The cardioprotective role of small heat-shock protein 20

Martin, T. P. , Currie, S. and Baillie, G. S. (2014) The cardioprotective role of small heat-shock protein 20. Biochemical Society Transactions, 42(2), pp. 270-273. (doi:10.1042/BST20130272)

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The small HSP (heat-shock protein) HSP20 is a molecular chaperone that is transiently up-regulated in response to cellular stress/damage. Although ubiquitously expressed in various tissues, it is most highly expressed in skeletal, cardiac and smooth muscle. Phosphorylation at Ser<sup>16</sup> by PKA (cAMP-dependent protein kinase) is essential for HSP20 to confer its protective qualities. HSP20 and its phosphorylation have been implicated in a variety of pathophysiological processes, but most prominently cardiovascular disease. A wealth of knowledge of the importance of HSP20 in contractile function and cardioprotection has been gained over the last decade. The present mini-review highlights more recent findings illustrating the cardioprotective properties of HSP20 and its potential as a therapeutic agent.

Item Type:Articles
Glasgow Author(s) Enlighten ID:Martin, Dr Tamara and Baillie, Professor George
Authors: Martin, T. P., Currie, S., and Baillie, G. S.
College/School:College of Medical Veterinary and Life Sciences > Institute of Cardiovascular and Medical Sciences
Journal Name:Biochemical Society Transactions
Publisher:Portland Press
ISSN (Online):1470-8752

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Project CodeAward NoProject NamePrincipal InvestigatorFunder's NameFunder RefLead Dept
582921Development of small molecules that induce the cardio-protective effects of HSP20George BaillieHeart Research UK (HEART-RES)RG2610/12/14RI CARDIOVASCULAR & MEDICAL SCIENCES