Suppr超能文献

人3β-羟基类固醇磺基转移酶(SULT2B1a和SULT2B1b)的表达与特性分析

Expression and characterization of the human 3 beta-hydroxysteroid sulfotransferases (SULT2B1a and SULT2B1b).

作者信息

Meloche C A, Falany C N

机构信息

Department of Pharmacology and Toxicology, University of Alabama at Birmingham, Room G133M, Volker Hall, 1670 University Boulevard, Birmingham, AL 35294, USA.

出版信息

J Steroid Biochem Mol Biol. 2001 Jun;77(4-5):261-9. doi: 10.1016/s0960-0760(01)00064-4.

Abstract

The human hydroxysteroid sulfotransferase, dehydroepiandrosterone sulfotransferase (DHEA-ST), is highly expressed in liver and adrenal cortex and displays reactivity towards a broad range of hydroxysteroids including 3 beta-hydroxysteroids, 3 alpha-hydroxysteroids, estrogens with a 3-phenolic moiety, and 17-hydroxyl group of androgens. In contrast, characterization of the newly described human hydroxysteroid sulfotransferase SULT2B1 isoforms shows that these enzymes are selective for the sulfation of 3 beta-hydroxysteroids, such as pregnenolone, epiandrosterone, DHEA, and androstenediol. There was no activity detected towards testosterone, dexamethasone, beta-estradiol, androsterone, or p-nitrophenol. The SULT2B1 gene encodes two isoforms, SULT2B1a and SULT2B1b, which are generated by alternate splicing of the first exon; therefore the SULT2B1 isoforms differ at their N-terminals. Northern Blot analysis detected a SULT2B1 message in RNA isolated from the human prostate and placenta. No SULT2B1 message was observed in RNA isolated from human liver, colon, lung, kidney, brain, or testis tissue. Purified SULT2B1a was used to generate a specific rabbit polyclonal anti-SULT2B1 antibody. The anti-SULT2B1 antibody did not react with expressed human EST, P-PST-1, M-PST, DHEA-ST, or ST1B2, during immunoblot analysis. The substrate specificity of the expressed SULT2B1 isoforms suggests that these enzymes are capable of regulating the activity of adrenal androgens in human tissues via their inactivation by sulfation.

摘要

人类羟基类固醇硫酸转移酶,脱氢表雄酮硫酸转移酶(DHEA - ST),在肝脏和肾上腺皮质中高度表达,对多种羟基类固醇具有反应活性,包括3β - 羟基类固醇、3α - 羟基类固醇、具有3 - 酚基部分的雌激素以及雄激素的17 - 羟基。相比之下,新描述的人类羟基类固醇硫酸转移酶SULT2B1亚型的特性表明,这些酶对3β - 羟基类固醇的硫酸化具有选择性,如孕烯醇酮、表雄酮、脱氢表雄酮和雄烯二醇。未检测到对睾酮、地塞米松、β - 雌二醇、雄酮或对硝基苯酚的活性。SULT2B1基因编码两种亚型,SULT2B1a和SULT2B1b,它们由第一个外显子的可变剪接产生;因此,SULT2B1亚型在其N端不同。Northern印迹分析在从人前列腺和胎盘中分离的RNA中检测到SULT2B1信息。在从人肝脏、结肠、肺、肾、脑或睾丸组织中分离的RNA中未观察到SULT2B1信息。纯化的SULT2B1a用于产生特异性兔多克隆抗SULT2B1抗体。在免疫印迹分析中,抗SULT2B1抗体与表达的人EST、P - PST - 1、M - PST、DHEA - ST或ST1B2不发生反应。表达的SULT2B1亚型的底物特异性表明,这些酶能够通过硫酸化使其失活来调节人体组织中肾上腺雄激素的活性。

文献AI研究员

20分钟写一篇综述,助力文献阅读效率提升50倍。

立即体验

用中文搜PubMed

大模型驱动的PubMed中文搜索引擎

马上搜索

文档翻译

学术文献翻译模型,支持多种主流文档格式。

立即体验