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Cells Overexpressing Hsp27 Show Accelerated Recovery from Heat-Induced Nuclear-Protein Aggregation

1994; Elsevier BV; Volume: 204; Issue: 3 Linguagem: Inglês

10.1006/bbrc.1994.2586

1090-2104

Harm H. Kampinga, Jeanette F. Brunsting, G.J.J. Stege, A. W. T. Konings, Jacques Landry,

Genetics, Aging, and Longevity in Model Organisms

Protein denaturation/aggregation upon cell exposure to heat shock is a likely cause of cell death. In the nucleus, protein aggregation has often been correlated to inhibition of nuclear located processes and heat-induced cell killing. In Chinese hamster 023 cells made thermotolerant by a prior heating (20′44°C + 10h 37°C) which induces the whole spectrum of heat shock proteins (hsps), the extent of nuclear protein aggregation during heat shock is reduced and the rate of recovery from aggregation after heat shock is enhanced. In contrast, a heat resistant Chinese hamster cell line overexpressing only hsp27 shows an unaltered sensitivity to formation of nuclear protein aggregates by heat, but shows the same enhanced rate of recovery from nuclear protein aggregation as thermo-tolerant cells. This suggests that accelerated recovery of protein aggregation could be partly responsible for hsp27-mediated thermoprotection.