Initial studies of the cytoplasmic FABP superfamily

Our colleagues and we have determined the complete primary structure of a low molecular weight cytoplasmic FABP (also known as z-protein) that binds to LCFAs with high affinities, obtained from rat liver.(1)) At the same time, we were the first to propose that rat FABP1, bovine FABP8 (MP-2), bovine CRBP and rat CRABP constituted a protein superfamily in 1982.(2)) Since then, extensive investigation of structures, functions and expressions has been carried out on a whole family of FABPs.(3))(–)(5)) Analyses of rat heart FABP; FABP1, FABP3 and α(2U)-globulin expressed in rat kidney; discovery of ileal FABP6 (I-15P); and first application of FABP2 as a diagnostic marker also stand out in particular.