NR AFYC

AU James,M.; Crabbe,C.; Hepburne-Scott,H.W.

TI Small heat shock proteins (sHSPs) as potential drug targets

QU Current Pharmaceutical Biotechnology 2001 Mar; 2(1): 77-111

PT journal article; review; review, tutorial

AB Small heat shock proteins (sHSPs) belong to a family of 12- to 43-kDa proteins that are ubiquitous and are largely conserved in amino acid sequence among all organisms. The principal heat-shock proteins that have chaperone activity (that is, they protect newly made proteins from misfolding) belong to five conserved classes: HSP100, HSP90, HSP70, HSP60 and the small heat-shock proteins (sHSPs). The sHSPs (which include alpha crystallin) can form large multimeric structures and have a wide range of cellular functions, including endowing cells with thermotolerance in vivo and being able to act as molecular chaperones in vitro; sHSPs do this by forming stable complexes with folding - or unfolding - intermediates of their protein substrates, probably the molten globule. This paper includes: a brief survey of the chaperone family, the small heat shock protein superfamily, transcription of sHSPs, sequence comparisons and structural models of small heat shock proteins - structural elements as potential drug targets, sHSPs as chaperone-like proteins, alpha crystallin chaperone-like activity, conformational diseases - the role of alpha crystallin small heat shock protein superfamily proteins, post-translational modification and useful pharmacological agents. Functionality of small heat shock proteins - targets and diseases where pharmacologically active agents are of importance, alpha crystallin - small heat shock proteins and prion diseases: specific targets for diagnostic tests and drug development, details of some specific small heat shock proteins as drug targets, structural and functional implications for treatment.

ZR 187

MH Animal; Drug Delivery Systems/*methods; Heat-Shock Proteins/*chemistry/genetics; Human; Molecular Weight; Support, Non-U.S. Gov't

AD Division of Cell and Molecular Biology, School of Animal and Microbial Sciences, The University of Reading, Berkshire, UK. m.j.c.crabbe@reading.ac.uk

SP englisch

PO Niederlande

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