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Rise in heat‐shock protein level confers tolerance to energy deprivation
Author(s) -
Gabai Vladimir L.,
Kabakov Alexander E.
Publication year - 1993
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(93)80997-9
Subject(s) - cycloheximide , rotenone , cytosol , hsp70 , protein biosynthesis , heat shock protein , biochemistry , stimulation , mitochondrion , biology , chemistry , microbiology and biotechnology , enzyme , neuroscience , gene
Heat shock (44°C for 10 min) or ATP depletion by an uncoupler (CCCP for 20 min) is shown to result in stimulation of hsp68/70 synthesis in Ehrlich tumor cells. After 3 h of recovery, the cells become thermotolerant. Surprisingly, repeated ATP depletion caused by CCCP or rotenone (a respiratory inhibitor) treatment, had a much lower effect on cell viability. Both induction of tolerance to energy deprivation and hsp68/70 synthesis were totally suppressed by cycloheximide, an inhibitor of cytosolic protein synthesis. In tolerant cells, rotenone still induced ATP depletion; however, protein aggregation (the rise in Triton‐insoluble proteins) was inhibited in these cells. It is suggested that cellular chaperones (e.g. hsp70) are involved in the protection of ischemie cells from necrosis, preventing protein aggregation under ATP deficiency.