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大鼠肝脏3α-羟基类固醇/二氢二醇脱氢酶cDNA的克隆与测序

Cloning and sequencing of the cDNA for rat liver 3 alpha-hydroxysteroid/dihydrodiol dehydrogenase.

作者信息

Pawlowski J E, Huizinga M, Penning T M

机构信息

Department of Pharmacology, University of Pennsylvania School of Medicine, Philadelphia 19104-6084.

出版信息

J Biol Chem. 1991 May 15;266(14):8820-5.

PMID:1840601
Abstract

Rat liver 3 alpha-hydroxysteroid dehydrogenase (3 alpha-HSD, EC 1.1.1.50) is an NAD(P)(+)-dependent oxidoreductase which will terminate androgen action by converting 5 alpha-dihydrotestosterone to 3 alpha-androstanediol. It is identical to dihydrodiol dehydrogenase and it can function as a 9-, 11-, and 15-hydroxyprostaglandin dehydrogenase. Its reactions are potently inhibited by the nonsteroidal anti-inflammatory drugs (NSAIDs). A cDNA (2.1 kilobases) for 3 alpha-HSD was cloned from a rat liver cDNA expression library in lambda gt11. Portions of the cDNA insert which contained an internal EcoRI site were subcloned into pGEM3, and dideoxysequencing revealed that the cDNA contains an open reading frame of 966 nucleotides which encode a protein of 322 amino acids with a monomer Mr of 37,029. The identity of this clone was confirmed by locating two tryptic peptides and two endoproteinase Lys-C peptides from purified 3 alpha-HSD within the nucleotide sequence. The amino acid sequence of rat liver 3 alpha-HSD bears no significant homology with 3 beta-, 17 beta- or 11 beta-hydroxysteroid dehydrogenases but has striking homology with bovine lung prostaglandin F synthase (69% homology at the amino acid level and 74% homology at the nucleotide level) which is a member of the aldehyde/aldose reductase family. This sequence homology supports previous correlates which suggest that in rat 3 alpha-HSD may represent an important target for NSAIDs. The nucleotide sequence also contains three peptides that have been identified by affinity labeling with either 3 alpha-bromoacetoxyandrosterone (substrate analog) or 11 alpha-bromoacetoxyprogesterone (glucocorticoid analog) to comprise the active site (see accompanying article (Penning, T. M., Abrams, W. R., and Pawlowski, J. E. (1991) J. Biol. Chem. 266, 8826-8834]. The sequence data presented suggests that 3 alpha-HSD, prostaglandin F synthase, and aldehyde/aldose reductases are members of a common gene family.

摘要

大鼠肝脏3α-羟基类固醇脱氢酶(3α-HSD,EC 1.1.1.50)是一种依赖NAD(P)(+)的氧化还原酶,它通过将5α-二氢睾酮转化为3α-雄烷二醇来终止雄激素作用。它与二氢二醇脱氢酶相同,并且可以作为9-、11-和15-羟基前列腺素脱氢酶发挥作用。其反应受到非甾体抗炎药(NSAIDs)的强烈抑制。从λgt11载体中的大鼠肝脏cDNA表达文库中克隆出了3α-HSD的cDNA(2.1千碱基)。将含有内部EcoRI位点的cDNA插入片段的部分亚克隆到pGEM3中,双脱氧测序显示该cDNA包含一个966个核苷酸的开放阅读框,编码一个由322个氨基酸组成的蛋白质,单体Mr为37,029。通过在核苷酸序列中定位来自纯化的3α-HSD的两个胰蛋白酶肽段和两个内肽酶Lys-C肽段,证实了该克隆的身份。大鼠肝脏3α-HSD的氨基酸序列与3β-、17β-或11β-羟基类固醇脱氢酶没有显著同源性,但与牛肺前列腺素F合酶具有显著同源性(氨基酸水平同源性为69%;核苷酸水平同源性为74%),牛肺前列腺素F合酶是醛/醛糖还原酶家族的成员。这种序列同源性支持了先前的相关性研究,表明在大鼠中3α-HSD可能是NSAIDs的一个重要靶点。核苷酸序列还包含三个肽段,通过用3α-溴乙酰氧基雄甾酮(底物类似物)或11α-溴乙酰氧基孕酮(糖皮质激素类似物)进行亲和标记已确定它们构成活性位点(见随附文章[Penning, T. M., Abrams, W. R., and Pawlowski, J. E. (1991) J. Biol. Chem. 266, 8826 - 8834])。所呈现的序列数据表明3α-HSD、前列腺素F合酶和醛/醛糖还原酶是一个共同基因家族的成员。

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