Targeting chaperones in transformed systems - A focus on Hsp90 and cancer Journal Article


Author: Chiosis, G.
Article Title: Targeting chaperones in transformed systems - A focus on Hsp90 and cancer
Abstract: The molecular chaperone Hsp90 is a protein with important roles in maintaining the functional stability and viability of cells under a transforming pressure. Cancer cells harbour mutated oncogenic proteins or proteins with dysregulated function and the chaperone is required to maintain their folded and functionally active conformation. In addition, by chaperoning key proteins such as Raf-1, Akt, survivin and hTERT, Hsp90 regulates signalling pathways necessary for the growth, survival and limitless replicative potential of most tumours. Important elements of the apoptotic pathways are also regulated by Hsp90. Overall, these characteristics propose Hsp90 as an important target of whose inhibition may aim at a wide-range of oncogenic transformations. Several years into Hsp90 research have shed light into the feasibility, but also the limitations, of such an approach. In this review, the authors present the current understanding on the relevance and possibility of translating Hsp90 inhibitors into therapeutic agents in cancer therapy. © 2006 Ashley Publications.
Keywords: signal transduction; protein kinase b; unclassified drug; gene mutation; histone deacetylase inhibitor; clinical trial; fatigue; review; cisplatin; raf protein; diarrhea; nonhuman; solid tumor; antineoplastic agents; liver dysfunction; drug targeting; protein conformation; protein function; anorexia; animals; cell viability; cell survival; cell function; unindexed drug; melanoma; apoptosis; liver toxicity; multiple myeloma; breast cancer; myalgia; drug design; survivin; cancer therapy; carcinogenesis; cell transformation, neoplastic; drug delivery systems; cancer inhibition; hematologic malignancy; feasibility study; protein processing; regulatory mechanism; recombinant antibody; drug mechanism; pyrazole derivative; medical research; cancer cell; pancreatitis; telomerase reverse transcriptase; heat shock protein 90 inhibitor; heat shock protein 90; hsp90 heat-shock proteins; nausea and vomiting; purine derivative; drug bioavailability; adenosine triphosphate; protein folding; kidney cancer; heat shock response; oxaliplatin; pyrimidine derivative; malignant transformation; 4 [n (2 hydroxyethyl) n [2 (3 indolyl)ethyl]aminomethyl]cinnamohydroxamic acid; radicicol; hsp90; chaperone; peptide derivative; drug solubility; molecular stability; molecular chaperones; ansamycin derivative; novobiocin; coumarin derivative; cnf 1010; mycograb; 17 allylamino 17 demethoxygeldanamycin; shepherdin; fr 901228; 17 dimethylaminoethylamino 17 demethoxygeldanamycin; ipi 504; transformed system; beta zearalenol
Journal Title: Expert Opinion on Therapeutic Targets
Volume: 10
Issue: 1
ISSN: 1472-8222
Publisher: Informa Healthcare  
Date Published: 2006-02-01
Start Page: 37
End Page: 50
Language: English
DOI: 10.1517/14728222.10.1.37
PUBMED: 16441227
PROVIDER: scopus
DOI/URL:
Notes: --- - "Cited By (since 1996): 44" - "Export Date: 4 June 2012" - "CODEN: EOTTA" - "Source: Scopus"
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  1. Gabriela Chiosis
    279 Chiosis