Initial studies of the cytoplasmic FABP superfamily

Abstract

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.

(Communicated by Tamio YAMAKAWA, M.J.A.)