Geese W J, Raftogianis R B
Department of Pharmacology, Fox Chase Cancer Center, 7701 Burholme Avenue, Philadelphia, PA 19111, USA.
Biochem Biophys Res Commun. 2001 Oct 19;288(1):280-9. doi: 10.1006/bbrc.2001.5746.
The human hydroxysteroid sulfotransferase (SULT) family is comprised of two subfamilies, SULT2A1 and SULT2B1. We characterized the substrate specificity, in vitro biochemical properties, and tissue distribution patterns of human SULT2B1a and SULT2B1b. In contrast to the wide substrate specificity of SULT2A1, SULT2B1a and SULT2B1b specifically catalyzed the sulfonation of 3beta-hydroxysteroids with high catalytic efficiency. Both SULT2B1 enzymes also sulfonated dihydrotestosterone. In vitro studies revealed that the biochemical properties of SULT2B1a and SULT2B1b were not significantly different from each other. However, tissue expression analysis suggested that they are differentially regulated. In contrast to the limited tissue distribution of SULT2A1, SULT2B1 was detected in a variety of hormone-responsive tissues including placenta, ovary, uterus, and prostate. The catalytic activity toward dehydroepiandrosterone and dihydrotestosterone, biologically important androgens, coupled with expression in prostate suggests that SULT2B1 may play a novel regulatory role that protects against the mitogenic effects of androgens.
人类羟基类固醇硫酸转移酶（SULT）家族由两个亚家族组成，即SULT2A1和SULT2B1。我们对人类SULT2B1a和SULT2B1b的底物特异性、体外生化特性及组织分布模式进行了表征。与SULT2A1广泛的底物特异性不同，SULT2B1a和SULT2B1b特异性催化3β-羟基类固醇的硫酸化反应，且催化效率很高。两种SULT2B1酶还能使双氢睾酮硫酸化。体外研究表明，SULT2B1a和SULT2B1b的生化特性彼此间无显著差异。然而，组织表达分析表明它们受到不同的调控。与SULT2A1有限的组织分布不同，在包括胎盘、卵巢、子宫和前列腺在内的多种激素反应性组织中均检测到了SULT2B1。对脱氢表雄酮和双氢睾酮（具有重要生物学意义的雄激素）的催化活性，以及在前列腺中的表达表明，SULT2B1可能发挥一种新的调节作用，以抵御雄激素的促有丝分裂作用。
Zotero 插件