The primary structure of a basic (pI 9.0) fatty acid-binding protein from liver of Gallus domesticus

Amino Acid Sequence, Binding Properties and Evolutionary Relationships of the Basic Liver Fatty‐Acid‐Binding Protein from the Catfish Rhamdia sapo

“…Thrl02+Gln substitution in catfish basic L-FABP may account for the binding of only one fatty acid, possibly its steric effect may be increased, apart from the influence of other residues, by Ser100+His replacement. Scapin et al (1990) reported the three-dimensional structure of chicken basic L-FABP and placed the fatty acid carboxylate close to Lys29 (Ceciliani et al, 1994). Catfish basic L-FABP has the same residue in this position.…”

“…Although the chicken basic L-FABP is part of this subfamily, it has been suggested that it is unlikely to be the avian counterpart of mammalian L-FABP but the product of a separate gene (Ceciliani et al, 1994;Schleicher et al, 1995). Results presented in this study provide further support for this proposal.…”

A Single Amino Acid Mutation in Zebrafish (Danio rerio) Liver Bile Acid-binding Protein Can Change the Stoichiometry of Ligand Binding

“…More recently, an alternative nomenclature has been proposed, since it is well known that different FABP types can be present in the same tissue (7). In particular, in the liver of several vertebrates, two paralogous groups of FABPs have been described: the liver FABPs and another group that was initially called the liver "basic" FABPs and is currently referred to as the liver bile acid-binding proteins (L-BABPs) (8,9). The reason for this unusual nomenclature was that the isoelectric point of the first protein of this group that was described, chicken liver BABP, is 9.0, and although it was evident that this protein was different from the canonical liver FABP, its specific ligand was unknown (10).…”

Differential expression of L-FABP and L-BABP between fat and lean chickens

“…It is also involved in partitioning of FAs to different metabolic pathways (Storch and Corsico, 2008) and delivery of peroxisome proliferator-activated receptor ligands to the nucleus and the resulting modulation of target-gene expressions (Wolfrum et al, 2001). L-BABP is another kind of FABP in chicken liver, which shows higher amino acid sequence similarity to mammalian ileal-type FABP than that of L-FABP, and was formerly named liver basic type FABP (Sewell et al, 1989;Sams et al, 1991;Ceciliani et al, 1994). So far, L-BABP has never been found in mammalian species, but it has been identified and characterized in some vertebrates including fish, amphibians, reptiles, and birds (Ceciliani et al, 1994;Di Pietro et al, 1996Córdoba et al, 1999;Denovan-Wright et al, 2000;Ko et al, 2004;Jordal et al, 2006).…”

“…L-BABP is another kind of FABP in chicken liver, which shows higher amino acid sequence similarity to mammalian ileal-type FABP than that of L-FABP, and was formerly named liver basic type FABP (Sewell et al, 1989;Sams et al, 1991;Ceciliani et al, 1994). So far, L-BABP has never been found in mammalian species, but it has been identified and characterized in some vertebrates including fish, amphibians, reptiles, and birds (Ceciliani et al, 1994;Di Pietro et al, 1996Córdoba et al, 1999;Denovan-Wright et al, 2000;Ko et al, 2004;Jordal et al, 2006). Recent research on the structure of the L-BABP crystal showed that the capacity of L-BABP for binding to long-chain fatty acids is weak, but is strong for bile acid (Schievano et al, 1994;Beringhelli et al, 2001;Guariento et al, 2008), which is consistent with the presumption that the main function of L-BABP is to transport bile acids rather than fatty acids in chicken (Nichesola et al, 2004;Capaldi et al, 2006).…”