Evidence for the Thr79Met polymorphism of the ileal fatty acid binding protein (FABP6) to be associated with type 2 diabetes in obese individuals

Grallert, Harald; Klapper, Maja; Pfäfflin, Albrecht; Schrezenmeir, Jürgen; Illig, Thomas; Boeing, Heiner; Döring, Frank

doi:10.1016/j.ymgme.2009.08.001

Cited by 14 publications

(12 citation statements)

References 31 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…In addition, FABP5 and FABP6 involved in the repressed PPAR signaling pathway were upregulated upon moderate PR. Both of them had been implicated in the diet‐induced insulin resistance . Additionally, glutathione metabolism and ascorbate metabolism were also altered upon moderate PR.…”

Section: Discussionmentioning

confidence: 99%

Integrated Remodeling of Gut–Liver Metabolism Induced by Moderate Protein Restriction Contributes to Improvement of Insulin Sensitivity

Zhang

Qiu

Wang

et al. 2018

Molecular Nutrition Food Res

View full text Add to dashboard Cite

show abstract

Section: Discussionmentioning

confidence: 99%

Integrated Remodeling of Gut–Liver Metabolism Induced by Moderate Protein Restriction Contributes to Improvement of Insulin Sensitivity

Zhang

Qiu

Wang

et al. 2018

Molecular Nutrition Food Res

View full text Add to dashboard Cite

show abstract

“…The Met allele of the Thr79Met substitution showed decreased risk for T2DM in a nested case-control study of 192 incident T2DM subjects and 384 controls from the European Prospective Investigation into Cancer and Nutrition (EPIC)-Potsdam cohort. The associative relationship for risk of T2DM and the Thr79Met SNP was further investigated in a larger cohort of 543 incident T2DM cases (EPIC-Potsdam cohort) and a case control study including 939 T2DM cases from the Co-operative Health Research in the Region Augsburg (KORA) [155]. The overall frequency of the homozygous rare ( Met79/Met79 ) allele was 16 per cent.…”

Section: The Human Fabp Gene Familymentioning

confidence: 99%

The human fatty acid-binding protein family: Evolutionary divergences and functions

2011

View full text Add to dashboard Cite

Fatty acid-binding proteins (FABPs) are members of the intracellular lipid-binding protein (iLBP) family and are involved in reversibly binding intracellular hydrophobic ligands and trafficking them throughout cellular compartments, including the peroxisomes, mitochondria, endoplasmic reticulum and nucleus. FABPs are small, structurally conserved cytosolic proteins consisting of a water-filled, interior-binding pocket surrounded by ten anti-parallel beta sheets, forming a beta barrel. At the superior surface, two alpha-helices cap the pocket and are thought to regulate binding. FABPs have broad specificity, including the ability to bind long-chain (C16-C20) fatty acids, eicosanoids, bile salts and peroxisome proliferators. FABPs demonstrate strong evolutionary conservation and are present in a spectrum of species including Drosophila melanogaster, Caenorhabditis elegans, mouse and human. The human genome consists of nine putatively functional protein-coding FABP genes. The most recently identified family member, FABP12, has been less studied.

show abstract

“…Within hepatocytes, BAs undergo carrier‐mediated transport after binding to cytosolic proteins such as BABPs . The involvement of BABPs as BA cytosolic transporters is well illustrated by recent findings suggesting that a protein of the family, defective of BA binding activity, would cause BA malabsorption with consequent increased resistance to type 2 diabetes in obese individuals . BAs are key signalling molecules and have a prominent role in energy homeostasis but they can exert toxic responses when they accumulate in hepatocytes .…”

Section: Introductionmentioning

confidence: 99%

Lipid binding protein response to a bile acid library: a combined NMR and statistical approach

et al. 2015

View full text Add to dashboard Cite

Primary bile acids, differing in hydroxylation pattern, are synthesized from cholesterol in the liver and, once formed, can undergo extensive enzyme‐catalysed glycine/taurine conjugation, giving rise to a complex mixture, the bile acid pool. Composition and concentration of the bile acid pool may be altered in diseases, posing a general question on the response of the carrier (bile acid binding protein) to the binding of ligands with different hydrophobic and steric profiles. A collection of NMR experiments (H/D exchange, HET‐SOFAST, ePHOGSY NOESY/ROESY and 15N relaxation measurements) was thus performed on apo and five different holo proteins, to monitor the binding pocket accessibility and dynamics. The ensemble of obtained data could be rationalized by a statistical approach, based on chemical shift covariance analysis, in terms of residue‐specific correlations and collective protein response to ligand binding. The results indicate that the same residues are influenced by diverse chemical stresses: ligand binding always induces silencing of motions at the protein portal with a concomitant conformational rearrangement of a network of residues, located at the protein anti‐portal region. This network of amino acids, which do not belong to the binding site, forms a contiguous surface, sensing the presence of the bound lipids, with a signalling role in switching protein–membrane interactions on and off.

show abstract

Evidence for the Thr79Met polymorphism of the ileal fatty acid binding protein (FABP6) to be associated with type 2 diabetes in obese individuals

Cited by 14 publications

References 31 publications

Integrated Remodeling of Gut–Liver Metabolism Induced by Moderate Protein Restriction Contributes to Improvement of Insulin Sensitivity

Integrated Remodeling of Gut–Liver Metabolism Induced by Moderate Protein Restriction Contributes to Improvement of Insulin Sensitivity

The human fatty acid-binding protein family: Evolutionary divergences and functions

Lipid binding protein response to a bile acid library: a combined NMR and statistical approach

Contact Info

Product

Resources

About