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1.  Use of Host- and Bacteria-Derived Salivary Markers in Detection of Periodontitis: A Cumulative Approach 
Disease markers  2011;30(6):299-305.
In the present study, we propose a novel diagnostic approach, using 3 different salivary markers, representing periodontal pathogen burden, inflammation, and tissue degradation, for detecting periodontitis. The salivary concentrations of Porphyromonas gingivalis, interleukin-1β, and matrix metalloproteinase-8, available from salivary specimens of 165 subjects (84 subjects with advanced periodontitis and 81 controls), were calculated together to obtain a cumulative risk score (CRS). In the calculation of CRS, the concentrations of each marker were divided into tertiles, and cumulative sub-score per each subject were calculated by the multiplication of the tertile values. Three CRS groups, indicating the lowest, medium, or highest risk, were formed with the cumulative sub-scores. Logistic regression analysis and ROC curves were performed to study the association of CRS with periodontitis. The results indicate that CRS, calculated from the 3 salivary biomarkers, is associated with advanced periodontitis more strongly than any of the markers individually. CRS offers a novel, non-invasive model for advanced periodontitis risk categorization that is especially useful in large population surveys where a periodontal examination is not feasible.
PMCID: PMC3825247  PMID: 21725158
IL-1β; MMP-8; Porphyromonas gingivalis; risk score; saliva
2.  Chlamydial and Periodontal Pathogens Induce Hepatic Inflammation and Fatty Acid Imbalance in Apolipoprotein E-Deficient Mice▿  
Infection and Immunity  2009;77(8):3442-3449.
Periodontitis and Chlamydia pneumoniae infection are independent risk factors for cardiovascular diseases. The aim of this study was to investigate the effect of C. pneumoniae and Aggregatibacter actinomycetemcomitans infection on hepatic inflammation and lipid homeostasis of apolipoprotein E-deficient mice. Mice were infected with viable C. pneumoniae intranasally three times for chronic infection or once for acute infection. Viable A. actinomycetemcomitans was administered 10 times intravenously alone or in concert with C. pneumoniae. Hepatic alterations were assessed by histochemistry, lipid quantification, and fatty acid profile analysis. The RNA expression levels and the presence of pathogens in the livers and lungs were detected by quantitative real-time PCR. Both pathogens were detected in the livers of the infected animals. Chronic C. pneumoniae infection induced marked changes in hepatic lipid homeostasis. A. actinomycetemcomitans infection resulted in inflammatory cell infiltration into the liver, accompanied by elevated hepatic RNA expression levels of inflammation-related genes and higher serum amyloid A and lipopolysaccharide concentrations. Our results indicate that proatherogenic pathogens infect the liver, causing proinflammatory alterations and lipid disturbances. This infection may maintain chronic systemic inflammation attributable to atherogenesis.
PMCID: PMC2715688  PMID: 19451238
3.  A Cytosolic Splice Variant of Cab45 Interacts with Munc18b and Impacts on Amylase Secretion by Pancreatic Acini 
Molecular Biology of the Cell  2007;18(7):2473-2480.
We identified in a yeast two-hybrid screen the EF-hand Ca2+-binding protein Cab45 as an interaction partner of Munc18b. Although the full-length Cab45 resides in Golgi lumen, we characterize a cytosolic splice variant, Cab45b, expressed in pancreatic acini. Cab45b is shown to bind 45Ca2+, and, of its three EF-hand motifs, EF-hand 2 is demonstrated to be crucial for the ion binding. Cab45b is shown to interact with Munc18b in an in vitro assay, and this interaction is enhanced in the presence of Ca2+. In this assay, Cab45b also binds the Munc18a isoform in a Ca2+-dependent manner. The endogenous Cab45b in rat acini coimmunoprecipitates with Munc18b, syntaxin 2, and syntaxin 3, soluble N-ethylmaleimide-sensitive factor attachment protein receptors with key roles in the Ca2+-triggered zymogen secretion. Furthermore, we show that Munc18b bound to syntaxin 3 recruits Cab45b onto the plasma membrane. Importantly, antibodies against Cab45b are shown to inhibit in a specific and dose-dependent manner the Ca2+-induced amylase release from streptolysin-O–permeabilized acini. The present study identifies Cab45b as a novel protein factor involved in the exocytosis of zymogens by pancreatic acini.
PMCID: PMC1924827  PMID: 17442889

Results 1-3 (3)