Functional Analysis of the Sulfotransferase, SULT2B1

磺基转移酶 SULT2B1 的功能分析

• 批准号: 6486488
• 负责人: WILLIAM J GEESE
• 金额: $ 3.12万
• 依托单位: RESEARCH INST OF FOX CHASE CAN CTR
• 依托单位国家: 美国
• 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: https://reporter.nih.gov/project-details/6486488
• 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

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）是类固醇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，SULT2B1 基因编码两种同工型 SULT2B1a 和 SULT2B1b，它们催化类固醇激素（包括脱氢表雄酮和二氢睾酮）的磺化。 SULT2B1 在类固醇激素反应组织中表达，包括前列腺和乳房。本研究计划的目标是阐明一种由 SULT2B1 催化的新型调节途径，该途径可消除类固醇激素依赖性细胞过程。拟议的研究将评估表达 SULT2B1 和天然存在的多态性 SULT2B1 同种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 SULT2B1 中进化获得的新型富含脯氨酸结构域的功能意义，以了解其对蛋白质-蛋白质相互作用的贡献。最后，将评估常见遗传 SULT2B1 多态性的功能意义。这些研究共同有可能阐明由 SULT2B1 催化的一种新的调节途径，该途径可以消除人类中类固醇激素依赖性细胞过程。

项目成果

3-Dimensional Tracking of Non-blinking 'Giant' Quantum Dots in Live Cells.

活细胞中不闪烁“巨型”量子点的 3 维跟踪。

• 发表时间: 2014-08-13
• 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

Ovarian tumor attachment, invasion, and vascularization reflect unique microenvironments in the peritoneum: insights from xenograft and mathematical models.

卵巢肿瘤的附着、侵袭和血管化反映了腹膜独特的微环境：异种移植和数学模型的见解。

• 发表时间: 2013
• 作者: Steinkamp, Mara P;Winner, Kimberly Kanigel;Davies, Suzy;Muller, Carolyn;Zhang, Yong;Hoffman, Robert M;Shirinifard, Abbas;Moses, Melanie;Jiang, Yi;Wilson, Bridget S
• 通讯作者: Wilson, Bridget S

Time-resolved three-dimensional molecular tracking in live cells.

活细胞中的时间分辨三维分子追踪。

• 发表时间: 2010-11-10
• 影响因子: 10.8
• 作者: Wells, Nathan P;Lessard, Guillaume A;Goodwin, Peter M;Phipps, Mary E;Cutler, Patrick J;Lidke, Diane S;Wilson, Bridget S;Werner, James H
• 通讯作者: Werner, James H

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。

• 发表时间: 2015-03-12
• 作者: DeVore, Matthew S;Stich, Dominik G;Keller, Aaron M;Ghosh, Yagnaseni;Goodwin, Peter M;Phipps, Mary E;Stewart, Michael H;Cleyrat, Cédric;Wilson, Bridget S;Lidke, Diane S;Hollingsworth, Jennifer A;Werner, James H
• 通讯作者: Werner, James H

The architectural relationship of components controlling mast cell endocytosis.

控制肥大细胞内吞作用的成分的结构关系。

• 发表时间: 2013-11-01
• 影响因子: 4
• 作者: Cleyrat, Cédric;Darehshouri, Anza;Anderson, Karen L;Page, Christopher;Lidke, Diane S;Volkmann, Niels;Hanein, Dorit;Wilson, Bridget S
• 通讯作者: Wilson, Bridget S