HSP70 and genomic stability.
The 70 kDa heat shock proteins (HSP70s) were initially identified by their elevated expression following hyperthermic cell stress, however, these highly conserved proteins also protect critical cellular functions from a wider range of important environmental and physiological stresses. At least one result of HSP70 expression is inhibition of stress induced caspase activation as well as downstream events in the apoptotic cell death pathway. HSP70 have been reported upregulated in tumor cells, selective inhibition of such proteins might be valuable approach to treat cancer. A recent study revealed that cells with inactivated HSP70 displayed telomere instability and high frequency of spontaneous chromosomal aberrations, indicating a possible role for HSP70 proteins in the maintenance of genomic stability.
Pandita
Tej K
TK
Department of Radiation Oncology, Washington University School of Medicine, St Louis, Missouri 63108, USA. pandita@wustl.edu
Higashikubo
Ryuji
R
Hunt
Clayton R
CR
D000818:Animals; D004249:DNA Damage; D004260:DNA Repair; D004268:DNA-Binding Proteins; D042822:Genomic Instability; D018840:HSP70 Heat-Shock Proteins / Q000235:genetics / Q000378:metabolism*; D051379:Mice; D018345:Mice, Knockout; D019098:Telomerase / Q000378:metabolism
D004268:DNA-Binding Proteins; D018840:HSP70 Heat-Shock Proteins; D019098:Telomerase