Functional Analysis of the Sulfotransferase, SULT2B1
磺基转移酶 SULT2B1 的功能分析
基本信息
- 批准号:6486488
- 负责人:
- 金额:$ 3.12万
- 依托单位:
- 依托单位国家:美国
- 项目类别:
- 财政年份:2002
- 资助国家:美国
- 起止时间:2002-03-11 至 2002-11-08
- 项目状态:已结题
- 来源:
- 关键词:SDS polyacrylamide gel electrophoresis affinity chromatography androgen receptor androgens biotransformation cell proliferation dehydroepiandrosterone dihydrotestosterone enzyme activity enzyme structure fluorescence microscopy fluorescence resonance energy transfer gel filtration chromatography genetic polymorphism genetic transcription glucuronosyltransferase immunoprecipitation neoplastic cell culture for noncancer research pharmacogenetics postdoctoral investigator protein protein interaction protein structure function steroid hormone sulfotransferase
项目摘要
Sulfate conjugation (sulfonation) is an important pathway in the biotransformation of steroid hormones. These reactions are catalyzed by a superfamily of cytosolic sulfotransferase (SULT) enzymes. In humans, the SULT2B1 gene encodes two isoforms, SULT2B1a and SULT2B1b, that catalyze the sulfonation of steroid hormones including dehydroepiepiandrosterone and dihydrotestosterone. SULT2B1 is expressed in steroid hormone-responsive tissues including prostate and breast. The goal of this research proposal seeks to elucidate a novel regulatory pathway, catalyzed by SULT2B1, that abrogates steroid- hormone dependent cellular processes. The proposed studies will evaluate the proliferative and transcriptional responses of cells expressing SULT2B1 and naturally occurring polymorphic SULT2B1 alloenzymes toward androgens. In complementary work, the functional significance of an evolutionarily acquired, novel proline-rich domain in SULT2B1 will be evaluated for its contribution to protein-protein interactions. Finally, the functional significance of common genetic SULT2B1 polymorphisms will be evaluated. Together these studies have the potential to elucidate a novel regulatory pathway, catalyzed by SULT2B1, that abrogates steroid hormone-dependent cellular processes in humans.
硫酸盐结合(磺化)是甾体激素生物转化的重要途径。这些反应由胞质磺基转移酶(SULT)超家族催化。在人类中,SULT 2B 1基因编码两种亚型,SULT 2B 1a和SULT 2B 1b,催化类固醇激素(包括脱氢表雄酮和二氢睾酮)的磺化。SULT 2B 1在类固醇激素敏感组织中表达,包括前列腺和乳腺。这项研究计划的目的是阐明一种新的调节途径,由SULT 2B 1催化,消除类固醇激素依赖性细胞过程。拟议的研究将评估表达SULT 2B 1和天然存在的多态性SULT 2B 1同种异型酶的细胞对雄激素的增殖和转录反应。在补充工作中,将评估SULT 2B 1中一个进化获得的新的富含脯氨酸的结构域对蛋白质-蛋白质相互作用的贡献的功能意义。最后,将评估常见遗传SULT 2B 1多态性的功能意义。总之,这些研究有可能阐明一种新的调节途径,由SULT 2B 1催化,消除类固醇激素依赖性的细胞过程在人类。
项目成果
期刊论文数量(6)
专著数量(0)
科研奖励数量(0)
会议论文数量(0)
专利数量(0)
Three dimensional time-gated tracking of non-blinking quantum dots in live cells.
活细胞中非闪烁量子点的三维时间选通跟踪。
- DOI:10.1117/12.2082943
- 发表时间:2015
- 期刊:
- 影响因子:0
- 作者:DeVore,MatthewS;Stich,DominikG;Keller,AaronM;Ghosh,Yagnaseni;Goodwin,PeterM;Phipps,MaryE;Stewart,MichaelH;Cleyrat,Cédric;Wilson,BridgetS;Lidke,DianeS;Hollingsworth,JenniferA;Werner,JamesH
- 通讯作者:Werner,JamesH
3-Dimensional Tracking of Non-blinking 'Giant' Quantum Dots in Live Cells.
- DOI:10.1002/adfm.201400349
- 发表时间:2014-08-13
- 期刊:
- 影响因子:19
- 作者:Keller, Aaron M.;Ghosh, Yagnaseni;DeVore, Matthew S.;Phipps, Mary E.;Stewart, Michael H.;Wilson, Bridget S.;Lidke, Diane S.;Hollingsworth, Jennifer A.;Werner, James H.
- 通讯作者:Werner, James H.
Note: Time-gated 3D single quantum dot tracking with simultaneous spinning disk imaging.
注:时间选通 3D 单量子点跟踪与同步旋转磁盘成像。
- DOI:10.1063/1.4937477
- 发表时间:2015
- 期刊:
- 影响因子:0
- 作者:DeVore,MS;Stich,DG;Keller,AM;Cleyrat,C;Phipps,ME;Hollingsworth,JA;Lidke,DS;Wilson,BS;Goodwin,PM;Werner,JH
- 通讯作者:Werner,JH
Ovarian tumor attachment, invasion, and vascularization reflect unique microenvironments in the peritoneum: insights from xenograft and mathematical models.
- DOI:10.3389/fonc.2013.00097
- 发表时间:2013
- 期刊:
- 影响因子:4.7
- 作者:Steinkamp MP;Winner KK;Davies S;Muller C;Zhang Y;Hoffman RM;Shirinifard A;Moses M;Jiang Y;Wilson BS
- 通讯作者:Wilson BS
Time-resolved three-dimensional molecular tracking in live cells.
- DOI:10.1021/nl103247v
- 发表时间:2010-11-10
- 期刊:
- 影响因子:10.8
- 作者:Wells NP;Lessard GA;Goodwin PM;Phipps ME;Cutler PJ;Lidke DS;Wilson BS;Werner JH
- 通讯作者:Werner JH
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