Stressproteine bei der Pathogenese des Prostatakarzinoms Journal Articles

abstract

• 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.

authors

• Hadaschik, BA
• Melchior, SW
• Sowery, Richard
• So, AI
• Gleave, ME

status

• published 

publication date

• May 2007

has subject area

• Antineoplastic Agents (MeSH)
• Apoptosis (MeSH)
• Chaperonins (MeSH)
• Clusterin (MeSH)
• Drug Delivery Systems (MeSH)
• Drug Resistance, Neoplasm (MeSH)
• Heat-Shock Proteins (MeSH)
• Humans (MeSH)
• Male (MeSH)
• Oligonucleotides, Antisense (MeSH)
• Prostatic Neoplasms (MeSH)

published in

• UROLOGIE  Journal

keywords

• Antineoplastic Agents
• Apoptosis
• Chaperonins
• Clusterin
• Drug Delivery Systems
• Drug Resistance, Neoplasm
• Heat-Shock Proteins
• Humans
• Male
• Oligonucleotides, Antisense
• Prostatic Neoplasms

Digital Object Identifier (DOI)

• 10.1007/s00120-007-1323-8

PubMed ID

• 17372715

start page

• 516

end page

• 520

volume

• 46

issue

• 5