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有针对性的蛋白质分解维持了氨酸激活

Natalie Burkard¹, Jan Becher, Cornelia Heindl

¹Department of Medicine, University of Wuerzburg, Wuerzburg, Germany.

|February 23, 2005

概括

通过 ангиотензин II 激活calpain,触发calcineurin 自抑制域的蛋白质分解,增加其活性和心肌细胞中的核转位. 这种机制有助于病理性心肌缩.

科学领域:

心血管生物学心血管生物学
疾病的分子机制.
酶学是一种酶学.

背景情况:

氨酸 (CnA) 在调节心肌缩方面起着至关重要的作用.
病理性工作负载诱导CnA自身抑制域的向蛋白解,增强其在人心肌中的活性.
在CnA激活的基础上精确的蛋白质分解机制需要研究.

研究的目的:

阐明负责心肌细胞中氨酸 (CnA) 激活的蛋白质分解机制.
为了调查calpain在蛋白质分解和激活CnA在高变性刺激下的作用.
确定CnA蛋白解对其活性和亚细胞局部化的影响.

主要方法:

用 ангиотензин II (Ang II) 刺激大鼠心肌细胞.
测定calpain活性和测量CnA蛋白解.
使用膜透性抑制剂抑制calpain.
通过免疫组织化学和GFP标记量化CnA活动和核转位的评估.

主要成果:

Ang II显著增加了calpain活性,并诱导了CnA自身抑制域的蛋白质分解.
卡尔帕因抑制阻止了Ang II诱导的蛋白质分解和随后的CnA激活.
二刺激导致了CnA核转位,该转位通过calpain抑制而逆转.
自抑制域的蛋白解导致构成性活性和核CnA.

结论:

Ang II诱导的卡尔激活介导了CnA自身抑制域的蛋白质分解.
这种蛋白质分解会增加CnA的活性,并促进其核转位,从而导致心肌缩.
自抑制域的丧失导致CnA的持续核定位和活性,即使在刺激被移除之后.

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