[Stress proteins in prostate cancer. Challenge and promise].
Therapeutic resistance is the underlying basis for most cancer deaths. Exposure to anticancer therapies induces expression of many stress proteins, including heat shock proteins and clusterin. These molecular chaperones interact with various client proteins to assist in their folding and enhance cellular recovery from stress conditions. Cellular stress and cell death are linked, as the induction of chaperones appear to function at key regulatory points in the control of apoptosis. On this basis and on the role of stress proteins in the regulation of steroid receptors, kinases, caspases, and other protein remodeling events, it is not surprising that molecular chaperones have been implicated in resistance to anticancer treatments. Recently, several chaperones have been reported to be involved in development and progression of hormone-refractory prostate cancer. In this review, we address some of the events initiated by treatment-induced stress and discuss the potential role of chaperone inhibitors in prostate cancer treatment.
Hadaschik
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BA
The Prostate Centre at Vancouver General Hospital, 2660 Oak Street, V6H 3Z6 Vancouver. boris.hadaschik@vch.ca
Melchior
S W
SW
Sowery
R D
RD
So
A I
AI
Gleave
M E
ME
D000970:Antineoplastic Agents / Q000009:adverse effects / Q000627:therapeutic use; D017209:Apoptosis / Q000502:physiology; D018833:Chaperonins / Q000037:antagonists & inhibitors / Q000502:physiology; D051152:Clusterin / Q000037:antagonists & inhibitors / Q000502:physiology; D016503:Drug Delivery Systems; D019008:Drug Resistance, Neoplasm / Q000502:physiology; D006360:Heat-Shock Proteins / Q000037:antagonists & inhibitors / Q000502:physiology*; D006801:Humans; D008297:Male; D016376:Oligonucleotides, Antisense / Q000627:therapeutic use; D011471:Prostatic Neoplasms / Q000188:drug therapy / Q000503:physiopathology*
D000970:Antineoplastic Agents; D051152:Clusterin; D006360:Heat-Shock Proteins; D016376:Oligonucleotides, Antisense; D018833:Chaperonins