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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Publisher's URL: http://dx.doi.org/10.1042/BST20130272
Abstract
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 |
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Status: | Published |
Refereed: | Yes |
Glasgow Author(s) Enlighten ID: | Baillie, Professor George and Martin, Dr Tamara |
Authors: | Martin, T. P., Currie, S., and Baillie, G. S. |
College/School: | College of Medical Veterinary and Life Sciences > School of Cardiovascular & Metabolic Health |
Journal Name: | Biochemical Society Transactions |
Publisher: | Portland Press |
ISSN: | 0300-5127 |
ISSN (Online): | 1470-8752 |
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