Disease relevance of LOC395345

• The structure of this liver protein appears very similar to that of the Escherichia coli derived rat intestinal FABP recently determined by X-ray diffraction methods [1].
• In these studies we show that transcriptional co-repression of the two lipid transfer proteins, liver fatty acid-binding protein (L-FABP) and MTP, which cooperatively shunt fatty acids into de novo synthesized glycerolipids and the transfer of lipids into VLDL, respectively, act together to maintain hepatic lipid homeostasis [2].
• FAO rat hepatoma cells express L-FABP and MTP and demonstrate the ability to assemble and secrete VLDL [2].

High impact information on LOC395345

• In contrast, L35 cells, derived as a single cell clone from FAO cells, do not express L-FABP or MTP nor do they assemble and secrete VLDL [2].
• Chicken liver bile acid-binding protein (formerly known as chicken liver basic fatty acid-binding protein) binds to anionic lipid membranes acquiring a partly folded state [Nolan, V., Perduca, M., Monaco, H., Maggio, B., and Montich, G. (2003) Biochim. Biophys. Acta 1611, 98-106] [3].
• Crystal structure of chicken liver basic fatty acid-binding protein complexed with cholic acid [4].
• The structure of Lb-FABP has been solved by (1)H NMR [5].
• Competition studies between cis-parinaric acid and the natural ligands indicated a decreasing affinity of chicken Lb-FABP for PA, OA, and retinoic acid (RA) [6].

Biological context of LOC395345

• The tissue distribution of this protein in embryonic and hatched chicks was determined using polyclonal antiserum prepared against this FABP [7].
• The molecular modeling of lungfish Lb-FABP predicts that nine of the conserved residues of Lb-FABPs are oriented toward the binding cavity, thus suggesting they are related to the protein binding characteristics [8].
• It seems FABP might play a role in lipid metabolism by interacting with membrane bound enzymes [9].
• The liver-type FABP constitutes 69% of the total FABPs, and its amino acid sequence presents the highest identity with chicken, catfish, iguana and elephant fish liver basic FABPs [10].
• The open-reading frame of the zebrafish FABP cDNA codes for a protein of 14.0 kDa with a calculated isoelectric point of 8 [11].

Anatomical context of LOC395345

• Chicken liver bile acid-binding protein is in a compact partly folded state at acidic pH. Its relevance to the interaction with lipid membranes [3].
• In the mature retina, this function is apparently not needed, because there is little staining of the retina in adults but obvious immunoreactivity in the ciliary epithelium, implying some other role for FABP in this tissue [7].
• FABP present in liver, heart, intestinal mucosa and omental fat responds to different diets [9].
• The mucosa of the mesenteric intestine of the chicken has been found to contain a fatty acid binding protein (FABP) with a molecular weight of less than 12,400 [12].
• The results indicated that the L-FABP gene polymorphisms were associated with abdominal fat weight and percentage of abdominal fat, and the L-FABP gene could be a candidate locus or linked to a major gene(s) that affects fatness traits in the chicken [13].

Associations of LOC395345 with chemical compounds

• The protein binds one molecule of oleic acid in a position that is significantly different from that of either of the two molecules that bind to rat liver FABP [14].
• The stoichiometry of binding of cholate is of two ligands per protein molecule, as observed in chicken L-BABP [14].
• The L-FABP protein has low affinity for palmitic and oleic acids and high affinity for linoleic and arachidonic acids and other hydrophobic ligands, all of them important for the metabolic functions of the liver [10].
• A high level of dietary fat or dietary supplementation with sodium taurocholate increased the concentration of FABP in the intestine [15].
• At hatching, the concentration of fatty acid binding protein (FABP) in the intestine of the broiler-type chicks was significantly less than in the New Hampshire and White Leghorn chicks [15].

Analytical, diagnostic and therapeutic context of LOC395345

• The three-dimensional structure of chicken liver basic fatty acid-binding protein has been determined at 2.7 A resolution by X-ray crystallography [1].
• FABP was purified by column chromatography and native gel electrophoresis; denaturing gel electrophoresis and isoelectric focusing were used to characterize the protein [7].
• Using fluorescence spectroscopy of the single Trp residue, circular dichroism in the far- and near-UV, Fourier transform infrared spectroscopy, and size-exclusion chromatography, we found that L-BABP was partly unfolded at pH 2.5 and low ionic strength, retaining some of its secondary structure [3].
• Tissue distribution of retinal FABP was determined by immunoblotting and localization of FABP in eyes of E15 and adult chickens was studied by immunohistochemistry on paraffin sections [7].
• In adult retinas, FABP is barely detectable on a Western blot [16].

References