Cells overexpressing Hsp27 show accelerated recovery from heat-induced nuclear protein aggregation.
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 O23 cells made thermotolerant by a prior heating (20'44 degrees C + 10h 37 degrees 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 thermotolerant cells. This suggests that accelerated recovery of protein aggregation could be partly responsible for hsp27-mediated thermoprotection.
Department of Radiobiology, University of Groningen, The Netherlands.
H H
HH
Kampinga
J F
JF
Brunsting
G J
GJ
Stege
A W
AW
Konings
J
J
Landry
D000818:Animals; D002460:Cell Line; D002467:Cell Nucleus / Q000378:metabolism*; D002470:Cell Survival / Q000502:physiology*; D002999:Clone Cells; D006224:Cricetinae; D006360:Heat-Shock Proteins / Q000096:biosynthesis / Q000502:physiology*; D006358:Hot Temperature; D006801:Humans; D009687:Nuclear Proteins / Q000378:metabolism*; D011489:Protein Denaturation; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000378:metabolism; D014162:Transfection
D006360:Heat-Shock Proteins; D009687:Nuclear Proteins; D011994:Recombinant Proteins