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1.  A comparison among the tissue-specific effects of aging and calorie restriction on TFAM amount and TFAM-binding activity to mtDNA in rat 
Biochimica et biophysica acta  2014;1840(7):2184-2191.
Background
Mitochondrial Transcription Factor A (TFAM) is regarded as a histone-like protein of mitochondrial DNA (mtDNA), performing multiple functions for this genome. Aging affects mitochondria in a tissue-specific manner and only calorie restriction (CR) is able to delay or prevent the onset of several age-related changes also in mitochondria.
Methods
Samples of the frontal cortex and soleus skeletal muscle from 6- and 26-month-old ad libitum-fed and 26-month-old calorie-restricted rats and of the livers from 18- and 28-month-old ad libitum-fed and 28-month-old calorie-restricted rats were used to detect TFAM amount, TFAM-binding to mtDNA and mtDNA content.
Results
We found an age-related increase in TFAM amount in the frontal cortex, not affected by CR, versus an age-related decrease in the soleus and liver, fully prevented by CR. The semi-quantitative analysis of in vivo binding of TFAM to specific mtDNA regions, by mtDNA immunoprecipitation assay and following PCR, showed a marked age-dependent decrease in TFAM-binding activity in the frontal cortex, partially prevented by CR. An age-related increase in TFAM-binding to mtDNA, fully prevented by CR, was found in the soleus and liver. MtDNA content presented a common age-related decrease, completely prevented by CR in the soleus and liver, but not in the frontal cortex.
Conclusions
The modulation of TFAM expression, TFAM-binding to mtDNA and mtDNA content with aging and CR showed a trend shared by the skeletal muscle and liver, but not by the frontal cortex counterpart.
General significance: Aging and CR appear to induce similar mitochondrial molecular mechanisms in the skeletal muscle and liver, different from those elicited in the frontal cortex.
doi:10.1016/j.bbagen.2014.03.004
PMCID: PMC4335656  PMID: 24631828
Mitochondrial Transcription Factor A; Mitochondrial Transcription Factor; A–mitochondrial deoxyribonucleic acid binding; Tissue-specificity; Aging rat; Calorie restriction
2.  Fat-1 transgenic mice with elevated omega-3 fatty acids are protected from allergic airway responses 
Biochimica et biophysica acta  2011;1812(9):1164-1169.
Omega-3 polyunsaturated fatty acids (n-3 PUFA) have been implicated in the alleviation of asthma. Recent studies have demonstrated that the n-3 PUFA derived lipid mediators, protectin D1 and resolvin E1, may act as potent resolution agonists in airway inflammation. The effects of the n-3 PUFA tissue status itself on asthma pathogenesis remains to be further investigated.
In this study allergic airway inflammation induced by allergen sensitization and aerosol challenge in Fat-1 and wild-type (WT) mice was investigated. Fat-1 transgenic mice displayed increased endogenous lung n-3 PUFA. When allergen-sensitized and aerosol-challenged, these animals had decreased airway inflammation with decreased leukocyte accumulation in bronchoalveolar lavage fluid (BALF) and lung parenchyma. The Fat-1 mice had a shift to the right in the dose-response relationship for methacholine induced bronchoconstriction with a significant increase in the log ED200. The Fat-1 mice had lower BALF concentrations of the pro-inflammatory cytokines IL-1α, IL-2, IL-5, IL-9, IL- 13, G-CSF, KC and RANTES. Furthermore, increased lung tissue amounts of the counter-regulatory mediators protectin D1 and resolvin E1 were found in Fat-1 mice after bronchoprovocative challenge.
These results therefore demonstrate a direct protective role for lung n-3 PUFA in allergic airway responses and an increased generation of protectin D1 and resolvin E1 in this context.
doi:10.1016/j.bbadis.2011.05.002
PMCID: PMC4325089  PMID: 21616147
Omega-3; resolvins; protectins; inflammation; asthma; Fat-1 mice
3.  Molecular and Bioenergetic Differences between Cells with African versus European Inherited Mitochondrial DNA Haplogroups: Implications for Population Susceptibility to Diseases 
Biochimica et biophysica acta  2013;1842(2):208-219.
The geographic origins of populations can be identified by their maternally inherited mitochondrial DNA (mtDNA) haplogroups. This study compared human cybrids (cytoplasmic hybrids), which are cell lines with identical nuclei but mitochondria from different individuals with mtDNA from either the H haplogroup or L haplogroup backgrounds. The most common European haplogroup is H while individuals of maternal African origin are of the L haplogroup. Despite lower mtDNA copy numbers, L cybrids had higher expression levels for nine mtDNA-encoded respiratory complex genes, decreased ATP turnover rates and lower levels of ROS production, parameters which are consistent with more efficient oxidative phosphorylation. Surprisingly, GeneChip arrays showed that the L and H cybrids had major differences in expression of genes of the canonical complement system (5 genes), dermatan/chondroitin sulfate biosynthesis (5 genes) and CCR3 signaling (9 genes). Quantitative nuclear gene expression studies confirmed that L cybrids had (a) lower expression levels of complement pathway and innate immunity genes and (b) increased levels of inflammation-related signaling genes, which are critical in human diseases. Our data support the hypothesis that mtDNA haplogroups representing populations from different geographic origins may play a role in differential susceptibilities to diseases.
doi:10.1016/j.bbadis.2013.10.016
PMCID: PMC4326177  PMID: 24200652
Mitochondrial haplogroups; transmitochondrial cybrids; inflammation; complement; mitochondria; complement activation; innate immunity; haplogroups; cybrids; retina
4.  THE INTEGRITY OF THE α-HELICAL DOMAIN OF INTESTINAL FATTY ACID BINDING PROTEIN IS ESSENTIAL FOR THE COLLISION-MEDIATED TRANSFER OF FATTY ACIDS TO PHOSPHOLIPID MEMBRANES 
Biochimica et biophysica acta  2008;1781(4):192-199.
Summary
Intestinal FABP (IFABP) and liver FABP (LFABP), homologous proteins expressed at high levels in intestinal absorptive cells, employ markedly different mechanisms of fatty acid transfer to acceptor model membranes. Transfer from IFABP occurs during protein-membrane-collisional interactions, while for LFABP transfer occurs by diffusion through the aqueous phase. In addition, transfer from IFABP is markedly faster than from LFABP. The overall goal of this study was to further explore the structural differences between IFABP and LFABP which underlie their large functional differences in ligand transport. In particular, we addressed the role of the αI-helix domain in the unique transport properties of intestinal FABP. A chimeric protein was engineered with the ‘body’ (ligand binding domain) of IFABP and the αI-helix of LFABP (α(I)LβIFABP), and the fatty acid transfer properties of the chimeric FABP were examined using a fluorescence resonance energy transfer assay. The results showed a significant decrease in the absolute rate of FA transfer from α(I)LβIFABP compared to IFABP. The results indicate that the αI-helix is crucial for IFABP collisional FA transfer, and further indicate the participation of the αII-helix in the formation of a protein-membrane “collisional complex”. Photo-crosslinking experiments with a photoactivable reagent demonstrated the direct interaction of IFABP with membranes and further supports the importance of the αI helix of IFABP in its physical interaction with membranes.
doi:10.1016/j.bbalip.2008.01.005
PMCID: PMC4319566  PMID: 18284926
fatty acid binding protein; fatty acid; chimeric proteins; lipid metabolism; small intestine; lipid transport
5.  [No title available] 
PMCID: PMC3766385  PMID: 23567800
6.  [No title available] 
PMCID: PMC3766491  PMID: 23648414
7.  [No title available] 
PMCID: PMC3770773  PMID: 23660153
8.  [No title available] 
PMCID: PMC3858408  PMID: 23668959
9.  [No title available] 
PMCID: PMC3858447  PMID: 23872352
10.  [No title available] 
PMCID: PMC3858512  PMID: 24021887
11.  [No title available] 
PMCID: PMC3867519  PMID: 23899502
12.  [No title available] 
PMCID: PMC3877165  PMID: 23680625
13.  [No title available] 
PMCID: PMC3877175  PMID: 23886914
14.  [No title available] 
PMCID: PMC3877202  PMID: 24071592
15.  [No title available] 
PMCID: PMC3877210  PMID: 23891718
16.  [No title available] 
PMCID: PMC3877419  PMID: 23732236
17.  [No title available] 
PMCID: PMC3901642  PMID: 24275510
18.  [No title available] 
PMCID: PMC3902145  PMID: 24269780
19.  [No title available] 
PMCID: PMC3905326  PMID: 24252613
20.  [No title available] 
PMCID: PMC3913072  PMID: 24296261
21.  [No title available] 
PMCID: PMC3915056  PMID: 24269842
22.  [No title available] 
PMCID: PMC3923981  PMID: 24286864
23.  [No title available] 
PMCID: PMC3925188  PMID: 24291127
24.  [No title available] 
PMCID: PMC3926667  PMID: 24275509
25.  [No title available] 
PMCID: PMC3928473  PMID: 24200678

Results 1-25 (2421)