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短暂性脑缺血后大鼠大脑皮层热休克蛋白的合成

Synthesis of heat shock proteins in rat brain cortex after transient ischemia.

作者信息

Dienel G A, Kiessling M, Jacewicz M, Pulsinelli W A

出版信息

J Cereb Blood Flow Metab. 1986 Aug;6(4):505-10. doi: 10.1038/jcbfm.1986.86.

DOI:10.1038/jcbfm.1986.86
PMID:3733910
Abstract

Cell-free protein synthesis and two-dimensional gel autoradiography were used to characterize early postischemic protein synthesis in rat neocortex. Severe forebrain ischemia was induced for 30 min (four-vessel occlusion model) and followed by 3 h of recirculation. Polysomes were isolated from the cerebral cortex, translated in vitro in a reticulocyte system, and analyzed by two-dimensional gel electrophoresis. The translation products of postischemic polysomes included a major new protein family (70 kDa) with multiple isoelectric variants that was found to comigrate with the 68- to 70-kDa "heat shock" protein synthesized from polysomes of hyperthermic rats. Two other stress proteins (93 and 110 kDa) also appeared to be synthesized in increased amounts after ischemia. A complement of proteins that was indistinguishable from that of controls was also synthesized after ischemia, indicating that messenger ribonucleic acid coding for most brain proteins is preserved after ischemia and is bound to polysomes.

摘要

无细胞蛋白质合成和二维凝胶放射自显影技术被用于表征大鼠新皮质缺血后早期的蛋白质合成情况。通过四血管闭塞模型诱导严重的前脑缺血30分钟,随后再灌注3小时。从大脑皮质分离多核糖体,在网织红细胞系统中进行体外翻译,并通过二维凝胶电泳进行分析。缺血后多核糖体的翻译产物包括一个主要的新蛋白质家族(70 kDa),具有多个等电变体,发现其与热应激大鼠多核糖体合成的68至70 kDa“热休克”蛋白迁移位置相同。另外两种应激蛋白(93和110 kDa)在缺血后合成量似乎也增加。缺血后还合成了一组与对照组无法区分的蛋白质,这表明编码大多数脑蛋白的信使核糖核酸在缺血后得以保留并与多核糖体结合。

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