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 Ser16 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.
| Original language | English |
|---|---|
| Pages (from-to) | 270-273 |
| Number of pages | 4 |
| Journal | Biochemical Society Transactions |
| Volume | 42 |
| Issue number | 2 |
| DOIs | |
| Publication status | Published - Apr 2014 |
Keywords
- cAMP
- cardioprotection
- heat-shock protein 20 (HSP20)
- peptide array
- phosphodiesterase type 4 (PDE4)
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Cite this
Martin, T., Currie, S., & Baillie, G. (2014). The cardioprotective role of small heat shock protein 20. Biochemical Society Transactions, 42(2), 270-273. https://doi.org/10.1042/BST20130272