Publication date: Available online 22 December 2015 Source:Journal of Clinical Lipidology
Author(s): Daiana Ibarretxe, Josefa Girona, Núria Amigó, Núria Plana, Raimón Ferré, Sandra Guaita, Roger Mallol, Mercedes Heras, Luis Masana
Background The role of circulating FABP5 on metabolic alterations is under active evaluation. On the other hand FABP5 SNPs (rs454550 and rs79370435) seem to modulate its effect. Objectives Our aim was to examine the role of circulating FABP5 levels and its main SNPs in atherogenic dyslipidemia (AD) assessed by 2D-NMR and related metabolic and inflammation markers. We hypothesized that circulating FABP5 may be a biomarker for metabolic risk. Methods We studied 459 subjects admitted to the metabolism unit because of lipid metabolism disturbances, and/or associated disorders. After a six-week lipid-lowering drug wash-out period, anamnesis and physical examination were performed. Carotid intimae-media thickness (cIMT) was measured by ultrasound. FABP5, FABP4, lipids, metabolic proteins and enzymes were determined by biochemical methods. The lipid profile was assessed by NMR. The rs454550 and rs79370435 FABP5 gene variants were also determined. Results The FABP5 plasma levels were positively correlated with adiposity, glucose metabolism and lipolysis parameters and were associated with AD, as assessed by NMR. There was a significant positive correlation between hsCRP and FABP5.The presence of type 2 diabetes, obesity, metabolic syndrome or AD was associated with higher FABP5 plasma levels (p< 0.005). The FABP5 concentrations, but not those of FABP4, were higher in patients with carotid plaques. FABP5 was a main determinant of plaque presence according to logistic regression analysis. The rare rs454550 allele was hyper-represented in non-obese subjects (p=0.011). Conclusions FABP5 is a biomarker of adiposity-associated metabolic derangements that include AD, thus underscoring the concomitant presence of inflammation. FABP5 is associated with increased subclinical atherosclerosis.
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[NMR paper] Mass spectrometry and NMR analysis of ligand binding by human liver fatty acid binding protein.
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Protein-ligand interactions are driven by many factors, including protein conformation and pH of the solution. Electrospray mass spectrometry can reveal the degree of protein folding from the distribution of...
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[NMR paper] Mass spectrometry and NMR analysis of ligand binding by human liver fatty acid binding protein.
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