Studies of the FABP family: a retrospective.
Following my research on the role played by soluble proteins in their function as hydrophobic ligand carriers acting through squalene epoxidase, Dr Odani and I started to work together on low molecular lipid binding proteins. As a result of this collaboration, in 1982 we managed to determine the complete primary structure of Z-protein in rat liver. This was the first report ever to give the complete amino acid sequence of a fatty acid binding protein (FABP). This gave momentum to further such research, and now extensive exploration has been carried out on a whole family of homologous intracellular hydrophobic ligand binding proteins, the product of the expression of an ancient gene family in numerous organisms. Takahashi et al. have determined the primary structures of mammalian FABP family protein in liver, intestine, heart, kidney, and skin through amino acid sequencing as well as through determination of the cDNA sequence. Out of all my research on the FABP family, I believe, my initial study on FABP in liver, my work on kidney FABP, heart type FABP and my discovery of an I-15P (BAPB) and I-FABP application as a diagnostic marker stand out in particular.
Ono
Teruo
T
Department of Dairy Science, Laboratory of Clinical Nutrition, Rakuno Gakuen University, 582-1 Midorimachi Bunkyodai, Ebetsu, 069-8501, Japan, onoteruo@rakuno.ac.jp
D000595:Amino Acid Sequence; D000818:Animals; D015415:Biomarkers; D002417:Cattle; D050556:Fatty Acid-Binding Proteins / Q000737:chemistry*; D006801:Humans; D007668:Kidney / Q000378:metabolism; D051379:Mice; D008969:Molecular Sequence Data; D015394:Molecular Structure; D011401:Promoter Regions, Genetic; D051381:Rats; D017386:Sequence Homology, Amino Acid
D015415:Biomarkers; D050556:Fatty Acid-Binding Proteins