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Human FABP1 Protein expressed in Wheat germ - ABIN1353338
Bronsky, Karpísek, Bronská, Pechová, Jancíková, Kotolová, Stejskal, Prusa, Nevoral: Adiponectin, adipocyte fatty acid binding protein, and epidermal fatty acid binding protein: proteins newly identified in human breast milk. in Clinical chemistry 2006
Show all 2 Pubmed References
CDH5 (show CDH5 Proteins) and FABP1 expression levels were both elevated in drug-induced liver injury.
A high resolution NMR comparative molecular analysis of L-FABP T94T and L-FABP T94A in their unbound states and in the presence of representative ligands of the fatty acid and bile acid classes showed that threonine to alanine replacement did not result in strongly perturbed structural and dynamic features, although differences in oleic acid binding by the two variants were detected.
Studies show that despite overall tertiary structure similarity, the hFABP1 differs significantly from rat FABP1 in secondary structure, much larger ligand binding cavity, and affinities/specificities for some ligands. Moreover, while both mouse and hFABP1 mediate ligand induction of PPARA (show PPARA Proteins), they differ markedly in genes induced. hFABP1 T94A variant is associated with altered body mass index.[review]
Urinary L-FABP, NGAL (show LCN2 Proteins), Kim-1 (show HAVCR1 Proteins) and albumin (show ALB Proteins) levels increased during the acute phase of kidney injury and were significantly correlated with the degree of tubulointerstitial fibrosis during the chronic phase. These markers could detect higher risk of progression to CKD.
L-FABP was found to associate with VEGFR2 on membrane rafts and subsequently activate the Akt/mTOR/P70S6K/4EBP1 and Src/FAK/cdc42 pathways, which resulted in up-regulation of VEGF-A accompanied by an increase in both angiogenic potential and migration activity. L-FABP significantly promoted tumor growth and metastasis in a xenograft mouse model.
In chronic kidney disease, high urinary L-FABP correlated with the development of end-stage renal disease and cardiovascular disease.
In the association of SNPs in FABP1 gene with PCOS, rs2197076 was more closely associated with its main features than rs2241883 and seemed to play a more important role in the pathogenesis of PCOS.
Urinary L-FABP appears to be a sensitive biomarker of acute kidney injury in patients undergoing abdominal aortic repair.
Urinary levels of NGAL (show LCN2 Proteins) are more sensitive than uKIM-1 and uL-FABP (show FABP2 Proteins) levels in predicting renal scarring in vesicoureteral reflux.
Loss of staining for LFABP appears to be common in hepatocellular carcinoma and may be seen in well-differentiated hepatocellular carcinoma.
Individually ablating SCPx (show SCP2 Proteins) or SCP2/SCPx (show SCP2 Proteins) elicited concomitant upregulation of L-FABP.
Lack of a significant decrease in the flux of HDL-[(3)H]CE to biliary FC or bile acids in FABP1(-/-) mice indicates the likely compensation of its function by an as yet unidentified mechanism. Taken together, these studies demonstrate that FABP1 and SCP2 facilitate the preferential movement of HDL-CEs to bile for final elimination
data showed that Fabp1 gene ablation markedly diminished the impact of high-fat diet on brain endocannabinoid levels, especially in male mice
Studies show that despite overall tertiary structure similarity, the hFABP1 differs significantly from rat FABP1 in secondary structure, much larger ligand binding cavity, and affinities/specificities for some ligands. Moreover, while both mouse and hFABP1 mediate ligand induction of PPARA (show PPARA Proteins), they differ markedly in genes induced.
FABP1 knockout increased brain levels of arachidonic acid-containing endocannabinoids
L-FABP was more important in hepatic retention of bile acids, while SCP-2/SCP-x (show SCP2 Proteins) more broadly affected biliary bile acid and phospholipid levels.
These findings suggest that some of the phenotypic divergence between the two L-Fabp(-/-) lines may reflect unanticipated differences in genetic background, underscoring the importance of genetic background in phenotypic characterization.
Loss of L-FABP and SCP-2 (show CRISP3 Proteins), or both induces hepatic lipid accumulation in female mice and mimics non-alcoholic fatty liver disease.
L-FABP appears to function more in hepatic retention of bile acids as well as hepatic uptake and biliary secretion of HDL (show HSD11B1 Proteins)-cholesterol
L-FABP is not required to channel ATGL (show PNPLA2 Proteins)-hydrolyzed FAs (show FAS Proteins) to mitochondria for beta-oxidation or the nucleus for PPAR-alpha (show PPARA Proteins) regulation
combinatorial interactions between multiple regulatory factors are responsible for the gene expression of L-FABP in the liver
This gene encodes the fatty acid binding protein found in liver. Fatty acid binding proteins are a family of small, highly conserved, cytoplasmic proteins that bind long-chain fatty acids and other hydrophobic ligands. This protein and FABP6 (the ileal fatty acid binding protein) are also able to bind bile acids. It is thought that FABPs roles include fatty acid uptake, transport, and metabolism.
fatty acid-binding protein 1
, fatty acid-binding protein, liver
, liver-type fatty acid-binding protein
, 14 kDa selenium-binding protein
, fatty acid binding protein liver
, squalene- and sterol-carrier protein
, fatty acid binding protein 1, liver
, fafatty acid binding protein 1, liver
, fatty acid-binding protein
, liver fatty acid binding protein
, fatty acid binding protein 1-A, liver
, LOW QUALITY PROTEIN: fatty acid-binding protein, liver