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大鼠成纤维细胞中68,000 Mr热休克蛋白合成与耐热性表达的解离。

Dissociation of 68,000 Mr heat shock protein synthesis from thermotolerance expression in rat fibroblasts.

作者信息

Widelitz R B, Magun B E, Gerner E W

出版信息

Radiat Res. 1984 Aug;99(2):433-7.

PMID:6463215
Abstract

Rat embryonic fibroblasts growing exponentially at either 35, 37, or 39 degrees C were exposed to 42 degrees C for times up to 6 hr. Cell survival was unaffected by this heat shock in cultures growing at 39 degrees C but survival was decreased in a temperature dependent manner in cells growing at 37 or 35 degrees C. Exposure to 42 degrees C of cells previously adapted to 35 or 37 degrees C resulted in the induction of heat shock proteins (hsps) with apparent molecular weights of 68,000 (hsp 68), 70,000 (hsp 70), and 89,000 (hsp 89); cells previously adapted to 39 degrees C expressed all hsps except hsp 68. Inasmuch as the synthesis of certain hsps may function to protect cells from thermal damage, these data indicate that hsp 68 may not be required for this adaptation-related thermotolerant survival response. Hsp 68 may only be expressed in cells destined to die.

摘要

在35℃、37℃或39℃下呈指数生长的大鼠胚胎成纤维细胞被暴露于42℃长达6小时。在39℃下生长的培养物中,这种热休克对细胞存活没有影响,但在37℃或35℃下生长的细胞中,存活率以温度依赖的方式降低。将先前适应35℃或37℃的细胞暴露于42℃会诱导出表观分子量为68,000(热休克蛋白68,hsp 68)、70,000(热休克蛋白70,hsp 70)和89,000(热休克蛋白89,hsp 89)的热休克蛋白;先前适应39℃的细胞表达除hsp 68之外的所有热休克蛋白。由于某些热休克蛋白的合成可能起到保护细胞免受热损伤的作用,这些数据表明,热休克蛋白68可能不是这种与适应相关的耐热存活反应所必需的。热休克蛋白68可能仅在注定死亡的细胞中表达。

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