检索结果-南通市图书馆

第十五届国际药理学大会

作者： Mehta Neeraj arg vivek Division of Pharmacology College of PharmacyOhio State University Columbus OHU.S.A. Division of Pharmacology College of PharmacyOhio State University Columbus OHU.S.A.

＜正＞ Ischemic preconditioning （IPC） can be mimicked by K+ channel openers such as diazoxide. Diazoxide has multiple ATP-sensitive K+ channel （KATP）-indepen-dent actions, and the mechanism underlying diazoxidemediated cardioprotection remains inconclusive. Giving that the KATP pore-forming subunit Kir6.2-knock-out mice have shown no cardioprotection of IPC, we tested the hypothesis that diazoxide protects the heart by promoting import of Kir6.2-containing KATP into mitochondria from cytosol where they are synthesized. The effect of diazoxide on mitochondrial localization of Kir6.2 was examined in KATP deficient COS-7 cells transfected with HA tagged Kir6.2 and SUR2A by laser confocal microscopy. We found that the percentage of cells showing mitochondrial localization of Kir6.2 was significantly higher in diazoxide （100 micro M）-treated group than that in control group （68.0% vs. 11.0%）. The effect was almost completely prevented by the KATP channel inhibitors 5-hydroxydecanoate or glibenclamide, or a selective protein kinase C （PKC） inhibitor chelerythrine. We conclude that diazoxide increases Kir6.2-containing KATP channels in mitochondria by activation of PKC.

关键词： preconditioning diazoxide PKC

来源： cnki会议评论

在线全文

cnki会议

学校读者我要写书评

暂无评论

Mechanism involved in the modulation of photoreceptor-specific cyclic nucleotidegated channel by the tyrosine kinase adapter protein Grb14

引用

Protein & Cell 2011年第11期2卷 906-917页

作者： vivek K.Gupta Ammaji Rajala Karla K.Rodgers Raju V.S.Rajala Department of Ophthalmology University of Oklahoma Health Sciences CenterOklahoma CityOK 73104USA Department of Cell Biology University of Oklahoma Health Sciences CenterOklahoma CityOK 73104USA Department of Biochemistry and Molecular Biology University of Oklahoma Health Sciences CenterOklahoma CityOK 73104USA Dean A.McGee Eye Institute University of Oklahoma Health Sciences CenterOklahoma CityOK 73104USA

We recently found that growth factor receptor-bound(Grb)protein 14 is a novel physiological modulator of photoreceptor specific cyclic nucleotide-gated channel alpha subunit(CNGA1).Grb14 promotes the CNG channel closure through its Ras-associating(RA)*** the current study we show that this RA domain-mediated inhibition of rod CNG channel is electrostatic in ***14 competes with cGMP for the CNGA1 binding pocket and electrostatically interacts with arg^(559) through a negatively chargedβ-turn at its RA ***,the three Glu residues(180–182)in Grb14 are absolutely critical for electrostatic interaction with the cGMP binding pocket and resultant *** study also demonstrates that substitution of Lys^(140) for Ala or in combination with polyglutamte mutants of Grb14 results in a significantly reduced binding with *** results suggest that in addition to Glu^(180–182) and Lys^(140),other residues in Grb14 may be involved in the electrostatic interaction with *** RA domain is highly conserved among the members of Grb7 family of proteins,which includes Grb7,Grb10 and ***,only Grb14 is able to modulate the channel activity,but not Grb7 and *** together,it suggests the existence of a divergence in RA domains among the members of the Grb7 family.

关键词： growth factor receptor-bound protein 14(Grb14) Ras-associating domain cyclic nucleotide gated channel rod outer segments tyrosine kinase signaling

来源：

维普期刊数据库

同方期刊数据库评论

在线全文

学校读者我要写书评

暂无评论

欢迎您,

建议与咨询留下您的常用邮箱和电话号码，以便我们向您反馈解决方案和替代方法

时间限定

文献类型

馆藏选择

核心期刊

语言

文献类型

帮助

文字说明：

检索规则说明：

检索范例：

分类表

所选分类

限定检索结果

文献类型

馆藏范围

日期分布

学科分类号

主题

机构

作者

语言

在线全文

在线全文

请选择保存的检索档案：

请选择收藏分类：

通借通还

欢迎您,

建议与咨询 留下您的常用邮箱和电话号码，以便我们向您反馈解决方案和替代方法

时间限定

文献类型

馆藏选择

核心期刊

语言

文献类型

帮助

文字说明：

检索规则说明：

检索范例：

分类表

所选分类

限定检索结果

文献类型

馆藏范围

日期分布

学科分类号

主题

机构

作者

语言

在线全文

在线全文

请选择保存的检索档案： 新增检索档案 确定 取消

请选择收藏分类： 新增自定义分类 确定 取消

通借通还

建议与咨询留下您的常用邮箱和电话号码，以便我们向您反馈解决方案和替代方法

请选择保存的检索档案：

请选择收藏分类：