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- W2023808836 abstract "The development of therapeutic resistance, after hormone or chemotherapy for example, is the underlying basis for most cancer deaths. Exposure to anticancer therapies induces expression of many stress related proteins, including small heat shock proteins (HSPs). HSPs interact with various client proteins to assist in their folding and enhance the cellular recovery from stress, thus restoring protein homeostasis and promoting cell survival. The events of cell stress and cell death are linked, as the induction of molecular chaperones appears to function at key regulatory points in the control of apoptosis. On the basis of these observations and on the role of molecular chaperones in the regulation of steroid receptors, kinases, caspases, and other protein remodelling events involved in chromosome replication and changes in cell structure, it is not surprising that molecular chaperones have been implicated in the control of cell growth and in resistance to various anticancer treatments that induce apoptosis. Recently, several molecular chaperones such as Clusterin and HSP27 have been reported to be involved in development and progression of hormone-refractory prostate cancer. In this review, we address some of the molecular and cellular events initiated by treatment induced stress, and discuss the potential role of chaperone proteins as targets for prostate cancer treatment. Keywords: Prostate cancer, heat shock protein, Clusterin, antisense oligonucleotide, OGX-011, chemotherapy, apoptosis" @default.
- W2023808836 created "2016-06-24" @default.
- W2023808836 creator A5009043218 @default.
- W2023808836 creator A5036127630 @default.
- W2023808836 creator A5062125605 @default.
- W2023808836 creator A5077243123 @default.
- W2023808836 date "2007-06-01" @default.
- W2023808836 modified "2023-09-26" @default.
- W2023808836 title "The Role of Stress Proteins in Prostate Cancer" @default.
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