Structural and biochemical characterization and evolutionary relationships of the fatty acid-binding protein 10 (Fabp10) of hake (Merluccius hubbsi)

Fish Physiol Biochem. 2016 Feb;42(1):149-65. doi: 10.1007/s10695-015-0126-x. Epub 2015 Sep 14.

Abstract

A fatty acid-binding protein (FABP) from the liver of Argentine hake (Merluccius hubbsi) was isolated and characterized and its expression analyzed. The determination of its partial primary structures (72%) showed that it presents highest identity with Fabp10, commonly termed liver basic-type FABP. The evolutionary tree showed greater relationship between the Fabp10 of hake (Me Fabp10) and the Fabp10 and the Fabp10a of teleost fish. Me Fabp10 had low affinity for palmitic, oleic and palmitoleic acid and high affinity for bilirubin, lysophosphatidylcholine and lysophosphatidylethanolamine, all of them important in the metabolic functions of the liver. Me Fabp10 was able to bind only one cis-parinaric acid molecule and was found to be expressed only in the liver.

Keywords: Fabp10; Fatty acid-binding protein; Hake; Liver.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Evolution, Molecular
  • Fatty Acid-Binding Proteins* / genetics
  • Fatty Acid-Binding Proteins* / metabolism
  • Female
  • Fish Proteins* / genetics
  • Fish Proteins* / metabolism
  • Gadiformes* / genetics
  • Gadiformes* / metabolism
  • Lipid Metabolism / genetics
  • Liver / metabolism
  • Molecular Sequence Data
  • Phylogeny

Substances

  • Fatty Acid-Binding Proteins
  • Fish Proteins