Department of Biochemistry, School of Medicine, Niigata University, Niigata, Japan.
Proc Jpn Acad Ser B Phys Biol Sci. 2010;86(3):220-8. doi: 10.2183/pjab.86.220.
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. 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. Since then, extensive investigation of structures, functions and expressions has been carried out on a whole family of FABPs. Analyses of rat heart FABP; FABP1, FABP3 and alpha(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.
我们的同事和我已经确定了从小鼠肝脏中提取的与 LCFAs 具有高亲和力的低分子量细胞质 FABP(也称为 z 蛋白)的完整一级结构。同时,我们在 1982 年率先提出大鼠 FABP1、牛 FABP8(MP-2)、牛 CRBP 和大鼠 CRABP 构成一个蛋白质超家族。此后,对 FABP 全家族的结构、功能和表达进行了广泛的研究。对大鼠心脏 FABP、大鼠肾脏中表达的 FABP1、FABP3 和α2U-球蛋白、发现回肠 FABP6(I-15P)、以及首次将 FABP2 用作诊断标志物的应用也尤为突出。