I'm contemplating purchasing this article,
I've pointed to it once before, but before
I do, my email is zathrasandrenee@earthlink.net
(if anybody wants to save me a few bucks. Splitting
it three ways might be nice for $30 each...awfully
pricy for one person to have to spend that)
Targeting chaperones in transformed systems – a focus on Hsp90 and cancer
Author: Chiosis, Gabriela
Source: Expert Opinion on Therapeutic Targets, Volume 10, Number 1, 1 February 2006, pp. 37-50(14)
ingentaconnect.com
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. |
