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 CR...
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Veröffentlicht in: | Proceedings of the Japan Academy, Series B Series B, 2010, Vol.86(3), pp.220-228 |
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Zusammenfassung: | 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 α2U-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.) |
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ISSN: | 0386-2208 1349-2896 |
DOI: | 10.2183/pjab.86.220 |