Stress-induced proteins in aortic smooth muscle cells and aorta of hypertensive rats.

Stress-induced proteins in aortic smooth muscle cells and aorta of hypertensive rats.
复制标题

高血压大鼠主动脉平滑肌细胞和主动脉中应激诱导的蛋白质。

DOI:
10.1152/ajpheart.1990.258.6.h1699
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发表时间:
1990
期刊:
The American journal of physiology
影响因子:
--
通讯作者:
Brecher,P
Brecher,P
中科院分区:
--
文献类型:
--
作者:
Kohane,DS;Sarzani,R;Schwartz,JH;Chobanian,AV;Brecher,P

文献摘要

被引文献

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目前的研究是为了确定血管平滑肌细胞在遭受实验性高血压时是否产生应激诱导的蛋白质。二维凝胶电泳用于分析培养细胞中对热休克或亚砷酸盐处理的反应的标记蛋白质。诱导的主要热休克蛋白 (HSP) 的分子量为 70、90 和 110 kDa。亚砷酸盐处理通过额外诱导 30-kDa 蛋白质产生类似的反应。热休克细胞总 RNA 的体外翻译以及使用 HSP 70 cDNA 的 RNA 印迹杂交表明 HSP 70 诱导受到转录调节。用去甲肾上腺素或血管紧张素 II 处理细胞可诱导细胞肥大,但不会引发 HSP。通过给予脱氧皮质酮和高盐摄入而导致高血压的大鼠的主动脉 RNA 的体外翻译也没有显示 HSP 诱导。使用高血压体内模型缺乏 HSP 诱导表明,可能不需要这些蛋白质来介导对实验性高血压的血管反应。
The current studies were performed to determine whether vascular smooth muscle cells produce stress-induced proteins when subjected to experimental hypertension. Two-dimensional gel electrophoresis was used to analyze labeled proteins in cultured cells in response to either heat shock or arsenite treatment. The major heat shock proteins (HSPs) induced had molecular masses of 70, 90, and 110 kDa. Arsenite treatment produced a similar response with the additional induction of a 30-kDa protein. In vitro translations of total RNA from heat-shocked cells, and RNA blot hybridization using HSP 70 cDNA suggested that HSP 70 induction was transcriptionally regulated. Treatment of cells with norepinephrine or angiotensin II induced cellular hypertrophy without eliciting HSPs. In vitro translation of aortic RNA from rats rendered hypertensive by administration of deoxycorticosterone and a high salt intake also did not reveal HSP induction. The absence of HSP induction using an in vivo model of hypertension suggests that those proteins may not be required to mediate the vascular response to experimental hypertension.