [110]. Alcoholism results in accumulation of acetaldehyde, which, consequently, causes genotoxicity. A similar change occurs due to accumulated acetaldehyde in hepatocellular carcinoma [112,113]. Moreover, according to World Cancer Research Fund (WCRF) analysis, alcohol intake is significantly correlated with increased breast cancer risk [90]. Numerous epidemiological studies supported a positive interaction between breast cancer risk and alcohol [114]. A meta-analysis revealed that high alcohol consumption (10 g of ethanol consumption per day) was highly associated with risks for ER+PR+, ER+PR, ER+, and ER breast tumors, but not ERPR tumors [115]. Additionally, there are several contradictory studies on the probable relationship of alcohol consumption with numerous histological grades or stages of prostate cancer [116,117,118,119,120]. Previous meta-analyses have also emphasized these irregularities, highlighting the necessity for further studies in this area [121,122].

3.2. Carbohydrates

Ingestion of nutritional carbohydrate, a key dietary factor, disturbs an individual’s glycemic response and insulin secretion, while consequences differ depending on the amount of carbohydrates consumed [167]. Carbohydrate quality could affect cancer risk, especially, that of breast cancer, significantly by influencing plasma levels of glucose and insulin, and insulin resistance [130]. Recent meta-analysis studies described a potential relationship between glycemic index (GI), degree of cancer risk, and intake of carbohydrate quality [168,169,170,171]. Previous studies suggest that oxidative stress may have an important role connecting acute hyperglycemia to augmented cardiovascular risk [172,173,174]. Acute enhancement in blood glucose concentrations may increase the formation of free radicals by an imbalance in the ratio of NADH to NAD and by non-enzymatic glycation increased by glucose in cells [175,176]. The direct indication from studies presented that enhanced hyperglycemia or meal consumption and its derived glucose can promote oxidative stress and impair antioxidant defenses [177,178]. Consequently, oxidative stress was significantly augmented after food intake that produced a superior degree of hyperglycemia in both normal subjects and those with diabetes [179]. According to the European Prospective Investigation into Cancer and Nutrition (EPIC), increased carbohydrate and glycemic burden in the food were associated with an increase in ER/PR and ER breast cancer among older women [180]. Similarly, the Women’s Health Initiative (WHI) suggested that consuming foods with high insulinogenic content may increase the risk of breast cancer [131]. Together, the potential relationship between cancer risk and dietary GI was more commonly stated by case-controls than by the cohort studies. A probable purpose for this is that case-control reports are more liable to problems of remembering and selection difficulty than cohort studies are. In addition, most case-control studies were conducted in Europe and most cohort studies were conducted in North America. The diverse results between studies performed in North Americans and Europeans may also reveal variances in nutritional lifestyles between the two regions. Individuals from Europe ingest carbohydrate-enriched food and different kinds of carbohydrates [181] compared to individuals in North America [182], who consistently consume more fats. Studies are often unable to demonstrate a relationship between oxidative stress-induced cancer risk and carbohydrate intake.

3.3. Fatty acids (FAs)

Dietary lipids or fats are frequently blamed as the key source of superfluous energy. When caloric consumption surpasses energy expenses, the resultant substrate-induced enhancement in citric acid cycle activity produces an excess of ROS. Moreover, dietary FA ingestion influences the relative FA configuration of biological membranes defining its sensibility to oxidative changes [183]. There are huge controversies around finding a relationship between FA-rich meals and cancer risk in population-based reports, despite a solid biological credibility underlying these relationships. The role of inflammation in membrane fluidity and functions, stimulation of growth factors, and regulation of gene expression, or its effect on circulating levels of endogenous hormones has been cited. Recent data demonstrate a link between dietary FA with induced oxidative stress and carcinogenesis in the rat model [184]. Several epidemiological studies mention that, rather than total dietary fat ingestion, subgroups of FAs could differentially affect cancer risk [185,186,187,188]. Essential FAs (EFAs) of the omega-3 family (α-linolenic acid, docosahexaenoic acid (DHA), and eicosapentaenoic acid (EPA)) and omega-6 family (arachidonic acid and linoleic acid) have been a vast subject of study, because of their dietary significance and their association with the prognosis of various types of cancers. In spite of numerous studies conducted over the last decades, recent scientific data are debatable and there is a lack of reliable conclusions about the effect of EFAs and the risk of breast, bladder, colorectal, lung, or prostate cancers [189,190,191,192]. In the broad literature regarding this type of EFA (omega-3, omega-6, and omega-3/omega-6 ratio) and its relationship to cancer progression, several underlying mechanisms have been hypothesized. One of the most established mechanisms is an association between inflammatory pathways and the function of omega-3 and omega-6 FAs on the action of cyclooxygenase-2 (COX-2) in prostate cancer [134,135,136]. On the contrary, Gao et al. [193] demonstrated that palmitate, a saturated FA, up-regulated COX-2 via NF-κB-dependent mechanism; consequently, COX-2-associated oxidative stress weakened endothelium-dependent relaxations in the mouse aortas. However, metabolic characteristics of these EFAs are completely conflicting. The COX-2 enzyme can convert omega-6 FAs into prostaglandin E2, a pro-inflammatory cytokine, which enables angiogenesis and cell proliferation, whereas prostaglandin E3 is produced from omega-3 FAs with the help of COX-2, which does not facilitate mitogenic characteristics [194].

This proposal could elucidate the results achieved by assessing the impact of the omega-3/omega-6 ratio on melanoma [195], and the effects of DHA- and EPA-rich fish oil on colorectal [196] or prostate cancer, where the diversity of results leads to contradictory conclusions [197,198].

3.4. Fiber

Consumption of whole grain cereals, vegetables, and fruits provides the fibers necessary for our health, with the recommended intake being approximately 21–38 g/day. The protective action of fibers is not only associated with colorectal cancer, but also with other cancer types. A study showed an 11% decrease in breast cancer risk in individuals consuming a fiber-rich diet versus that in individuals consuming the lowest amount of fiber [142]. This association is dose-dependent; cancer risk decreased 7% with each 10 g/day of fiber intake, which is not dependent on the ethnic group, region, or menopausal status [142]. Moreover, the WCRF assessment board concluded an inadequate level of data regarding the relationship between dietary fiber and breast cancer risk [90]. Similarly, an organized review and meta-analysis of potential studies presented a significant inverse relationship between nutritional fiber intake and breast cancer risk [143]. In addition, the recent epidemiological proof is not convincing regarding the ability of fiber intake to decrease colorectal cancer risk. Some studies have shown significant results, with up to a 25% reduction in cancer risk by ingesting around 12.6–33.1 g/day of fiber, or 17% reduction by consuming fiber three times a day, though some studies have not found any beneficial effects [144,199].

3.5. Flavonoids

Cancer initiation and progression have been associated with oxidative stress by enhancing DNA mutations or increasing DNA damage, genome variability, and cell proliferation, and hence antioxidant agents could intervene with carcinogenesis [200]. Among the antioxidant compounds, isoflavones are the most well-known compounds that possess well-characterized anti-estrogenic activity (antagonistic for the β-estrogen receptor); functions in intracellular steroid metabolism (inhibiting the enzyme that transforms androgen to estrogen); and anti-angiogenic, anti-proliferative, and pro-apoptotic activities in various tumor cells [149,150,151]. Other flavonoid compounds, polyphenols, have anticancer activity both in humans and animal models [201,202]. Currently, increasing attention is directed towards the role of natural antioxidant agents on modulating intracellular ROS levels resulting into epigenetic alterations of essential genes in tumorigenesis [202]. Several flavonoids were confirmed to disrupt the enzymes leading to epigenetic modifications, which regulate the inflammation process that might oscillate in cancer [202]. Excessive ROS generation may lead to tissue injury that may induce inflammatory process [203], the inflammatory mediators may be involved in various chronic diseases, including CVD, neurological disease, and carcinogenesis [204]. Although in vitro studies depict a positive outcome, case-control results and phase III clinical trials afford unconvincing data for certain kinds of tumors, such as breast or prostate neoplasms [151,205]. A study on Asian women revealed that isoflavone consumption of 20 mg/day can decrease breast cancer risk by 29% as compared to that after consumption of 5 mg/day [152]. On the contrary, according to a meta-analysis, no association was found in western women, even though these women ingested 0.8 mg of isoflavones per day [151]. Previously, studies have stated that Asian men consume high amounts of isoflavone-containing foods, while western counterparts consume mostly red meat-containing foods with minimal isoflavones [206,207,208]. This variation in results can be caused by numerous factors, including dose and type of isoflavones, type of cancer, or even diverse enzymatic polymorphisms between subjects [209].

3.6. Proteins

In a nutritional diet, protein is the most important element for human health. Proteins contain no nutritional value until they are digested by protease and peptidase enzymes. Excessive protein consumption can induce amino acid oxidation and urea synthesis [210], and impair the nutritional efficacy of energy utilization [211]. An interesting study stated that high protein intake could obliterate the stability of antioxidants and oxidation of amino acids in the digestive system of mice and promote generation of ROS in the digestive gland [212]. A conceivable explanation is that ROS might be generated after meat consumption during its metabolism [213]. Moreover, high-protein ingestion can result in oxidative stress, inducing risk for long-term diseases, including carcinogenesis [214,215,216]. In patients with cancer, protein consumption is decreased tremendously due to reduced digestion, low food intake, and augmented catabolism [217]. Recently, an epidemiological study showed that intake of protein-rich food (especially animal protein) could be associated with a higher risk of cancer [157]. Moreover, a few epidemiological studies have discovered an association between intake of animal protein (e.g., red meats) and several diseases (e.g., hypertension and colon cancer) [218,219]. There are no particular enduring clinical trials analyzing meatless diets for children or adults. Similarly, there is little evidence indicating that colorectal cancer progression occurs upon satisfactory consumption of animal protein [158]. Recent studies from large cohorts, such as the Health Professional Follow-up Study, the Nurse’s Health Study, and the Multiethnic Cohort, depicted insignificant or inverse correlations between ingestion of unrefined red meat and colon cancer [218,220]. Together, research from the interference studies on cancer and diet, including the Polyp Prevention Trial and the Women’s Health Initiative, found that a reduction in dietary consumption of animal protein (e.g., processed meat and red meat) did not decrease the risk of colon cancer and/or had no outcome on adenoma relapse in the large bowel [221,222,223].

3.7. Vitamins

Recent epidemiological studies have been conducted to discover the association between vitamin consumption and the risk of cancer diagnosis. According to previous studies, numerous vitamins, including vitamin A, B, C, D, and E, have been implicated in the risk of cancer occurrence [161,162,163,164,165]. Vitamins C, D, and E and selenium share fundamental antioxidant properties and all protect against oxidative stress and its harmful effects in our body that lead to carcinogenesis. However, oxidative stress is a natural process with positive outcomes, such as improved immune response [224]. Previous studies stated that high-dose vitamin C killed cancer cells by playing a role as a pro-drug, which provides hydrogen peroxide (H2O2) [225,226,227]. Vitamin C-induced elevated levels of ROS, including H2O2, are considered to play a vital role in carcinogenesis [226]. Previous studies also reported that vitamin C administration promoted cytotoxicity by ATP reduction in some cancer cells [227,228,229]. A case-control study involving women from Klang Valley and Selangor, Malaysia, demonstrated that a good antioxidant consumption, including vitamins A and E, can reduce oxidative stress and subsequently prevent breast cancer risk [230]. The relationships between breast cancer and B vitamins have been broadly studied and these relationships are complex. From questionnaires, epidemiological studies have estimated an association between folate consumption and the risk of breast cancer with conflicting results [231]. On the contrary, preventive effects have been witnessed in individuals with low folate consumption and occasional vitamin intake [232]. Moreover, there are questionable findings for vitamin B in prostate cancer [233], for vitamins C and E in liver [234] and prostate cancers [235], and for folic acid and vitamin D in pancreatic cancer [236,237].

4. The Association between Oxidative Stress and Cancer Progression

An association between oxidative stress and cellular alteration was first recognized in 1981 when it was identified that insulin raised intracellular H2O2 levels and augmented tumor cell proliferation [238]. After more than three decades, the function of ROS in cancer progression remains conflicting. Oxidative stress is involved in various diseases, including neurodegenerative diseases [239,240], chronic inflammation [241,242], metabolic disorders [243,244], and extensively in various cancers [245,246,247,248,249]. The rise in ROS levels from oxidative stress, as a consequence of oncogene signaling pathways, may exploit underlying mutagenesis and genomic variability in cancer cells to stimulate cancer progression. Cancer cells require high levels of ATP because it acts as “fuel” for aberrant cell proliferation. However, the effect of this excess energy generation is the accumulation of ROS, which needs to be prevented by scavenging actions to ensure cell survival [250]. To prevent these possibly toxic effects of ROS, numerous oncogenes also augment the expression of nuclear factor erythroid 2-related factor 2 (NRF2), which diminishes ROS levels and stimulates tumorigenesis [251]. Similarly, NRF2 not only offers protection against chemical carcinogens, but also augments cancer progression by defending cancer cells from ROS and DNA damage [252,253,254,255,256,257,258]. In contrast, NRF2 deletion in pancreatic cancer cells augmented DNA damage and inhibited carcinogenesis [251].

Several studies have assessed ROS levels and generation under numerous conditions with the aim of determining when ROS are carcinogenic and when they are cancer suppressive [259]. At low or endurable levels, ROS may aid cancer progression either by playing as signaling elements or by stimulating alterations in genomic DNA or DNA damage. For example, ROS can promote expression of cyclin D1, phosphorylation of extracellular signal-regulated kinase (ERK) and JUN N-terminal kinase (JNK), and activation of mitogen-activated protein kinase (MAPK), all of which are connected to cancer progression and survival [260,261,262,263,264,265]. Moreover, ROS have been found to inversely incapacitate tumor suppressors, including protein tyrosine phosphatases (PTPs) and phosphatase and tensin homolog (PTEN), due to the existence of the redox-sensitive cysteine residues that exist in their catalytic sites [266,267,268]. Remarkably, PTPs can also control signaling pathways to induce the expression of antioxidant enzymes and diminish ROS levels [269]. Additionally, normal stem cell renewal and differentiation are controlled by ROS levels [270]; while cancer stem cells (CSCs) share similar properties with normal stem cells, comparatively little is known regarding their association with redox status. Recently, studies have shown that the liver and breast cancer stem cells tend to have low ROS levels, leading to the augmented expression of ROS-scavenging signaling proteins [270]. If CSC growth is vital for tumor initiation, then retaining low ROS levels in CSCs may be essential for the endurance of pre-neoplastic foci. Hence, although chemotherapy and radiotherapy prompt ROS generation, they are beneficial for abolishing most cancer cells, yet may be unable to cure the patient, leading to the greater capability of CSCs to endure in circumstances of high ROS by increasing antioxidants levels [250]. As ROS are debatable mediators of the adverse effects of some anticancer drugs and ionizing radiation, CSCs may be favorably released and aggressively selected by actions that depend on increased ROS levels. Furthermore, the supplementary oxidative stress prompted by these actions may cause further mutations and DNA damage, resulting in the expansion of drug-resistant cancer cells (Figure 5).

Figure 5
A schematic diagram of overall signaling pathways of cancer progression induced by oxidative stress. SOD: superoxide dismutases; Mito-ETC: mitochondrial electron transport chain, GSH: glutathione; GR: glutathione reductase; GPX: glutathione peroxidase; ...

At elevated levels, ROS stimulate cell death and harmful cellular damage. In this case, cancer cells must overcome increased levels of ROS, particularly at initial stages of cancer progression. A recent study found that circumstances that enhance oxidative stress also raise the specific pressure on pre-neoplastic cells to induce influential antioxidant mechanisms [271]. Increased levels of ROS are also prompted by dissipation from the cell matrix [272]. This feature is relevant during metastasis of cancer cells that need to survive upon migration to distant organs. Thus, cancer cells typically have a high antioxidant capability that controls ROS levels and are attuned with biological functions of the cell, but are quite higher than the antioxidant capacity of normal cells. Moreover, increased ROS levels by endogenous antioxidants are unfavorable to cancer cells as well as cancer progression. We consider that targeting these enriched antioxidant protective mechanisms may represent an approach that can precisely destroy cancer cells, including CSCs, while sparing normal cells.

5. Conclusions

In the human body, nutrition is one of the vital regulators of oxidative stress. Nutrient consumption and the associated postprandial oxidative stress result in the accumulation of molecular alterations in the crucial signaling pathways of several organs, critically changing the cellular milieu. However, the particular pathophysiological roles of oxidative stress and nutrition are still elusive, with targeted therapeutic modalities representing a puzzling field. Specifically, when the organs of the gastrointestinal (GI) tract are exposed to the highest amount of dietary associated carcinogens, the injurious effects of these components affect the whole body system. Over the past decades, extensive studies have revealed that alterations in the cell metabolism play a vital role in the progression of various types of cancer. In general, carcinogenesis as well as dietary carcinogen-associated carcinogenesis, is significantly correlated with chronic and/or acute oxidative stress. The precise nature of the effect of oxidative stress on cancer development and/or response to treatment requires further exploration. The association between nutrition and oxidative stress may have an important role in cancer and CSC progression as well as therapy. To validate and confirm all of these above-mentioned hypotheses, more detailed further investigations and research are required. Recently developed technologies, including metabolomics and deep DNA sequencing, are imperative tools that would support to define how the metabolism of cancer cells become accustomed and offers a buffer against augmented oxidative stress. However, the pathophysiological relationship between carcinogenesis and oxidative stress opens prospects for protective and even therapeutic use of beneficial, healthy dietary compounds indicated as nutraceuticals. Therefore, this review details our understanding of the correlation between nutrition, oxidative stress, and cancer development, and uncovers related crucial therapeutic strategies.

Acknowledgments

This paper was supported by Konkuk University in 2016.

Abbreviations

8-OHdG8-OH deoxyguanosine
AGEadvanced glycation end product
ATPadenosine triphosphate
BMIbody mass index
COX-2cyclooxygenase 2
CPT-1carnitine palmitoyltransferase-1
CRPC-reactive protein
CSCcancer stem cells
CVDcardiovascular disease
DAGdiacylglycerols
DHAdocosahexaenoic acid
EFAEssential fatty acids
EPAeicosapentaenoic acid
EPICEuropean Prospective Investigation into Cancer and Nutrition
ER:endoplasmic reticulum
ERKextracellular signal-regulated kinase
ETC:electron transport chain
FFAfree fatty acids
FoxO1Forkhead box protein O1
GIglycemic indexes
GLUT4glucose transporter type 4
GPXglutathione peroxidase
GRglutathione reductase
GRXoglutaredoxin (oxidized)
GRXrglutaredoxin (reduced)
GSHrglutathione (reduced)
HDLhigh-density lipoproteins
IARCInternational Agency for Research on Cancer
IGTimpaired glucose tolerance
IKKαIκB kinase α
IKKβIκB kinase β
IL- 6Interleukin 6
IκBαinhibitor κBα
JNKc-Jun N-terminal kinase
MAPKmitogen-activated protein kinase
MCP-1Monocyte chemoattractant protein-1
MDAmalondialdehyde
Mito-ETCmitochondrial electron transport chain
MNCmononuclear cells
NADPHnicotinamide adenine dinucleotide phosphate
NF-κBnuclear factor κB
NOnitric oxide
NOX4NADPH oxidase 4
NRF2nuclear factor erythroid 2-related factor 2
PAI-1plasminogen activator inhibitor-1
PCOSpolycystic ovarian syndrome
PKCprotein kinase C
PMNLpolymorphonuclear leukocytes
PTENphosphatase and tensin homolog
PTPprotein tyrosine phosphatase
ROSreactive oxygen species
SODsuperoxide dismutase
TAGtriacylglycerol
TLR4:Toll-like receptor 4
TRXothioredoxin (oxidized)
TRXrthioredoxin (reduced)
VLDLvery low-density lipoproteins
WCRFWorld Cancer Research Fund
WHIWomen’s Health Initiative
WHOWorld Health Organization

Author Contributions

Author Contributions

Subbroto Kumar Saha designed this work, collected the data, and co-wrote the manuscript. Soo Bin Lee, Jihye Won, Hye Yeon Choi, Kyeongseok Kim, Gwang-Mo Yang, and Ahmed Abdal Dayem collected the data and helped edit the manuscript. Ssang-goo Cho designed the work, collected and reorganized the data, and wrote and edited the manuscript.

Conflicts of Interest

Conflicts of Interest

The authors declare no conflict of interest.

References

1. Ferlay J., Soerjomataram I., Dikshit R., Eser S., Mathers C., Rebelo M., Parkin D.M., Forman D., Bray F. Cancer incidence and mortality worldwide: Sources, methods and major patterns in GLOBOCAN 2012. Int. J. Cancer. 2015;136:E359–E386. doi: 10.1002/ijc.29210. [PubMed] [Cross Ref]
2. Mosby T.T., Cosgrove M., Sarkardei S., Platt K.L., Kaina B. Nutrition in Adult and Childhood Cancer: Role of Carcinogens and Anti-carcinogens. Anticancer Res. 2012;32:4171–4192. [PubMed]
3. Torre L.A., Bray F., Siegel R.L., Ferlay J., Lortet-Tieulent J., Jemal A. Global Cancer Statistics, 2012. CA Cancer J. Clin. 2015;65:87–108. doi: 10.3322/caac.21262. [PubMed] [Cross Ref]
4. Troselj K.G., Gueraud F., Glavan T.M., Pierre F., Zarkovic N. Food Toxicology. CRC Press; Boca Raton, FL, USA: 2016. A Review on Food-Associated Carcinogenesis; pp. 35–56.
5. Diamanti-Kandarakis E., Papalou O., Kandaraki E.A., Kassi G. MECHANISMS IN ENDOCRINOLOGY Nutrition as a mediator of oxidative stress in metabolic and reproductive disorders in women. Eur. J. Endocrinol. 2017;176:R79–R99. doi: 10.1530/EJE-16-0616. [PubMed] [Cross Ref]
6. Commoner B., Townsend J., Pake G.E. Free radicals in biological materials. Nature. 1954;174:689–691. doi: 10.1038/174689a0. [PubMed] [Cross Ref]
7. Halliwell B. Reactive oxygen species in living systems: Source, biochemistry, and role in human disease. Am. J. Med. 1991;91:S14–S22. doi: 10.1016/0002-9343(91)90279-7. [PubMed] [Cross Ref]
8. Turrens J.F. Mitochondrial formation of reactive oxygen species. J. Physiol. 2003;552:335–344. doi: 10.1113/jphysiol.2003.049478. [PubMed] [Cross Ref]
9. Halliwell B. Oxidative stress, nutrition and health. Experimental strategies for optimization of nutritional antioxidant intake in humans. Free Radic. Res. 1996;25:57–74. doi: 10.3109/10715769609145656. [PubMed] [Cross Ref]
10. Sies H., Stahl W., Sevanian A. Nutritional, dietary and postprandial oxidative stress. J. Nutr. 2005;135:969–972. [PubMed]
11. Forcados G.E., Chinyere C.N., Shu M.L. Acalypha wilkesiana: Therapeutic and toxic potential. J. Med. Surg. Pathol. 2016;1:122.
12. Alpay M., Backman L.R.F., Cheng X.D., Dukel M., Kim W.J., Ai L.B., Brown K.D. Oxidative stress shapes breast cancer phenotype through chronic activation of ATM-dependent signaling. Breast Cancer Res. Treat. 2015;151:75–87. doi: 10.1007/s10549-015-3368-5. [PubMed] [Cross Ref]
13. Pisoschi A.M., Pop A. The role of antioxidants in the chemistry of oxidative stress: A review. Eur. J. Med. Chem. 2015;97:55–74. doi: 10.1016/j.ejmech.2015.04.040. [PubMed] [Cross Ref]
14. Dalle-Donne I., Rossi R., Colombo R., Giustarini D., Milzani A. Biomarkers of oxidative damage in human disease. Clin. Chem. 2006;52:601–623. doi: 10.1373/clinchem.2005.061408. [PubMed] [Cross Ref]
15. Agarwal A., Aponte-Mellado A., Premkumar B.J., Shaman A., Gupta S. The effects of oxidative stress on female reproduction: A review. Reprod. Biol. Endocrinol. 2012;10:49. doi: 10.1186/1477-7827-10-49. [PMC free article] [PubMed] [Cross Ref]
16. Tangvarasittichai S. Oxidative stress, insulin resistance, dyslipidemia and type 2 diabetes mellitus. World J. Diabetes. 2015;6:456–480. doi: 10.4239/wjd.v6.i3.456. [PMC free article] [PubMed] [Cross Ref]
17. Lee J.D., Cai Q., Shu X.O., Nechuta S.J. The role of biomarkers of oxidative stress in breast cancer risk and prognosis: A systematic review of the epidemiologic literature. J. Women’s Health. 2017;26:467–482. doi: 10.1089/jwh.2016.5973. [PubMed] [Cross Ref]
18. Zhang L., Li L., Gao G., Wei G., Zheng Y., Wang C., Gao N., Zhao Y., Deng J., Chen H. Elevation of GPRC5A expression in colorectal cancer promotes tumor progression through VNN-1 induced oxidative stress. Int. J. Cancer. 2017;140:2734–2747. doi: 10.1002/ijc.30698. [PubMed] [Cross Ref]
19. Saijo H., Hirohashi Y., Torigoe T., Horibe R., Takaya A., Murai A., Kubo T., Kajiwara T., Tanaka T., Shionoya Y., et al. Plasticity of lung cancer stem-like cells is regulated by the transcription factor HOXA5 that is induced by oxidative stress. Oncotarget. 2016;7:50043–50056. doi: 10.18632/oncotarget.10571. [PMC free article] [PubMed] [Cross Ref]
20. Wang Z.P., Li Z.N., Ye Y.S., Xie L.J., Li W. Oxidative stress and liver cancer: Etiology and therapeutic targets. Oxidative Med. Cell. Longev. 2016;2016:7891574. doi: 10.1155/2016/7891574. [PMC free article] [PubMed] [Cross Ref]
21. Oh B., Figtree G., Costa D., Eade T., Hruby G., Lim S., Elfiky A., Martine N., Rosenthal D., Clarke S., et al. Oxidative stress in prostate cancer patients: A systematic review of case control studies. Prostate Int. 2016;4:71–87. doi: 10.1016/j.prnil.2016.05.002. [PMC free article] [PubMed] [Cross Ref]
22. Saed G.M., Diamond M.P., Fletcher N.M. Updates of the role of oxidative stress in the pathogenesis of ovarian cancer. Gynecol. Oncol. 2017;145:595–602. doi: 10.1016/j.ygyno.2017.02.033. [PubMed] [Cross Ref]
23. Jaroonwitchawan T., Chaicharoenaudomrung N., Natnkaew J., Noisa P. Curcumin attenuates paraquat-induced cell death in human neuroblastoma cells through modulating oxidative stress and autophagy. Neurosci. Lett. 2017;636:40–47. doi: 10.1016/j.neulet.2016.10.050. [PubMed] [Cross Ref]
24. Forcados G.E., James D.B., Sallau A.B., Muhammad A., Mabeta P. Oxidative stress and carcinogenesis: Potential of phytochemicals in breast cancer therapy. Nutr. Cancer. 2017;69:365–374. doi: 10.1080/01635581.2017.1267777. [PubMed] [Cross Ref]
25. Matsui A., Ikeda T., Enomoto K., Hosoda K., Nakashima H., Omae K., Watanabe M., Hibi T., Kitajima M. Increased formation of oxidative DNA damage, 8-hydroxy-2′-deoxyguanosine, in human breast cancer tissue and its relationship to GSTP1 and COMT genotypes. Cancer Lett. 2000;151:87–95. doi: 10.1016/S0304-3835(99)00424-3. [PubMed] [Cross Ref]
26. Sova H., Jukkola-Vuorinen A., Puistola U., Kauppila S., Karihtala P. 8-Hydroxydeoxyguanosine: A new potential independent prognostic factor in breast cancer. Br. J. Cancer. 2010;102:1018–1023. doi: 10.1038/sj.bjc.6605565. [PMC free article] [PubMed] [Cross Ref]
27. Aldini G., Dalle-Donne I., Facino R.M., Milzani A., Carini M. Intervention strategies to inhibit protein carbonylation by lipoxidation-derived reactive carbonyls. Med. Res. Rev. 2007;27:817–868. doi: 10.1002/med.20073. [PubMed] [Cross Ref]
28. Skurk T., Alberti-Huber C., Herder C., Hauner H. Relationship between adipocyte size and adipokine expression and secretion. J. Clin. Endocrinol. Metab. 2007;92:1023–1033. doi: 10.1210/jc.2006-1055. [PubMed] [Cross Ref]
29. Montezano A.C., Dulak-Lis M., Tsiropoulou S., Harvey A., Briones A.M., Touyz R.M. Oxidative stress and human hypertension: Vascular mechanisms, biomarkers, and novel therapies. Can. J. Cardiol. 2015;31:631–641. doi: 10.1016/j.cjca.2015.02.008. [PubMed] [Cross Ref]
30. Wong W.T., Tian X.Y., Huang Y. Endothelial dysfunction in diabetes and hypertension: Cross talk in RAS, BMP4, and ROS-dependent COX-2-derived prostanoids. J. Cardiovasc. Pharmacol. 2013;61:204–214. doi: 10.1097/FJC.0b013e31827fe46e. [PubMed] [Cross Ref]
31. WHO Diet, nutrition and the prevention of chronic diseases; Proceedings of the WHO/FAO Expert Consultation on Diet, Nutrition and the Prevention of Chronic Diseases; Geneva, Switzerland. 28 January–1 February 2002.
32. Hernanz R., Briones A.M., Salaices M., Alonso M.J. New roles for old pathways? A circuitous relationship between reactive oxygen species and cyclo-oxygenase in hypertension. Clin. Sci. 2014;126:111–121. doi: 10.1042/CS20120651. [PubMed] [Cross Ref]
33. Ward N.C., Hodgson J.M., Puddey I.B., Mori T.A., Beilin L.J., Croft K.D. Oxidative stress in human hypertension: Association with antihypertensive treatment, gender, nutrition, and lifestyle. Free Radic. Biol. Med. 2004;36:226–232. doi: 10.1016/j.freeradbiomed.2003.10.021. [PubMed] [Cross Ref]
34. Houstis N., Rosen E.D., Lander E.S. Reactive oxygen species have a causal role in multiple forms of insulin resistance. Nature. 2006;440:944–948. doi: 10.1038/nature04634. [PubMed] [Cross Ref]
35. Hotamisligil G.S. Inflammation and metabolic disorders. Nature. 2006;444:860–867. doi: 10.1038/nature05485. [PubMed] [Cross Ref]
36. Lee H.-S. Impact of maternal diet on the epigenome during in utero life and the developmental programming of diseases in childhood and adulthood. Nutrients. 2015;7:9492–9507. doi: 10.3390/nu7115467. [PMC free article] [PubMed] [Cross Ref]
37. Barker D.J., Osmond C., Winter P., Margetts B., Simmonds S.J. Weight in infancy and death from ischaemic heart disease. Lancet. 1989;334:577–580. doi: 10.1016/S0140-6736(89)90710-1. [PubMed] [Cross Ref]
38. Barker D.J. Maternal nutrition, fetal nutrition, and disease in later life. Nutr. J. 1997;13:807–813. doi: 10.1016/S0899-9007(97)00193-7. [PubMed] [Cross Ref]
39. Armitage J.A., Taylor P.D., Poston L. Experimental models of developmental programming: Consequences of exposure to an energy rich diet during development. J. Physiol. 2005;565:3–8. doi: 10.1113/jphysiol.2004.079756. [PubMed] [Cross Ref]
40. Gamborg M., Byberg L., Rasmussen F., Andersen P.K., Baker J.L., Bengtsson C., Canoy D., Drøyvold W., Eriksson J.G., Forsén T. Birth weight and systolic blood pressure in adolescence and adulthood: Meta-regression analysis of sex-and age-specific results from 20 Nordic studies. Am. J. Epidemiol. 2007;166:634–645. doi: 10.1093/aje/kwm042. [PubMed] [Cross Ref]
41. Thompson L.P., Al-Hasan Y. Impact of oxidative stress in fetal programming. J. Pregnancy. 2012;2012:582748. doi: 10.1155/2012/582748. [PMC free article] [PubMed] [Cross Ref]
42. Aiken C.E., Tarry-Adkins J.L., Penfold N.C., Dearden L., Ozanne S.E. Decreased ovarian reserve, dysregulation of mitochondrial biogenesis, and increased lipid peroxidation in female mouse offspring exposed to an obesogenic maternal diet. FASEB J. 2016;30:1548–1556. doi: 10.1096/fj.15-280800. [PMC free article] [PubMed] [Cross Ref]
43. Saad M.I., Abdelkhalek T.M., Haiba M.M., Saleh M.M., Hanafi M.Y., Tawfik S.H., Kamel M.A. Maternal obesity and malnourishment exacerbate perinatal oxidative stress resulting in diabetogenic programming in F1 offspring. J. Endocrinol. Investig. 2016;39:643–655. doi: 10.1007/s40618-015-0413-5. [PubMed] [Cross Ref]
44. Fetoui H., Garoui M., Zeghal N. Protein restriction in pregnant- and lactating rats-induced oxidative stress and hypohomocysteinaemia in their offspring. J. Anim. Physiol. Anim. Nutr. 2009;93:263–270. doi: 10.1111/j.1439-0396.2008.00812.x. [PubMed] [Cross Ref]
45. Sen S., Simmons R.A. Maternal Antioxidant Supplementation Prevents Adiposity in the Offspring of Western Diet-Fed Rats. Diabetes. 2010;59:3058–3065. doi: 10.2337/db10-0301. [PMC free article] [PubMed] [Cross Ref]
46. Mohanty P., Hamouda W., Garg R., Aljada A., Ghanim H., Dandona P. Glucose challenge stimulates reactive oxygen species (ROS) generation by leucocytes. J. Clin. Endocrinol. Metab. 2000;85:2970–2973. doi: 10.1210/jcem.85.8.6854. [PubMed] [Cross Ref]
47. Mohanty P., Ghanim H., Hamouda W., Aljada A., Garg R., Dandona P. Both lipid and protein intakes stimulate increased generation of reactive oxygen species by polymorphonuclear leukocytes and mononuclear cells. Am. J. Clin. Nutr. 2002;75:767–772. [PubMed]
48. Aljada A., Mohanty P., Ghanim H., Abdo T., Tripathy D., Chaudhuri A., Dandona P. Increase in intranuclear nuclear factor kappaB and decrease in inhibitor kappaB in mononuclear cells after a mixed meal: Evidence for a proinflammatory effect. Am. J. Clin. Nutr. 2004;79:682–690. [PubMed]
49. Ceriello A., Motz E. Is oxidative stress the pathogenic mechanism underlying insulin resistance, diabetes, and cardiovascular disease? The common soil hypothesis revisited. Arterioscler. Thromb. Vasc. Biol. 2004;24:816–823. doi: 10.1161/01.ATV.0000122852.22604.78. [PubMed] [Cross Ref]
50. Wallace J.P., Johnson B., Padilla J., Mather K. Postprandial lipaemia, oxidative stress and endothelial function: A review. Int. J. Clin. Pract. 2010;64:389–403. doi: 10.1111/j.1742-1241.2009.02146.x. [PubMed] [Cross Ref]
51. Dandona P., Mohanty P., Ghanim H., Aljada A., Browne R., Hamouda W., Prabhala A., Afzal A., Garg R. The suppressive effect of dietary restriction and weight loss in the obese on the generation of reactive oxygen species by leukocytes, lipid peroxidation, and protein carbonylation. J. Clin. Endocrinol. Metab. 2001;86:355–362. doi: 10.1210/jcem.86.1.7150. [PubMed] [Cross Ref]
52. Dandona P., Mohanty P., Hamouda W., Ghanim H., Aljada A., Garg R., Kumar V. Inhibitory effect of a two day fast on reactive oxygen species (ROS) generation by leucocytes and plasma ortho-tyrosine and meta-tyrosine concentrations. J. Clin. Endocrinol. Metab. 2001;86:2899–2902. doi: 10.1210/jcem.86.6.7745. [PubMed] [Cross Ref]
53. Rizza W., Veronese N., Fontana L. What are the roles of calorie restriction and diet quality in promoting healthy longevity? Ageing Res. Rev. 2014;13:38–45. doi: 10.1016/j.arr.2013.11.002. [PubMed] [Cross Ref]
54. Bloomer R.J., Fisher-Wellman K.H. Systemic oxidative stress is increased to a greater degree in young, obese women following consumption of a high fat meal. Oxidative Med. Cell. Longev. 2009;2:19–25. doi: 10.4161/oxim.2.1.7860. [PMC free article] [PubMed] [Cross Ref]
55. Goto C., Nishioka K., Umemura T., Jitsuiki D., Sakagutchi A., Kawamura M., Chayama K., Yoshizumi M., Higashi Y. Acute moderate-intensity exercise induces vasodilation through oxide bioavailiability an increase in nitric in humans. Am. J. Hypertens. 2007;20:825–830. doi: 10.1016/j.amjhyper.2007.02.014. [PubMed] [Cross Ref]
56. Elosua R., Molina L., Fito M., Arquer A., Sanchez-Queseda J.L., Covas M.I., Ordonez-Llanos J., Marrugat J. Response of oxidative stress biomarkers to a 16-week aerobic physical activity program, and to acute physical activity, in healthy young men and women. Atherosclerosis. 2003;167:327–334. doi: 10.1016/S0021-9150(03)00018-2. [PubMed] [Cross Ref]
57. Bloomer R.J., Ferebee D.E., Fisher-Wellman K.H., Quindry J.C., Schilling B.K. Postprandial oxidative stress: Influence of sex and exercise training status. Med. Sci. Sports Exerc. 2009;41:2111–2119. doi: 10.1249/MSS.0b013e3181a9e832. [PubMed] [Cross Ref]
58. Droge W. Free radicals in the physiological control of cell function. Physiol. Rev. 2002;82:47–95. doi: 10.1152/physrev.00018.2001. [PubMed] [Cross Ref]
59. Uribarri J., Stirban A., Sander D., Cai W., Negrean M., Buenting C.E., Koschinsky T., Vlassara H. Single oral challenge by advanced glycation end products acutely impairs endothelial function in diabetic and nondiabetic subjects. Diabetes Care. 2007;30:2579–2582. doi: 10.2337/dc07-0320. [PubMed] [Cross Ref]
60. Diamanti-Kandarakis E., Katsikis I., Piperi C., Alexandraki K., Panidis D. Effect of long-term orlistat treatment on serum levels of advanced glycation end-products in women with polycystic ovary syndrome. Clin. Endocrinol. 2007;66:103–109. doi: 10.1111/j.1365-2265.2006.02693.x. [PubMed] [Cross Ref]
61. Muoio D.M., Newgard C.B. Mechanisms of disease: Molecular and metabolic mechanisms of insulin resistance and β-cell failure in type 2 diabetes. Nat. Rev. Mol. Cell Biol. 2008;9:193–205. doi: 10.1038/nrm2327. [PubMed] [Cross Ref]
62. Samuel V.T., Liu Z.X., Qu X., Elder B.D., Bilz S., Befroy D., Romanelli A.J., Shulman G.I. Mechanism of hepatic insulin resistance in non-alcoholic fatty liver disease. J. Biol. Chem. 2004;279:32345–32353. doi: 10.1074/jbc.M313478200. [PubMed] [Cross Ref]
63. Soardo G., Donnini D., Domenis L., Catena C., De Silvestri D., Cappello D., Dibenedetto A., Carnelutti A., Bonasia V., Pagano C., et al. Oxidative stress is activated by free fatty acids in cultured human hepatocytes. Metab. Syndr. Relat. Disord. 2011;9:397–401. doi: 10.1089/met.2010.0140. [PubMed] [Cross Ref]
64. Lara-Castro C., Garvey W.T. Intracellular lipid accumulation in liver and muscle and the insulin resistance syndrome. Endocrinol. Metab. Clin. N. Am. 2008;37:841–856. doi: 10.1016/j.ecl.2008.09.002. [PMC free article] [PubMed] [Cross Ref]
65. Le Lay S., Simard G., Martinez M.C., Andriantsitohaina R. Oxidative stress and metabolic pathologies: From an adipocentric point of view. Oxidative Med. Cell. Longev. 2014;2014:908539. doi: 10.1155/2014/908539. [PMC free article] [PubMed] [Cross Ref]
66. Kusminski C.M., Scherer P.E. Mitochondrial dysfunction in white adipose tissue. Trends Endocrinol. Metab. 2012;23:435–443. doi: 10.1016/j.tem.2012.06.004. [PMC free article] [PubMed] [Cross Ref]
67. Mahadev K., Motoshima H., Wu X.D., Ruddy J.M., Arnold R.S., Cheng G.J., Lambeth J.D., Goldstein B.J. The NAD(P)H oxidase homolog Nox4 modulates insulin-stimulated generation of H2O2 and plays an integral role in insulin signal transduction. Mol. Cell. Biol. 2004;24:1844–1854. doi: 10.1128/MCB.24.5.1844-1854.2004. [PMC free article] [PubMed] [Cross Ref]
68. Han C.Y., Umemoto T., Omer M., Den Hartigh L.J., Chiba T., Leboeuf R., Buller C.L., Sweet I.R., Pennathur S., Abel E.D., et al. NADPH Oxidase-derived reactive oxygen species increases expression of monocyte chemotactic factor genes in cultured adipocytes. J. Biol. Chem. 2012;287:10379–10393. doi: 10.1074/jbc.M111.304998. [PMC free article] [PubMed] [Cross Ref]
69. Herieka M., Erridge C. High-fat meal induced postprandial inflammation. Mol. Nutr. Food Res. 2014;58:136–146. doi: 10.1002/mnfr.201300104. [PubMed] [Cross Ref]
70. Magne J., Mariotti F., Fischer R., Mathe V., Tome D., Huneau J.F. Early postprandial low-grade inflammation after high-fat meal in healthy rats: Possible involvement of visceral adipose tissue. J. Nutr. Biochem. 2010;21:550–555. doi: 10.1016/j.jnutbio.2009.03.004. [PubMed] [Cross Ref]
71. Travers R.L., Motta A.C., Betts J.A., Thompson D. Adipose tissue metabolic and inflammatory responses to a mixed meal in lean, overweight and obese men. Eur. J. Nutr. 2017;56:375–385. doi: 10.1007/s00394-015-1087-7. [PMC free article] [PubMed] [Cross Ref]
72. Cruz-Teno C., Perez-Martinez P., Delgado-Lista J., Yubero-Serrano E.M., Garcia-Rios A., Marin C., Gomez P., Jimenez-Gomez Y., Camargo A., Rodriguez-Cantalejo F., et al. Dietary fat modifies the postprandial inflammatory state in subjects with metabolic syndrome: The LIPGENE study. Mol. Nutr. Food Res. 2012;56:854–865. doi: 10.1002/mnfr.201200096. [PubMed] [Cross Ref]
73. Meneses M.E., Camargo A., Perez-Martinez P., Delgado-Lista J., Cruz-Teno C., Jimenez-Gomez Y., Paniagua J.A., Gutierrez-Mariscal F.M., Tinahones F.J., Vidal-Puig A., et al. Postprandial inflammatory response in adipose tissue of patients with metabolic syndrome after the intake of different dietary models. Mol. Nutr. Food Res. 2011;55:1759–1770. doi: 10.1002/mnfr.201100200. [PubMed] [Cross Ref]
74. Donath M.Y. Targeting inflammation in the treatment of type 2 diabetes: Time to start. Nat. Rev. Drug Discov. 2014;13:465–476. doi: 10.1038/nrd4275. [PubMed] [Cross Ref]
75. Furukawa S., Fujita T., Shimabukuro M., Iwaki M., Yamada Y., Nakajima Y., Nakayama O., Makishima M., Matsuda M., Shimomura I. Increased oxidative stress in obesity and its impact on metabolic syndrome. J. Clin. Investig. 2004;114:1752–1761. doi: 10.1172/JCI21625. [PMC free article] [PubMed] [Cross Ref]
76. Murdolo G., Piroddi M., Luchetti F., Tortoioli C., Canonico B., Zerbinati C., Galli F., Iuliano L. Oxidative stress and lipid peroxidation by-products at the crossroad between adipose organ dysregulation and obesity-linked insulin resistance. Biochimie. 2013;95:585–594. doi: 10.1016/j.biochi.2012.12.014. [PubMed] [Cross Ref]
77. Maechler P., Jornot L., Wollheim C.B. Hydrogen peroxide alters mitochondrial activation and insulin secretion in pancreatic β cells. J. Biol. Chem. 1999;274:27905–27913. doi: 10.1074/jbc.274.39.27905. [PubMed] [Cross Ref]
78. Tiedge M., Lortz S., Drinkgern J., Lenzen S. Relation between antioxidant enzyme gene expression and antioxidative defense status of insulin-producing cells. Diabetes. 1997;46:1733–1742. doi: 10.2337/diab.46.11.1733. [PubMed] [Cross Ref]
79. Jacqueminet S., Briaud I., Rouault C., Reach G., Poitout V. Inhibition of insulin gene expression by long-term exposure of pancreatic β cells to palmitate is dependent on the presence of a stimulatory glucose concentration. Metab. Clin. Exp. 2000;49:532–536. doi: 10.1016/S0026-0495(00)80021-9. [PubMed] [Cross Ref]
80. Sakai K., Matsumoto K., Nishikawa T., Suefuji M., Nakamaru K., Hirashima Y., Kawashima J., Shirotani T., Ichinose K., Brownlee M., et al. Mitochondrial reactive oxygen species reduce insulin secretion by pancreatic β-cells. Biochem. Biophys. Res. Commun. 2003;300:216–222. doi: 10.1016/S0006-291X(02)02832-2. [PubMed] [Cross Ref]
81. Nowotny K., Jung T., Hohn A., Weber D., Grune T. Advanced glycation end products and oxidative stress in type 2 diabetes mellitus. Biomolecules. 2015;5:194–222. doi: 10.3390/biom5010194. [PMC free article] [PubMed] [Cross Ref]
82. DeFronzo R.A., Gunnarsson R., Bjorkman O., Olsson M., Wahren J. Effects of insulin on peripheral and splanchnic glucose metabolism in noninsulin-dependent (type II) diabetes mellitus. J. Clin. Investig. 1985;76:149–155. doi: 10.1172/JCI111938. [PMC free article] [PubMed] [Cross Ref]
83. Dimitriadis G., Mitrou P., Lambadiari V., Maratou E., Raptis S.A. Insulin effects in muscle and adipose tissue. Diabetes Res. Clin. Pract. 2011;93:S52–S59. doi: 10.1016/S0168-8227(11)70014-6. [PubMed] [Cross Ref]
84. Galgani J.E., Moro C., Ravussin E. Metabolic flexibility and insulin resistance. Am. J. Physiol. Endocrinol. Metab. 2008;295:E1009–E1017. doi: 10.1152/ajpendo.90558.2008. [PubMed] [Cross Ref]
85. Corpeleijn E., Saris W.H.M., Blaak E.E. Metabolic flexibility in the development of insulin resistance and type 2 diabetes: Effects of lifestyle. Obes. Rev. 2009;10:178–193. doi: 10.1111/j.1467-789X.2008.00544.x. [PubMed] [Cross Ref]
86. Pagel-Langenickel I., Bao J.J., Pang L.Y., Sack M.N. The role of mitochondria in the pathophysiology of skeletal muscle insulin resistance. Endocr. Rev. 2010;31:25–51. doi: 10.1210/er.2009-0003. [PubMed] [Cross Ref]
87. Heilbronn L.K., de Jonge L., Frisard M.I., DeLany J.P., Larson-Meyer D.E., Rood J., Nguyen T., Martin C.K., Volaufova J., Most M.M., et al. Effect of 6-month calorie restriction on biomarkers of longevity, metabolic adaptation, and oxidative stress in overweight individuals: A randomized controlled trial. J. Am. Med. Assoc. 2006;295:1539–1548. doi: 10.1001/jama.295.13.1539. [PMC free article] [PubMed] [Cross Ref]
88. Ceriello A., Esposito K., La Sala L., Pujadas G., De Nigris V., Testa R., Bucciarelli L., Rondinelli M., Genovese S. The protective effect of the Mediterranean diet on endothelial resistance to GLP-1 in type 2 diabetes: A preliminary report. Cardiovasc. Diabetol. 2014;13:140. doi: 10.1186/s12933-014-0140-9. [PMC free article] [PubMed] [Cross Ref]
89. Vineis P., Wild C.P. Global cancer patterns: Causes and prevention. Lancet. 2014;383:549–557. doi: 10.1016/S0140-6736(13)62224-2. [PubMed] [Cross Ref]
90. World Cancer Research Fund/American Institute for Cancer Research . Food, Nutrition, Physical Activity, and the Prevention of Cancer: A Global Perspective. American Institute for Cancer Research; Washington, DC, USA: 2007.
91. World Cancer Research Fund/American Institute for Cancer Research . Breast Cancer 2010 Report: Food, Nutrition, Physical Activity, and the Prevention of Breast Cancer. American Institute for Cancer Research; Washington, DC, USA: 2010.
92. World Cancer Research Fund/American Institute for Cancer Research . Colorectal Cancer 2011 Report: Food, Nutrition, Physical Activity, and the Prevention of Colorectal Cancer. American Institute for Cancer Research; Washington, DC, USA: 2011.
93. World Cancer Research Fund/American Institute for Cancer Research . Pancreatic Cancer 2012 Report: Food, Nutrition, Physical Activity, and the Prevention of Pancreatic Cancer. American Institute for Cancer Research; Washington, DC, USA: 2012.
94. World Cancer Research Fund/American Institute for Cancer Research . Endometrial Cancer 2013 Report: Food, Nutrition, Physical Activity, and the Prevention of Endometrial Cancer. American Institute for Cancer Research; Washington, DC, USA: 2013.
95. World Cancer Research Fund/American Institute for Cancer Research . Ovarian Cancer 2014 Report: Food, Nutrition, Physical Activity, and the Prevention of Ovarian Cancer. American Institute for Cancer Research; Washington, DC, USA: 2014.
96. Ames B.N., Wakimoto P. Are vitamin and mineral deficiencies a major cancer risk? Nat. Rev. Cancer. 2002;2:694–704. doi: 10.1038/nrc886. [PubMed] [Cross Ref]
97. Brash D.E., Havre P. New careers for antioxidants. Proc. Natl. Acad. Sci. USA. 2002;99:13969–13971. doi: 10.1073/pnas.232574399. [PubMed] [Cross Ref]
98. Mathers J., Coxhead J., Tyson J. Nutrition and DNA repair-potential molecular mechanisms of action. Curr. Cancer Drug Targets. 2007;7:425–431. doi: 10.2174/156800907781386588. [PubMed] [Cross Ref]
99. Shimada T., Fujii-Kuriyama Y. Metabolic activation of polycyclic aromatic hydrocarbons to carcinogens by cytochromes P450 1A1 and 1B1. Cancer Sci. 2004;95:1–6. doi: 10.1111/j.1349-7006.2004.tb03162.x. [PubMed] [Cross Ref]
100. Shimada T., Inoue K., Suzuki Y., Kawai T., Azuma E., Nakajima T., Shindo M., Kurose K., Sugie A., Yamagishi Y., et al. Arylhydrocarbon receptor-dependent induction of liver and lung cytochromes P450 1A1, 1A2, and 1B1 by polycyclic aromatic hydrocarbons and polychlorinated biphenyls in genetically engineered C57BL/6J mice. Carcinogenesis. 2002;23:1199–1207. doi: 10.1093/carcin/23.7.1199. [PubMed] [Cross Ref]
101. Puga A., Ma C., Marlowe J.L. The aryl hydrocarbon receptor cross-talks with multiple signal transduction pathways. Biochem. Pharmacol. 2009;77:713–722. doi: 10.1016/j.bcp.2008.08.031. [PMC free article] [PubMed] [Cross Ref]
102. Androutsopoulos V.P., Tsatsakis A.M., Spandidos D.A. Cytochrome P450 CYP1A1: Wider roles in cancer progression and prevention. BMC Cancer. 2009;9:187 doi: 10.1186/1471-2407-9-187. [PMC free article] [PubMed] [Cross Ref]
103. Baan R., Straif K., Grosse Y., Secretan B., El Ghissassi F., Bouvard V., Altieri A., Cogliano V., WHO International Agency for Research on Cancer Monograph Working Group Carcinogenicity of alcoholic beverages. Lancet Oncol. 2007;8:292–293. doi: 10.1016/S1470-2045(07)70099-2. [PubMed] [Cross Ref]
104. Savolainen V., Liesto K., Männikkö A., Penttilä A., Karhunen P. Alcohol consumption and alcoholic liver disease: Evidence of a threshold level of effects of ethanol. ‎Alcohol. Clin. Exp. Res. 1993;17:1112–1117. doi: 10.1111/j.1530-0277.1993.tb05673.x. [PubMed] [Cross Ref]
105. Wu D., Cederbaum A.I. Oxidative stress and alcoholic liver disease. Semin. Liver Dis. 2009;29:141–154. doi: 10.1055/s-0029-1214370. [PubMed] [Cross Ref]
106. Sabitha K., Venugopal B., Rafi M., Ramana K. Role of antioxidant enzymes in glucose and lipid metabolism in association with obesityand type 2 diabetes. Am. J. Med. Sci. Med. 2014;2:21–24. doi: 10.12691/ajmsm-2-1-5. [Cross Ref]
107. Fang J.-L., Vaca C.E. Detection of DNA adducts of acetaldehyde in peripheral white blood cells of alcohol abusers. Carcinogenesis. 1997;18:627–632. doi: 10.1093/carcin/18.4.627. [PubMed] [Cross Ref]
108. Praud D., Rota M., Rehm J., Shield K., Zatoński W., Hashibe M., La Vecchia C., Boffetta P. Cancer incidence and mortality attributable to alcohol consumption. Int. J. Cancer. 2016;138:1380–1387. doi: 10.1002/ijc.29890. [PubMed] [Cross Ref]
109. Gavin D.P., Kusumo H., Zhang H., Guidotti A., Pandey S.C. Role of Growth arrest and DNA damage-inducible, β in alcohol-drinking behaviors. Alcohol. Clin. Exp. Res. 2016;40:263–272. doi: 10.1111/acer.12965. [PMC free article] [PubMed] [Cross Ref]
110. Chuang S.C., La Vecchia C., Boffetta P. Liver cancer: Descriptive epidemiology and risk factors other than HBV and HCV infection. Cancer Lett. 2009;286:9–14. doi: 10.1016/j.canlet.2008.10.040. [PubMed] [Cross Ref]
111. Druesne-Pecollo N., Tehard B., Mallet Y., Gerber M., Norat T., Hercberg S., Latino-Martel P. Alcohol and genetic polymorphisms: Effect on risk of alcohol-related cancer. Lancet Oncol. 2009;10:173–180. doi: 10.1016/S1470-2045(09)70019-1. [PubMed] [Cross Ref]
112. Deshpande N., Kandi S., Muddeshwar M., Ramana K.V. Effect of alcohol consumption and oxidative stress and its role in dna damage. Am. J. Biomed. Res. 2014;2:7–10. doi: 10.12691/ajbr-2-1-2. [Cross Ref]
113. Wang Y., Millonig G., Nair J., Patsenker E., Stickel F., Mueller S., Bartsch H., Seitz H.K. Ethanol-induced cytochrome P4502E1 causes carcinogenic etheno-DNA lesions in alcoholic liver disease. Hepatology. 2009;50:453–461. doi: 10.1002/hep.22978. [PubMed] [Cross Ref]
114. Brooks P.J., Zakhari S. Moderate alcohol consumption and breast cancer in women: From epidemiology to mechanisms and interventions. Alcohol. Clin. Exp. Res. 2013;37:23–30. doi: 10.1111/j.1530-0277.2012.01888.x. [PMC free article] [PubMed] [Cross Ref]
115. Suzuki R., Orsini N., Mignone L., Saji S., Wolk A. Alcohol intake and risk of breast cancer defined by estrogen and progesterone receptor status—A meta-analysis of epidemiological studies. Int. J. Cancer. 2008;122:1832–1841. doi: 10.1002/ijc.23184. [PubMed] [Cross Ref]
116. Zuccolo L., Lewis S.J., Donovan J.L., Hamdy F.C., Neal D.E., Smith G.D. Alcohol consumption and PSA-detected prostate cancer risk—A case-control nested in the ProtecT study. Int. J. Cancer. 2013;132:2176–2185. doi: 10.1002/ijc.27877. [PMC free article] [PubMed] [Cross Ref]
117. Sawada N., Inoue M., Iwasaki M., Sasazuki S., Yamaji T., Shimazu T., Tsugane S. Alcohol and smoking and subsequent risk of prostate cancer in Japanese men: The Japan Public Health Center-based prospective study. Int. J. Cancer. 2014;134:971–978. doi: 10.1002/ijc.28423. [PubMed] [Cross Ref]
118. Watters J.L., Park Y., Hollenbeck A., Schatzkin A., Albanes D. Alcoholic beverages and prostate cancer in a prospective US cohort study. Am. J. Epidemiol. 2010;172:773–780. doi: 10.1093/aje/kwq200. [PMC free article] [PubMed] [Cross Ref]
119. Chao C., Haque R., Van Den Eeden S.K., Caan B.J., Poon K.Y., Quinn V.P. Red wine consumption and risk of prostate cancer: The California men’s health study. Int. J. Cancer. 2010;126:171–179. doi: 10.1002/ijc.24637. [PubMed] [Cross Ref]
120. Breslow R.A., Chen C.M., Graubard B.I., Mukamal K.J. Prospective study of alcohol consumption quantity and frequency and cancer-specific mortality in the US population. Am. J. Epidemiol. 2011;174:1044–1053. doi: 10.1093/aje/kwr210. [PMC free article] [PubMed] [Cross Ref]
121. Middleton Fillmore K., Chikritzhs T., Stockwell T., Bostrom A., Pascal R. Alcohol use and prostate cancer: A meta-analysis. Mol. Nutr. Food Res. 2009;53:240–255. doi: 10.1002/mnfr.200800122. [PubMed] [Cross Ref]
122. Rota M., Scotti L., Turati F., Tramacere I., Islami F., Bellocco R., Negri E., Corrao G., Boffetta P., La Vecchia C. Alcohol consumption and prostate cancer risk: A meta-analysis of the dose–risk relation. Eur. J. Cancer Prev. 2012;21:350–359. doi: 10.1097/CEJ.0b013e32834dbc11. [PubMed] [Cross Ref]
123. Shahedi K., Pandol S.J., Hu R. Oxidative stress and alcoholic pancreatitis. J. Gastroenterol. Hepatol. Res. 2013;2:335–342.
124. Kandi S., Deshpande N., Pinnelli V.B.K., Devaki R., Rao P., Ramana K. Alcoholism and its role in the development of oxidative stress and DNA damage: An Insight. Am. J. Med. Sci. Med. 2014;2:64–66. doi: 10.12691/ajmsm-2-3-3. [Cross Ref]
125. Cunningham C.C., Bailey S.M. Ethanol consumption and liver mitochondria function. Neurosignals. 2001;10:271–282. doi: 10.1159/000046892. [PubMed] [Cross Ref]
126. Arranz S., Chiva-Blanch G., Valderas-Martínez P., Medina-Remón A., Lamuela-Raventós R.M., Estruch R. Wine, beer, alcohol and polyphenols on cardiovascular disease and cancer. Nutrients. 2012;4:759–781. doi: 10.3390/nu4070759. [PMC free article] [PubMed] [Cross Ref]
127. Varela-Rey M., Woodhoo A., Martinez-Chantar M.-L., Mato J.M., Lu S.C. Alcohol, DNA methylation, and cancer. Alcohol Res. 2013;35:25. [PMC free article] [PubMed]
128. Wei-Chuan T., Yi-Heng L., Chih-Chan L., Ting-Hsing C., Jyh-Hong C. Effects of oxidative stress on endothelial function after a high-fat meal. Clin. Sci. 2004;106:315–319. [PubMed]
129. Gregersen S., Samocha-Bonet D., Heilbronn L., Campbell L. Inflammatory and oxidative stress responses to high-carbohydrate and high-fat meals in healthy humans. J. Nutr. Metab. 2012;2012:238056. doi: 10.1155/2012/238056. [PMC free article] [PubMed] [Cross Ref]
130. Michels K.B., Mohllajee A.P., Roset-Bahmanyar E., Beehler G.P., Moysich K.B. Diet and breast cancer: A review of the prospective observational studies. Cancer. 2007;109:2712–2749. doi: 10.1002/cncr.22654. [PubMed] [Cross Ref]
131. Shikany J.M., Redden D.T., Neuhouser M.L., Chlebowski R.T., Rohan T.E., Simon M.S., Liu S., Lane D.S., Tinker L. Dietary glycemic load, glycemic index, and carbohydrate and risk of breast cancer in the Women’s Health Initiative. Nutr. Cancer. 2011;63:899–907. doi: 10.1080/01635581.2011.587227. [PMC free article] [PubMed] [Cross Ref]
132. Amador-Licona N., Díaz-Murillo T.A., Gabriel-Ortiz G., Pacheco-Moises F.P., Pereyra-Nobara T.A., Guízar-Mendoza J.M., Barbosa-Sabanero G., Orozco-Aviña G., Moreno-Martínez S.C., Luna-Montalbán R. Omega 3 fatty acids supplementation and oxidative stress in HIV-seropositive patients. A clinical trial. PLoS ONE. 2016;11:e0151637 doi: 10.1371/journal.pone.0151637. [PMC free article] [PubMed] [Cross Ref]
133. Assies J., Mocking R.J., Lok A., Ruhé H.G., Pouwer F., Schene A.H. Effects of oxidative stress on fatty acid-and one-carbon-metabolism in psychiatric and cardiovascular disease comorbidity. Acta Psychiatr. Scand. 2014;130:163–180. doi: 10.1111/acps.12265. [PMC free article] [PubMed] [Cross Ref]
134. Bieniek J., Childress C., Swatski M.D., Yang W. COX-2 inhibitors arrest prostate cancer cell cycle progression by down/regulation of kinetochore/ centromere proteins. Prostate. 2014;74:999–1011. doi: 10.1002/pros.22815. [PubMed] [Cross Ref]
135. Liu J., Hu S., Cui Y., Sun M.-K., Xie F., Zhang Q., Jin J. Saturated fatty acids up-regulate COX-2 expression in prostate epithelial cells via toll-like receptor 4/NF-κB signaling. Inflammation. 2014;37:467–477. doi: 10.1007/s10753-013-9760-6. [PubMed] [Cross Ref]
136. Gu Z.N., Suburu J., Chen H.Q., Chen Y.Q. Mechanisms of Omega-3 polyunsaturated fatty acids in prostate cancer prevention. Biomed. Res. Int. 2013;2013:824563. doi: 10.1155/2013/824563. [PMC free article] [PubMed] [Cross Ref]
137. Larsson S.C., Kumlin M., Ingelman-Sundberg M., Wolk A. Dietary long-chain n-3 fatty acids for the prevention of cancer: A review of potential mechanisms. Am. J. Clin. Nutr. 2004;79:935–945. [PubMed]
138. Sánchez D., Quiñones M., Moulay L., Muguerza B., Miguel M., Aleixandre A. Soluble fiber-enriched diets improve inflammation and oxidative stress biomarkers in Zucker fatty rats. Pharmacol. Res. 2011;64:31–35. doi: 10.1016/j.phrs.2011.02.005. [PubMed] [Cross Ref]
139. Nance S.A., A’ja V.D., Gwathmey T.M., Hairston K.G. Soluble dietary fiber in obesity-associated inflammation and oxidative stress in African American women. FASEB J. 2017;31:434.2. [PubMed]
140. Belobrajdic D.P., Lam Y.Y., Mano M., Wittert G.A., Bird A.R. Cereal based diets modulate some markers of oxidative stress and inflammation in lean and obese Zucker rats. Nutr. Metab. 2011;8:27. doi: 10.1186/1743-7075-8-27. [PMC free article] [PubMed] [Cross Ref]
141. Diniz Y.S., Cicogna A.C., Padovani C.R., Silva M.D., Faine L.A., Galhardi C.M., Rodrigues H.G., Novelli E.L. Dietary restriction and fibre supplementation: Oxidative stress and metabolic shifting for cardiac health. Can. J. Physiol. Pharmacol. 2003;81:1042–1048. doi: 10.1139/y03-097. [PubMed] [Cross Ref]
142. Dong J.Y., He K., Wang P.Y., Qin L.Q. Dietary fiber intake and risk of breast cancer: A meta-analysis of prospective cohort studies. Am. J. Clin. Nutr. 2011;94:900–905. doi: 10.3945/ajcn.111.015578. [PubMed] [Cross Ref]
143. Aune D., Chan D.S.M., Greenwood D.C., Vieira A.R., Rosenblatt D.A.N., Vieira R., Norat T. Dietary fiber and breast cancer risk: A systematic review and meta-analysis of prospective studies. Ann. Oncol. 2012;23:1394–1402. doi: 10.1093/annonc/mdr589. [PubMed] [Cross Ref]
144. Romaneiro S., Parekh N. Dietary fiber intake and colorectal cancer risk: Weighing the evidence from epidemiologic studies. Top. Clin. Nutr. 2012;27:41–47. doi: 10.1097/TIN.0b013e3182461dd4. [Cross Ref]
145. Lottenberg A.M.P., Fan P.L.T., Buonacorso V. Effects of dietary fiber intake on inflammation in chronic diseases. Einstein. 2010;8:254–258. doi: 10.1590/s1679-45082010md1310. [PubMed] [Cross Ref]
146. Mukai R., Terao J. Role of dietary flavonoids in oxidative stress and prevention of muscle atrophy. J. Phys. Fit. Sport Med. 2013;2:385–392. doi: 10.7600/jpfsm.2.385. [Cross Ref]
147. Costa Marques T.H., Santos De Melo C.H., De Carvalho F., Rusbene B., Costa L.M., De Souza A.A., David J.M., De Lima David J.P., De Freitas R.M. Phytochemical profile and qualification of biological activity of an isolated fraction of Bellis perennis. Biol. Res. 2013;46:231–238. doi: 10.4067/S0716-97602013000300002. [PubMed] [Cross Ref]
148. Yokomizo A., Moriwaki M. Effects of uptake of flavonoids on oxidative stress induced by hydrogen peroxide in human intestinal Caco-2 cells. Biosci. Biotechnol. Biochem. 2006;70:1317–1324. doi: 10.1271/bbb.50604. [PubMed] [Cross Ref]
149. Zhang H.Y., Cui J., Zhang Y., Wang Z.L., Chong T., Wang Z.M. Isoflavones and prostate cancer: A review of some critical issues. Chin. Med. J. 2016;129:341–347. [PMC free article] [PubMed]
150. Tse G., Eslick G.D. Soy and isoflavone consumption and risk of gastrointestinal cancer: A systematic review and meta-analysis. Eur. J. Nutr. 2016;55:63–73. doi: 10.1007/s00394-014-0824-7. [PubMed] [Cross Ref]
151. Nagata C. Factors to consider in the association between soy isoflavone intake and breast cancer risk. J. Epidemiol. 2010;20:83–89. doi: 10.2188/jea.JE20090181. [PMC free article] [PubMed] [Cross Ref]
152. Stubert J., Gerber B. Isoflavones—Mechanism of action and impact on breast cancer risk. Breast Care. 2009;4:22–29. doi: 10.1159/000200980. [PMC free article] [PubMed] [Cross Ref]
153. Kobayashi T., Nakata T., Kuzumaki T. Effect of flavonoids on cell cycle progression in prostate cancer cells. Cancer Lett. 2002;176:17–23. doi: 10.1016/S0304-3835(01)00738-8. [PubMed] [Cross Ref]
154. Ramos S. Effects of dietary flavonoids on apoptotic pathways related to cancer chemoprevention. J. Nutr. Biochem. 2007;18:427–442. doi: 10.1016/j.jnutbio.2006.11.004. [PubMed] [Cross Ref]
155. Petzke K.J., Elsner A., Proll J., Thielecke F., Metges C.C. Long-term high protein intake does not increase oxidative stress in rats. J. Nutr. 2000;130:2889–2896. [PubMed]
156. Ezraty B., Gennaris A., Barras F., Collet J.-F. Oxidative stress, protein damage and repair in bacteria. Nat. Rev. Microbiol. 2017;15:385–396. doi: 10.1038/nrmicro.2017.26. [PubMed] [Cross Ref]
157. Levine M.E., Suarez J.A., Brandhorst S., Balasubramanian P., Cheng C.-W., Madia F., Fontana L., Mirisola M.G., Guevara-Aguirre J., Wan J. Low protein intake is associated with a major reduction in IGF-1, cancer, and overall mortality in the 65 and younger but not older population. Cell Metab. 2014;19:407–417. doi: 10.1016/j.cmet.2014.02.006. [PMC free article] [PubMed] [Cross Ref]
158. Alexander D.D., Weed D.L., Miller P.E., Mohamed M.A. Red meat and colorectal cancer: A quantitative update on the state of the epidemiologic science. J. Am. Coll. Nutr. 2015;34:521–543. doi: 10.1080/07315724.2014.992553. [PMC free article] [PubMed] [Cross Ref]
159. Olson J.A. Carotenoids and Vitamin A: An Overview. In: Ong A.S.H., Packer L., editors. Lipid-Soluble Antioxidants: Biochemistry and Clinical Applications. Birkhäuser Basel; Basel, Switzerland: 1992. pp. 178–192.
160. Meydani M. Protective role of dietary vitamin E on oxidative stress in aging. Age. 1992;15:89–93. doi: 10.1007/BF02435007. [Cross Ref]
161. Huang X.Y., Gao Y.S., Zhi X.S., Ta N., Jiang H., Zheng J.M. Association between vitamin A, retinol and carotenoid intake and pancreatic cancer risk: Evidence from epidemiologic studies. Sci. Rep. 2016;6:38936. doi: 10.1038/srep38936. [PMC free article] [PubMed] [Cross Ref]
162. Gong Z., Holly E.A., Bracci P.M. Intake of folate, vitamins B6, B12 and methionine and risk of pancreatic cancer in a large population-based case–control study. Cancer Causes Control. 2009;20:1317–1325. doi: 10.1007/s10552-009-9352-9. [PMC free article] [PubMed] [Cross Ref]
163. Fan H., Kou J.T., Han D.D., Li P., Zhang D., Wu Q., He Q. Association between vitamin C intake and the risk of pancreatic cancer: A meta-analysis of observational studies. Sci. Rep. 2015;5:13973. doi: 10.1038/srep13973. [PMC free article] [PubMed] [Cross Ref]
164. Cadeau C., Fournier A., Mesrine S., Clavel-Chapelon F., Fagherazzi G., Boutron-Ruault M.C. Postmenopausal breast cancer risk and interactions between body mass index, menopausal hormone therapy use, and vitamin D supplementation: Evidence from the E3N cohort. Int. J. Cancer. 2016;139:2193–2200. doi: 10.1002/ijc.30282. [PubMed] [Cross Ref]
165. Peng L.J., Liu X.D., Lu Q., Tang T.Q., Yang Z.Y. Vitamin E intake and pancreatic cancer risk: A meta-analysis of observational studies. Med. Sci. Monit. 2015;21:1249–1255. [PMC free article] [PubMed]
166. Garland C.F., Garland F.C., Gorham E.D., Lipkin M., Newmark H., Mohr S.B., Holick M.F. The role of vitamin D in cancer prevention. Am. J. Public Health. 2006;96:252–261. doi: 10.2105/AJPH.2004.045260. [PubMed] [Cross Ref]
167. Brand-Miller J.C. Postprandial glycemia, glycemic index, and the prevention of type 2 diabetes. Am. J. Clin. Nutr. 2004;80:243–244. [PubMed]
168. Turati F., Galeone C., Gandini S., Augustin L.S., Jenkins D.J., Pelucchi C., La Vecchia C. High glycemic index and glycemic load are associated with moderately increased cancer risk. Mol. Nutr. Food Res. 2015;59:1384–1394. doi: 10.1002/mnfr.201400594. [PubMed] [Cross Ref]
169. Choi Y., Giovannucci E., Lee J.E. Glycaemic index and glycaemic load in relation to risk of diabetes-related cancers: A meta-analysis. Br. J. Nutr. 2012;108:1934–1947. doi: 10.1017/S0007114512003984. [PubMed] [Cross Ref]
170. Ye Y., Wu Y., Xu J., Ding K., Shan X., Xia D. Association between dietary carbohydrate intake, glycemic index and glycemic load, and risk of gastric cancer. Eur. J. Nutr. 2017;56:1169–1177. doi: 10.1007/s00394-016-1166-4. [PubMed] [Cross Ref]
171. Melkonian S.C., Daniel C.R., Ye Y., Pierzynski J.A., Roth J.A., Wu X. Glycemic index, glycemic load, and lung cancer risk in non-hispanic whites. Cancer Epidemiol. Biomark. Prev. 2016;25:532–539. doi: 10.1158/1055-9965.EPI-15-0765. [PMC free article] [PubMed] [Cross Ref]
172. Gordin D., Groop P.-H. Aspects of Hyperglycemia Contribution to arterial stiffness and cardiovascular complications in patients with type 1 diabetes. J. Diabetes Sci. Technol. 2016;10:1059–1064. doi: 10.1177/1932296816636894. [PMC free article] [PubMed] [Cross Ref]
173. Ceriello A. The post-prandial state and cardiovascular disease: Relevance to diabetes mellitus. Diabetes Metab. Res. Rev. 2000;16:125–132. doi: 10.1002/(SICI)1520-7560(200003/04)16:2<125::AID-DMRR90>3.0.CO;2-4. [PubMed] [Cross Ref]
174. Vanessa Fiorentino T., Prioletta A., Zuo P., Folli F. Hyperglycemia-induced oxidative stress and its role in diabetes mellitus related cardiovascular diseases. Curr. Pharm. Des. 2013;19:5695–5703. doi: 10.2174/1381612811319320005. [PubMed] [Cross Ref]
175. Tang W.H., Martin K.A., Hwa J. Aldose reductase, oxidative stress, and diabetic mellitus. Front. Pharmacol. 2012;3:87. doi: 10.3389/fphar.2012.00087. [PMC free article] [PubMed] [Cross Ref]
176. Hu Y., Block G., Norkus E.P., Morrow J.D., Dietrich M., Hudes M. Relations of glycemic index and glycemic load with plasma oxidative stress markers. Am. J. Clin. Nutr. 2006;84:70–76. [PubMed]
177. Bajaj S., Khan A. Antioxidants and diabetes. Indian J. Endocrinol. Metab. 2012;16:S267–S271. [PMC free article] [PubMed]
178. Choi S.-W., Benzie I.F., Ma S.-W., Strain J., Hannigan B.M. Acute hyperglycemia and oxidative stress: Direct cause and effect? Free Radic. Biol. Med. 2008;44:1217–1231. doi: 10.1016/j.freeradbiomed.2007.12.005. [PubMed] [Cross Ref]
179. De Kreutzenberg S.V., Fadini G.P., Boscari F., Rossi E., Guerra S., Sparacino G., Cobelli C., Ceolotto G., Bottero M., Avogaro A. Impaired hemodynamic response to meal intake in insulin-resistant subjects: An impedance cardiography approach. Am. J. Clin. Nutr. 2011;93:926–933. doi: 10.3945/ajcn.110.003582. [PubMed] [Cross Ref]
180. Romieu I., Ferrari P., Rinaldi S., Slimani N., Jenab M., Olsen A., Tjonneland A., Overvad K., Boutron-Ruault M.-C., Lajous M. Dietary glycemic index and glycemic load and breast cancer risk in the European Prospective Investigation into Cancer and Nutrition (EPIC) Am. J. Clin. Nutr. 2012;96:345–355. doi: 10.3945/ajcn.111.026724. [PubMed] [Cross Ref]
181. Wirfalt E., McTaggart A., Pala V., Gullberg B., Frasca G., Panico S., Bueno-de-Mesquita H.B., Peeters P.H., Engeset D., Skeie G., et al. Food sources of carbohydrates in a European cohort of adults. Public Health Nutr. 2002;5:1197–1215. doi: 10.1079/PHN2002399. [PubMed] [Cross Ref]
182. O’Neil C.E., Keast D.R., Fulgoni V.L., Nicklas T.A. Food sources of energy and nutrients among adults in the US: NHANES 2003–2006. Nutrients. 2012;4:2097–2120. doi: 10.3390/nu4122097. [PMC free article] [PubMed] [Cross Ref]
183. Varela-López A., Quiles J.L., Cordero M., Giampieri F., Bullón P. Oxidative stress and dietary fat type in relation to periodontal disease. Antioxidants. 2015;4:322–344. doi: 10.3390/antiox4020322. [PMC free article] [PubMed] [Cross Ref]
184. Guéraud F., Taché S., Steghens J.-P., Milkovic L., Borovic-Sunjic S., Zarkovic N., Gaultier E., Naud N., Héliès-Toussaint C., Pierre F. Dietary polyunsaturated fatty acids and heme iron induce oxidative stress biomarkers and a cancer promoting environment in the colon of rats. Free Radic. Biol. Med. 2015;83:192–200. doi: 10.1016/j.freeradbiomed.2015.02.023. [PubMed] [Cross Ref]
185. Ruiz R.B., Hernandez P.S. Diet and cancer: Risk factors and epidemiological evidence. Maturitas. 2014;77:202–208. doi: 10.1016/j.maturitas.2013.11.010. [PubMed] [Cross Ref]
186. Dinwiddie M.T., Terry P.D., Whelan J., Patzer R.E. Omega-3 fatty acid consumption and prostate cancer: A review of exposure measures and results of epidemiological studies. J. Am. Coll. Nutr. 2016;35:452–468. doi: 10.1080/07315724.2015.1032444. [PubMed] [Cross Ref]
187. Mocellin M.C., Camargo C.Q., Nunes E.A., Fiates G.M.R., Trindade E.B.S.M. A systematic review and meta-analysis of the n-3 polyunsaturated fatty acids effects on inflammatory markers in colorectal cancer. Clin. Nutr. 2016;35:359–369. doi: 10.1016/j.clnu.2015.04.013. [PubMed] [Cross Ref]
188. Bassett J.K., Hodge A.M., English D.R., MacInnis R.J., Giles G.G. Plasma phospholipids fatty acids, dietary fatty acids, and breast cancer risk. Cancer Causes Control. 2016;27:759–773. doi: 10.1007/s10552-016-0753-2. [PubMed] [Cross Ref]
189. MacLean C.H., Newberry S.J., Mojica W.A., Khanna P., Issa A.M., Suttorp M.J., Lim Y.W., Traina S.B., Hilton L., Garland R., et al. Effects of omega-3 fatty acids on cancer risk—A systematic review. JAMA J. Am. Med. Assoc. 2006;295:403–415. doi: 10.1001/jama.295.4.403. [PubMed] [Cross Ref]
190. Chan J.M., Gann P.H., Giovannucci E.L. Role of diet in prostate cancer development and progression. J. Clin. Oncol. 2005;23:8152–8160. doi: 10.1200/JCO.2005.03.1492. [PubMed] [Cross Ref]
191. Eser P.O., Vanden Heuvel J.P., Araujo J., Thompson J.T. Marine-and plant-derived Omega-3 fatty acids differentially regulate prostate cancer cell proliferation. Mol. Clin. Oncol. 2013;1:444–452. [PMC free article] [PubMed]
192. McCarty M.F., Lavie C.J., O’Keefe J.H. Omega-3 and prostate cancer: Examining the pertinent evidence. Mayo Clin. Proc. 2014;89:444. doi: 10.1016/j.mayocp.2013.10.029. [PubMed] [Cross Ref]
193. Gao Z., Zhang H., Liu J., Lau C.W., Liu P., Chen Z.Y., Lee H.K., Tipoe G.L., Ho H.M., Yao X. Cyclooxygenase-2-dependent oxidative stress mediates palmitate-induced impairment of endothelium-dependent relaxations in mouse arteries. Biochem. Pharmacol. 2014;91:474–482. doi: 10.1016/j.bcp.2014.08.009. [PubMed] [Cross Ref]
194. Hori S., Butler E., McLoughlin J. Prostate cancer and diet: Food for thought? BJU Int. 2011;107:1348–1359. doi: 10.1111/j.1464-410X.2010.09897.x. [PubMed] [Cross Ref]
195. Shapira N. Nutritional approach to sun protection: A suggested complement to external strategies. Nutr. Rev. 2010;68:75–86. doi: 10.1111/j.1753-4887.2009.00264.x. [PubMed] [Cross Ref]
196. Barone M., Lofano K., De Tullio N., Licinio R., Albano F., Di Leo A. Dietary, endocrine, and metabolic factors in the development of colorectal cancer. J. Gastrointest. Cancer. 2012;43:13–19. doi: 10.1007/s12029-011-9332-7. [PubMed] [Cross Ref]
197. Chua M.E., Sio M.C., Sorongon M.C., Dy J.S. Relationship of dietary intake of omega-3 and omega-6 Fatty acids with risk of prostate cancer development: A meta-analysis of prospective studies and review of literature. Prostate Cancer. 2012;2012:826254. doi: 10.1155/2012/826254. [PMC free article] [PubMed] [Cross Ref]
198. Szymanski K.M., Wheeler D.C., Mucci L.A. Fish consumption and prostate cancer risk: A review and meta-analysis. Am. J. Clin. Nutr. 2010;92:1223–1233. doi: 10.3945/ajcn.2010.29530. [PubMed] [Cross Ref]
199. Aune D., Chan D.S., Lau R., Vieira R., Greenwood D.C., Kampman E., Norat T. Dietary fibre, whole grains, and risk of colorectal cancer: Systematic review and dose-response meta-analysis of prospective studies. BMJ. 2011;343:d6617. doi: 10.1136/bmj.d6617. [PubMed] [Cross Ref]
200. Mileo A.M., Miccadei S. Polyphenols as modulator of oxidative stress in cancer disease: New therapeutic strategies. Oxidative Med. Cell. Longev. 2016;2016:6475624. doi: 10.1155/2016/6475624. [PMC free article] [PubMed] [Cross Ref]
201. Luo K.-W., Ko C.-H., Yue G.G.-L., Lee J.K.-M., Li K.-K., Lee M., Li G., Fung K.-P., Leung P.-C., Bik-San Lau C. Green tea (Camellia sinensis) extract inhibits both the metastasis and osteolytic components of mammary cancer 4T1 lesions in mice. J. Nutr. Biochem. 2014;25:395–403. doi: 10.1016/j.jnutbio.2013.11.013. [PubMed] [Cross Ref]
202. Norat T., Aune D., Chan D., Romaguera D. Advances in Nutrition and Cancer. Springer; Berlin, Germany: 2014. Fruits and vegetables: Updating the epidemiologic evidence for the WCRF/AICR lifestyle recommendations for cancer prevention; pp. 35–50. [PubMed]
203. Willcox J.K., Ash S.L., Catignani G.L. Antioxidants and prevention of chronic disease. Crit. Rev. Food Sci. Nutr. 2004;44:275–295. doi: 10.1080/10408690490468489. [PubMed] [Cross Ref]
204. Hussain T., Tan B., Yin Y., Blachier F., Tossou M.C.B., Rahu N. Oxidative stress and inflammation: What polyphenols can do for us? Oxidative Med. Cell. Longev. 2016;2016:7432797. doi: 10.1155/2016/7432797. [PMC free article] [PubMed] [Cross Ref]
205. De Souza P.L., Russell P.J., Kearsley J.H., Howes L.G. Clinical pharmacology of isoflavones and its relevance for potential prevention of prostate cancer. Nutr. Rev. 2010;68:542–555. doi: 10.1111/j.1753-4887.2010.00314.x. [PubMed] [Cross Ref]
206. Messina M.J. Emerging evidence on the role of soy in reducing prostate cancer risk. Nutr. Rev. 2003;61:117–131. doi: 10.1301/nr.2003.apr.117-131. [PubMed] [Cross Ref]
207. Sarkar F.H., Li Y.W. Soy isoflavones and cancer prevention. Cancer Investig. 2003;21:744–757. doi: 10.1081/CNV-120023773. [PubMed] [Cross Ref]
208. Yan L., Spitznagel E.L. Soy consumption and prostate cancer risk in men: A revisit of a meta-analysis. Am. J. Clin. Nutr. 2009;89:1155–1163. doi: 10.3945/ajcn.2008.27029. [PubMed] [Cross Ref]
209. Saxena A., Dhillon V.S., Shahid M., Khalil H.S., Rani M., Das T.P., Hedau S., Hussain A., Naqvi R.A., Deo S.V.S., et al. GSTP1 methylation and polymorphism increase the risk of breast cancer and the effects of diet and lifestyle in breast cancer patients. Exp. Ther. Med. 2012;4:1097–1103. [PMC free article] [PubMed]
210. Frassetto L.A., Todd K.M., Morris R.C., Jr., Sebastian A. Estimation of net endogenous noncarbonic acid production in humans from diet potassium and protein contents. Am. J. Clin. Nutr. 1998;68:576–583. [PubMed]
211. Welbourne T.C. Acid-base balance and plasma glutamine concentration in man. Eur. J. Appl. Physiol. Occup. Physiol. 1980;45:185–188. doi: 10.1007/BF00421326. [PubMed] [Cross Ref]
212. Gu C., Shi Y., Le G. Effect of dietary protein level and origin on the redox status in the digestive tract of mice. Int. J. Mol. Sci. 2008;9:464–475. doi: 10.3390/ijms9040464. [PMC free article] [PubMed] [Cross Ref]
213. Montonen J., Boeing H., Fritsche A., Schleicher E., Joost H.-G., Schulze M.B., Steffen A., Pischon T. Consumption of red meat and whole-grain bread in relation to biomarkers of obesity, inflammation, glucose metabolism and oxidative stress. Eur. J. Nutr. 2013;52:337–345. doi: 10.1007/s00394-012-0340-6. [PMC free article] [PubMed] [Cross Ref]
214. Wu G. Amino acids: Metabolism, functions, and nutrition. Amino Acids. 2009;37:1–17. doi: 10.1007/s00726-009-0269-0. [PubMed] [Cross Ref]
215. De Carvalho A.M., de Oliveira A.A.F., de Melo Loureiro A.P., Gattás G.J.F., Fisberg R.M., Marchioni D.M. Arginine intake is associated with oxidative stress in a general population. Nutrition. 2017;33:211–215. doi: 10.1016/j.nut.2016.07.005. [PubMed] [Cross Ref]
216. Ferguson L.R. Meat and cancer. Meat Sci. 2010;84:308–313. doi: 10.1016/j.meatsci.2009.06.032. [PubMed] [Cross Ref]
217. Dodson S., Baracos V.E., Jatoi A., Evans W.J., Cella D., Dalton J.T., Steiner M.S. Muscle wasting in cancer cachexia: Clinical implications, diagnosis, and emerging treatment strategies. Annu. Rev. Med. 2011;62:265–279. doi: 10.1146/annurev-med-061509-131248. [PubMed] [Cross Ref]
218. Bernstein A.M., Song M.Y., Zhang X.H., Pan A., Wang M.L., Fuchs C.S., Le N., Chan A.T., Willett W.C., Ogino S., et al. Processed and unprocessed red meat and risk of colorectal cancer: Analysis by tumor location and modification by time. PLoS ONE. 2015;10:e0135959 doi: 10.1371/journal.pone.0135959. [PMC free article] [PubMed] [Cross Ref]
219. Anand S.S., Hawkes C., de Souza R.J., Mente A., Dehghan M., Nugent R., Zulyniak M.A., Weis T., Bernstein A.M., Krauss R.M., et al. Food consumption and its impact on cardiovascular disease: Importance of solutions focused on the globalized food system: A report from the workshop convened by the world heart federation. J. Am. Coll. Cardiol. 2015;66:1590–1614. doi: 10.1016/j.jacc.2015.07.050. [PMC free article] [PubMed] [Cross Ref]
220. Ollberding N.J., Wilkens L.R., Henderson B.E., Kolonel L.N., Le Marchand L. Meat consumption, heterocyclic amines and colorectal cancer risk: The Multiethnic Cohort Study. Int. J. Cancer. 2012;131:E1125–E1133. doi: 10.1002/ijc.27546. [PMC free article] [PubMed] [Cross Ref]
221. Beresford S.A.A., Johnson K.C., Ritenbaugh C., Lasser N.L., Snetselaar L.G., Black H.R., Anderson G.L., Assaf A.R., Bassford T., Bowen D., et al. Low-fat dietary pattern and risk of colorectal cancer—The Women’s Health Initiative randomized controlled dietary modification trial. J. Am. Med. Assoc. 2006;295:643–654. doi: 10.1001/jama.295.6.643. [PubMed] [Cross Ref]
222. Schatzkin A., Lanza E., Corle D., Lance P., Iber F., Caan B., Shike M., Weissfeld J., Burt R., Cooper M.R., et al. Lack of effect of a low-fat, high-fiber diet on the recurrence of colorectal adenomas. N. Engl. J. Med. 2000;342:1149–1155. doi: 10.1056/NEJM200004203421601. [PubMed] [Cross Ref]
223. Lanza E., Schatzkin A., Daston C., Corle D., Freedman L., Ballard-Barbash R., Caan B., Lance P., Marshall J., Iber F., et al. Implementation of a 4-y, high-fiber, high-fruit-and-vegetable, low-fat dietary intervention: Results of dietary changes in the Polyp Prevention Trial. Am. J. Clin. Nutr. 2001;74:387–401. [PubMed]
224. Trapp D., Knez W., Sinclair W. Could a vegetarian diet reduce exercise-induced oxidative stress? A review of the literature. J. Sports Sci. 2010;28:1261–1268. doi: 10.1080/02640414.2010.507676. [PubMed] [Cross Ref]
225. Chen Q., Espey M.G., Sun A.Y., Pooput C., Kirk K.L., Krishna M.C., Khosh D.S., Drisko J., Levine M. Pharmacologic doses of ascorbate act as a prooxidant and decrease growth of aggressive tumor xenografts in mice. Proc. Natl. Acad. Sci. USA. 2008;105:11105–11109. doi: 10.1073/pnas.0804226105. [PubMed] [Cross Ref]
226. Uetaki M., Tabata S., Nakasuka F., Soga T., Tomita M. Metabolomic alterations in human cancer cells by vitamin C-induced oxidative stress. Sci. Rep. 2015;5:13896. doi: 10.1038/srep13896. [PMC free article] [PubMed] [Cross Ref]
227. Chen Q., Espey M.G., Krishna M.C., Mitchell J.B., Corpe C.P., Buettner G.R., Shacter E., Levine M. Pharmacologic ascorbic acid concentrations selectively kill cancer cells: Action as a pro-drug to deliver hydrogen peroxide to tissues. Proc. Natl. Acad. Sci. USA. 2005;102:13604–13609. doi: 10.1073/pnas.0506390102. [PubMed] [Cross Ref]
228. Du J.A., Martin S.M., Levine M., Wagner B.A., Buettner G.R., Wang S.H., Taghiyev A.F., Du C.B., Knudson C.M., Cullen J.J. Mechanisms of ascorbate-induced cytotoxicity in pancreatic cancer. Clin. Cancer Res. 2010;16:509–520. doi: 10.1158/1078-0432.CCR-09-1713. [PMC free article] [PubMed] [Cross Ref]
229. Chen P., Yu J., Chalmers B., Drisko J., Yang J., Li B.Y., Chen Q. Pharmacological ascorbate induces cytotoxicity in prostate cancer cells through ATP depletion and induction of autophagy. Anti-Cancer Drug. 2012;23:437–444. doi: 10.1097/CAD.0b013e32834fd01f. [PubMed] [Cross Ref]
230. Sharhar S., Normah H., Fatimah A., Fadilah R.N., Rohi G.A., Amin I., Cham B.G., Rizal R.M., Fairulnizal M.N. Antioxidant intake and status, and oxidative stress in relation to breast cancer risk: A case-control study. Asian Pac. J. Cancer Prev. 2008;9:343–349. [PubMed]
231. Xu X., Chen J. One-carbon metabolism and breast cancer: An epidemiological perspective. J. Genet. Genom. 2009;36:203–214. doi: 10.1016/S1673-8527(08)60108-3. [PMC free article] [PubMed] [Cross Ref]
232. Lajous M., Lazcano-Ponce E., Hernandez-Avila M., Willett W., Romieu I. Folate, vitamin B-6, and vitamin B-12 intake and the risk of breast cancer among Mexican women. Cancer Epidemiol. Biomark. Prev. 2006;15:443–448. doi: 10.1158/1055-9965.EPI-05-0532. [PubMed] [Cross Ref]
233. Bassett J.K., Severi G., Hodge A.M., Baglietto L., Hopper J.L., English D.R., Giles G.G. Dietary intake of B vitamins and methionine and prostate cancer incidence and mortality. Cancer Causes Control. 2012;23:855–863. doi: 10.1007/s10552-012-9954-5. [PubMed] [Cross Ref]
234. Glauert H.P., Calfee-Mason K., Stemm D.N., Tharappel J.C., Spear B.T. Dietary antioxidants in the prevention of hepatocarcinogenesis: A review. Mol. Nutr. Food Res. 2010;54:875–896. doi: 10.1002/mnfr.200900482. [PubMed] [Cross Ref]
235. Trottier G., Bostrom P.J., Lawrentschuk N., Fleshner N.E. Nutraceuticals and prostate cancer prevention: A current review. Nat. Rev. Urol. 2010;7:21–30. doi: 10.1038/nrurol.2009.234. [PubMed] [Cross Ref]
236. Sanchez G.V., Weinstein S.J., Stolzenberg-Solomon R.Z. Is dietary fat, vitamin D, or folate associated with pancreatic cancer? Mol. Carcinog. 2012;51:119–127. doi: 10.1002/mc.20833. [PMC free article] [PubMed] [Cross Ref]
237. Johnson J., de Mejia E.G. Dietary factors and pancreatic cancer: The role of food bioactive compounds. Mol. Nutr. Food Res. 2011;55:58–73. doi: 10.1002/mnfr.201000420. [PubMed] [Cross Ref]
238. Oberley L.W. Free radicals and diabetes. Free Radic. Biol. Med. 1988;5:113–124. doi: 10.1016/0891-5849(88)90036-6. [PubMed] [Cross Ref]
239. Niedzielska E., Smaga I., Gawlik M., Moniczewski A., Stankowicz P., Pera J., Filip M. Oxidative Stress in Neurodegenerative Diseases. Mol. Neurobiol. 2016;53:4094–4125. doi: 10.1007/s12035-015-9337-5. [PMC free article] [PubMed] [Cross Ref]
240. Sairazi N.S.M., Sirajudeen K., Asari M.A., Mummedy S., Muzaimi M., Sulaiman S.A. Effect of tualang honey against KA-induced oxidative stress and neurodegeneration in the cortex of rats. BMC Complement. Altern. Med. 2017;17:31 [PMC free article] [PubMed]
241. Lindqvist D., Dhabhar F.S., James S.J., Hough C.M., Jain F.A., Bersani F.S., Reus V.I., Verhoeven J.E., Epel E.S., Mahan L., et al. Oxidative stress, inflammation and treatment response in major depression. Psychoneuroendocrinology. 2017;76:197–205. doi: 10.1016/j.psyneuen.2016.11.031. [PubMed] [Cross Ref]
242. Kallaur A.P., Reiche E.M.V., Oliveira S.R., Simao A.N.C., Pereira W.L.D.J., Alfieri D.F., Flauzino T., Proenca C.D., Lozovoy M.A.B., Kaimen-Maciel D.R., et al. Genetic, immune-inflammatory, and oxidative stress biomarkers as predictors for disability and disease progression in multiple sclerosis. Mol. Neurobiol. 2017;54:31–44. doi: 10.1007/s12035-015-9648-6. [PubMed] [Cross Ref]
243. Carrier A. Metabolic syndrome and oxidative stress: A complex relationship. Antioxid. Redox Signal. 2017;26:429–431. doi: 10.1089/ars.2016.6929. [PubMed] [Cross Ref]
244. Ratneswaran A., Sun M.M.G., Dupuis H., Sawyez C., Borradaile N., Beier F. Nuclear receptors regulate lipid metabolism and oxidative stress markers in chondrocytes. J. Mol. Med. 2017;95:431–444. doi: 10.1007/s00109-016-1501-5. [PMC free article] [PubMed] [Cross Ref]
245. Doppler H., Storz P. Mitochondrial and Oxidative Stress-Mediated Activation of Protein Kinase D1 and its importance in Pancreatic Cancer. Front. Oncol. 2017;7:41. doi: 10.3389/fonc.2017.00041. [PMC free article] [PubMed] [Cross Ref]
246. Weber J., Zuehlsdorff T., Cole D., Di Antonio M., Bohndiek S. An Activatable Contrast Agent for Photoacoustic Imaging to Probe Oxidative Stress in Cancer. Proc. Physiol. Soc. 2016;36:C06.
247. Piskounova E., Agathocleous M., Murphy M., Hu Z.P., DeBerardinis R., Morrison S. Oxidative stress limits metastasis of human melanoma cells. Cancer Res. 2016;76:2806. doi: 10.1158/1538-7445.AM2016-2806. [Cross Ref]
248. Toyokuni S. Oxidative stress as an iceberg in carcinogenesis and cancer biology. Arch. Biochem. Biophys. 2016;595:46–49. doi: 10.1016/j.abb.2015.11.025. [PubMed] [Cross Ref]
249. Prasad S., Gupta S.C., Pandey M.K., Tyagi A.K., Deb L. Oxidative stress and cancer: Advances and challenges. Oxidative Med. Cell. Longev. 2016;2016:5010423. doi: 10.1155/2016/5010423. [PMC free article] [PubMed] [Cross Ref]
250. Gorrini C., Harris I.S., Mak T.W. Modulation of oxidative stress as an anticancer strategy. Nat. Rev. Drug Discov. 2013;12:931–947. doi: 10.1038/nrd4002. [PubMed] [Cross Ref]
251. DeNicola G.M., Karreth F.A., Humpton T.J., Gopinathan A., Wei C., Frese K., Mangal D., Yu K.H., Yeo C.J., Calhoun E.S., et al. Oncogene-induced Nrf2 transcription promotes ROS detoxification and tumorigenesis. Nature. 2011;475:106–109. doi: 10.1038/nature10189. [PMC free article] [PubMed] [Cross Ref]
252. Ramos-Gomez M., Kwak M.-K., Dolan P.M., Itoh K., Yamamoto M., Talalay P., Kensler T.W. Sensitivity to carcinogenesis is increased and chemoprotective efficacy of enzyme inducers is lost in Nrf2 transcription factor-deficient mice. Proc. Natl. Acad. Sci. USA. 2001;98:3410–3415. doi: 10.1073/pnas.051618798. [PubMed] [Cross Ref]
253. Iida K., Itoh K., Kumagai Y., Oyasu R., Hattori K., Kawai K., Shimazui T., Akaza H., Yamamoto M. Nrf2 is essential for the chemopreventive efficacy of oltipraz against urinary bladder carcinogenesis. Cancer Res. 2004;64:6424–6431. doi: 10.1158/0008-5472.CAN-04-1906. [PubMed] [Cross Ref]
254. Hayes J.D., McMahon M. The double-edged sword of Nrf2: Subversion of redox homeostasis during the evolution of cancer. Mol. Cell. 2006;21:732–734. doi: 10.1016/j.molcel.2006.03.004. [PubMed] [Cross Ref]
255. Hu X., Roberts J.R., Apopa P.L., Kan Y.W., Ma Q. Accelerated ovarian failure induced by 4-vinyl cyclohexene diepoxide in Nrf2 null mice. Mol. Cell. Biol. 2006;26:940–954. doi: 10.1128/MCB.26.3.940-954.2006. [PMC free article] [PubMed] [Cross Ref]
256. Xu C.J., Yuan X.L., Pan Z., Shen G.X., Kim J.H., Yu S.W., Khor T.O., Li W.G., Ma J.J., Kong A.N.T. Mechanism of action of isothiocyanates: The induction of ARE-regulated genes is associated with activation of ERK and JNK and the phosphorylation and nuclear translocation of Nrf2. Mol. Cancer Ther. 2006;5:1918–1926. doi: 10.1158/1535-7163.MCT-05-0497. [PubMed] [Cross Ref]
257. Ma Q. Role of Nrf2 in Oxidative Stress and Toxicity. Annu. Rev. Pharmacol. Toxicol. 2013;53:401–426. doi: 10.1146/annurev-pharmtox-011112-140320. [PMC free article] [PubMed] [Cross Ref]
258. Satoh T., McKercher S.R., Lipton S.A. Nrf2/ARE-mediated antioxidant actions of pro-electrophilic drugs. Free Radic. Biol. Med. 2013;65:645–657. doi: 10.1016/j.freeradbiomed.2013.07.022. [PMC free article] [PubMed] [Cross Ref]
259. Trachootham D., Alexandre J., Huang P. Targeting cancer cells by ROS-mediated mechanisms: A radical therapeutic approach? Nat. Rev. Drug Discov. 2009;8:579–591. doi: 10.1038/nrd2803. [PubMed] [Cross Ref]
260. Ranjan P., Anathy V., Burch P.M., Weirather K., Lambeth J.D., Heintz N.H. Redox-dependent expression of cyclin D1 and cell proliferation by Nox1 in mouse lung epithelial cells. Antioxid. Redox Signal. 2006;8:1447–1459. doi: 10.1089/ars.2006.8.1447. [PubMed] [Cross Ref]
261. Martindale J.L., Holbrook N.J. Cellular response to oxidative stress: Signaling for suicide and survival. J. Cell. Physiol. 2002;192:1–15. doi: 10.1002/jcp.10119. [PubMed] [Cross Ref]
262. Zhao W., Lu M.S., Zhang Q.W. Chloride intracellular channel 1 regulates migration and invasion in gastric cancer by triggering the ROS-mediated p38 MAPK signaling pathway. Mol. Med. Rep. 2015;12:8041–8047. doi: 10.3892/mmr.2015.4459. [PMC free article] [PubMed] [Cross Ref]
263. Wang P., Zeng Y., Liu T., Zhang C., Yu P.W., Hao Y.X., Luo H.X., Liu G. Chloride intracellular channel 1 regulates colon cancer cell migration and invasion through ROS/ERK pathway. World J. Gastroenterol. 2014;20:2071–2078. doi: 10.3748/wjg.v20.i8.2071. [PMC free article] [PubMed] [Cross Ref]
264. Shi Y., Nikulenkov F., Zawacka-Pankau J., Li H., Gabdoulline R., Xu J., Eriksson S., Hedström E., Issaeva N., Kel A. ROS-dependent activation of JNK converts p53 into an efficient inhibitor of oncogenes leading to robust apoptosis. Cell Death Differ. 2014;21:612–623. doi: 10.1038/cdd.2013.186. [PMC free article] [PubMed] [Cross Ref]
265. Shimura T., Sasatani M., Kamiya K., Kawai H., Inaba Y., Kunugita N. Mitochondrial reactive oxygen species perturb AKT/cyclin D1 cell cycle signaling via oxidative inactivation of PP2A in lowdose irradiated human fibroblasts. Oncotarget. 2016;7:3559–3570. [PMC free article] [PubMed]
266. Leslie N.R., Bennett D., Lindsay Y.E., Stewart H., Gray A., Downes C.P. Redox regulation of PI 3-kinase signalling via inactivation of PTEN. EMBO J. 2003;22:5501–5510. doi: 10.1093/emboj/cdg513. [PubMed] [Cross Ref]
267. Xu D., Rovira I.I., Finkel T. Oxidants painting the cysteine chapel: Redox regulation of PTPs. Dev. Cell. 2002;2:251–252. doi: 10.1016/S1534-5807(02)00132-6. [PubMed] [Cross Ref]
268. Sullivan L.B., Chandel N.S. Mitochondrial reactive oxygen species and cancer. Cancer Metab. 2014;2:17. doi: 10.1186/2049-3002-2-17. [PMC free article] [PubMed] [Cross Ref]
269. Harris I.S., Blaser H., Moreno J., Treloar A.E., Gorrini C., Sasaki M., Mason J.M., Knobbe C.B., Rufini A., Halle M., et al. PTPN12 promotes resistance to oxidative stress and supports tumorigenesis by regulating FOXO signaling. Oncogene. 2014;33:1047–1054. doi: 10.1038/onc.2013.24. [PubMed] [Cross Ref]
270. Shi X., Zhang Y., Zheng J., Pan J. Reactive oxygen species in cancer stem cells. Antioxid. Redox Signal. 2012;16:1215–1228. doi: 10.1089/ars.2012.4529. [PMC free article] [PubMed] [Cross Ref]
271. Diehn M., Cho R.W., Lobo N.A., Kalisky T., Dorie M.J., Kulp A.N., Qian D., Lam J.S., Ailles L.E., Wong M., et al. Association of reactive oxygen species levels and radioresistance in cancer stem cells. Nature. 2009;458:780–783. doi: 10.1038/nature07733. [PMC free article] [PubMed] [Cross Ref]
272. Schafer Z.T., Grassian A.R., Song L., Jiang Z., Gerhart-Hines Z., Irie H.Y., Gao S., Puigserver P., Brugge J.S. Antioxidant and oncogene rescue of metabolic defects caused by loss of matrix attachment. Nature. 2009;461:109–113. doi: 10.1038/nature08268. [PMC free article] [PubMed] [Cross Ref]
273. Dayem A.A., Choi H.Y., Kim J.H., Cho S.G. Role of oxidative stress in stem, cancer, and cancer stem cells. Cancers. 2010;2:859–884. doi: 10.3390/cancers2020859. [PMC free article] [PubMed] [Cross Ref]

Articles from International Journal of Molecular Sciences are provided here courtesy of Multidisciplinary Digital Publishing Institute (MDPI)