Enzymatic Properties and Physiological Role of Membrane bound-Prostaglandin E Synthase
膜结合前列腺素 E 合酶的酶学特性和生理作用
基本信息
- 批准号:09680637
- 负责人:
- 金额:$ 2.05万
- 依托单位:
- 依托单位国家:日本
- 项目类别:Grant-in-Aid for Scientific Research (C)
- 财政年份:1997
- 资助国家:日本
- 起止时间:1997 至 2000
- 项目状态:已结题
- 来源:
- 关键词:
项目摘要
E series of prostaglandin (PG)s were first discovered in sheep seminal vesicles. PGE_2 is widely distributed in various organs, and exhibits various biological activities such as smooth muscle dilatation/contraction, Na^+ excretion, body temperature regulation, inhibition of gastric acid secretion, and inhibition of immune responses. PGE synthase (EC.5. 3. 99. 3.) catalyzes the conversion of PGH_2 to PGE_2. In 1997, we reported that PGE synthase activity is widely distributed in the microsomal fractions of rat organs. Most of the PGE synthase activities in these organs absolutely required glutathione (GSH). In contrast, the enzyme activity in the heart, spleen, and uterine microsomes required SH-reducing reagents including dithiothreitol (DTT), GSH, or β- mercaptoethanol (β-Mer), but the requirement for its catalytic activity was not specific for GSH.We purified the GSH specific PGE synthase from bovine heart microsomes to apparent homogeneity, and partially purified the GSH unspecific PGE synthase from sheep seminal vesicle microsomes. We examined their molecular and catalytic properties.
E系列前列腺素(PG)S是在绵羊精囊中首次发现的。前列腺素E_2(PGE_2)广泛分布于多种器官,具有多种生物活性,如平滑肌扩张/收缩、Na~+排泄、体温调节、抑制胃酸分泌、抑制免疫反应等。前列腺素E合成酶(EC.5.3.99。3.)PGE合酶催化PGH_2转化为PGE_2。1997年,我们报道了PGE合成酶活性广泛分布于大鼠器官的微粒体部分。这些器官中的大多数前列腺素E合成酶活性绝对需要谷胱甘肽(GSH)。相反,心脏、脾和子宫微粒体中的酶活性需要SH还原剂,如二硫苏糖醇(DTT)、谷胱甘肽或β-硫醇(β-Mer),但对其催化活性的要求并不是GSH所特有的。我们研究了它们的分子和催化性质。
项目成果
期刊论文数量(0)
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专利数量(0)
Nishizawa,M.,Watanabe,K.,and Ito,S.: "Close Kinship of Human 20a-Hydroxysteroid Dehydrogenase Gene with Three Aldo-keto Reductase Genes."Genes Cells.. 5・2. 111-125 (2000)
Nishizawa, M.、Watanabe, K. 和 Ito, S.:“人类 20a-羟基类固醇脱氢酶基因与三个醛酮还原酶基因的密切关系。” 基因细胞.. 111-125 (2000)
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- 影响因子:0
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Watanabe,K.,Kurihara,K.,and Suzuki,T.: "Purification and Characterization of Membrance-bound Prostaglandin E Synthase from Bovine Heart."Biochim.Biophys.Acta. 1439. 406-414 (1999)
Watanabe, K.、Kurihara, K. 和 Suzuki, T.:“来自牛心脏的膜结合前列腺素 E 合酶的纯化和表征。”Biochim.Biophys.Acta。
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- 影响因子:0
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Watanabe Kikuko: "Two types of microsomal prostaglandin E synthase-Glutathione-dependent and-independent prostaglandin E synthases・・・" Biochem.Biophys.Res.Commun.235. 148-152 (1997)
Watanabe Kikuko:“两种类型的微粒体前列腺素 E 合酶 - 谷胱甘肽依赖性和非依赖性前列腺素 E 合酶……”Biochem.Biophys.Res.Commun.235 (1997)。
- DOI:
- 发表时间:
- 期刊:
- 影响因子:0
- 作者:
- 通讯作者:
Nishizawa,M.,Watanabe,K.,and Ito,S.: "Close Kinship of Human 20a-Hydroxysteroid Dehydrogenase Gene with Three Aldo-keto Reductase Genes."Genes Cells.. 5・2. 111-125 (2001)
Nishizawa, M.、Watanabe, K. 和 Ito, S.:“人类 20a-羟基类固醇脱氢酶基因与三个醛酮还原酶基因的密切关系。” 基因细胞.. 111-125 (2001)
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- 影响因子:0
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Suzuki-Yamamoto, T., Yokoi. H., Tsuruo, Y., Watanabe, K.and Ishimura, K.: "Identification of prostaglandin F-producing cells in the liver."Histochem. Cell Biol.. 112 (6). 451-456 (1999)
铃木山本,T.,横井。
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WATANABE Kikuko其他文献
WATANABE Kikuko的其他文献
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{{ truncateString('WATANABE Kikuko', 18)}}的其他基金
Pathophysiological roles of prostaglandin F synthase
前列腺素 F 合酶的病理生理作用
- 批准号:
13670152 - 财政年份:2001
- 资助金额:
$ 2.05万 - 项目类别:
Grant-in-Aid for Scientific Research (C)
The structure and function of prostaglandin F synthase. (a dual function enzyme)
前列腺素F合酶的结构和功能。
- 批准号:
05670156 - 财政年份:1993
- 资助金额:
$ 2.05万 - 项目类别:
Grant-in-Aid for General Scientific Research (C)
The structure and function of PGF synthase
PGF合酶的结构和功能
- 批准号:
01570145 - 财政年份:1989
- 资助金额:
$ 2.05万 - 项目类别:
Grant-in-Aid for General Scientific Research (C)
相似海外基金
NEW APPROACH TO PURIFICATION OF MEMBRANE-BOUND ENZYME - APPLIED TO PAF SYNTHETIC ENZYME PURIFICATION
膜结合酶纯化新方法——应用于 PAF 合成酶纯化
- 批准号:
12672120 - 财政年份:2000
- 资助金额:
$ 2.05万 - 项目类别:
Grant-in-Aid for Scientific Research (C)
effect of the inhibitor to membrane-bound enzyme on the growth of invasion of cancer cells
膜结合酶抑制剂对癌细胞侵袭生长的影响
- 批准号:
06671642 - 财政年份:1994
- 资助金额:
$ 2.05万 - 项目类别:
Grant-in-Aid for General Scientific Research (C)