The cardioprotective role of small heat shock protein 20

Tamara Martin, Susan Currie, George Baillie

Research output: Contribution to journalArticle

10 Citations (Scopus)

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 languageEnglish
Pages (from-to)270-273
Number of pages4
JournalBiochemical Society Transactions
Volume42
Issue number2
DOIs
Publication statusPublished - Apr 2014

Keywords

  • cAMP
  • cardioprotection
  • heat-shock protein 20 (HSP20)
  • peptide array
  • phosphodiesterase type 4 (PDE4)

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