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耐热小鼠肿瘤细胞株的生化分析：热休克蛋白70家族的一个新成员。

Biochemical analysis of heat-resistant mouse tumor cell strains: a new member of the HSP70 family.

作者信息

Anderson R L, Van Kersen I, Kraft P E, Hahn G M

机构信息

Department of Radiation Oncology, Stanford University, California 94305.

出版信息

Mol Cell Biol. 1989 Aug;9(8):3509-16. doi: 10.1128/mcb.9.8.3509-3516.1989.

DOI:10.1128/mcb.9.8.3509-3516.1989
PMID:2796993
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC362398/
Abstract

A series of heat-resistant mutants selected from a murine tumor cell line, RIF-1, display a markedly increased and stable resistance to heat shock. The mutant cell lines were analyzed for differences that may explain their increased resistance. Membrane lipid analysis showed no change in cholesterol content but an increase in the proportion of saturated fatty acids in the phospholipid fraction. Two-dimensional gel analysis revealed a generally increased constitutive synthesis of several major heat shock proteins (HSP), including HSP90, 68, 60, and 28. In addition, a new protein in the 70-kilodalton region is present in the resistant lines. The new protein has a lower isoelectric point than the constitutive HSP70 does, is only weakly induced by heat shock, and is immunologically cross-reactive with other members of the HSP70 family. After heat shock, the mutants display increases in HSP similar to those seen in the wild-type cells and they develop further transient tolerance to heat. Analysis of these mutants may help in understanding the function of HSP, both in normal growth and after heat shock.

摘要

从鼠肿瘤细胞系RIF-1中筛选出的一系列耐热突变体，对热休克表现出显著增强且稳定的抗性。对这些突变细胞系进行分析，以找出可能解释其抗性增强的差异。膜脂分析表明胆固醇含量没有变化，但磷脂部分中饱和脂肪酸的比例有所增加。二维凝胶分析显示，包括HSP90、68、60和28在内的几种主要热休克蛋白（HSP）的组成型合成普遍增加。此外，抗性细胞系中存在一种70千道尔顿区域的新蛋白。这种新蛋白的等电点比组成型HSP70低，仅受热休克微弱诱导，并且与HSP70家族的其他成员具有免疫交叉反应性。热休克后，突变体中HSP的增加与野生型细胞中观察到的情况相似，并且它们对热产生进一步的短暂耐受性。对这些突变体的分析可能有助于理解HSP在正常生长和热休克后的功能。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4af8/362398/873beded0532/molcellb00056-0370-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4af8/362398/6d34f7fdbcd1/molcellb00056-0367-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4af8/362398/3a636bd8e9c3/molcellb00056-0368-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4af8/362398/0242a18d5bfe/molcellb00056-0369-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4af8/362398/873beded0532/molcellb00056-0370-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4af8/362398/6d34f7fdbcd1/molcellb00056-0367-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4af8/362398/3a636bd8e9c3/molcellb00056-0368-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4af8/362398/0242a18d5bfe/molcellb00056-0369-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4af8/362398/873beded0532/molcellb00056-0370-a.jpg

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