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Cardiovascular Research Advance Access first published online on April 8, 2008
This version [Corrected Proof] published online on April 25, 2008
Cardiovascular Research, doi:10.1093/cvr/cvn091
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Published on behalf of the European Society of Cardiology. All rights reserved. © The Author 2008. For permissions please email: journals.permissions@oxfordjournals.org

Overexpression of heat shock protein 27 protects against ischaemia/reperfusion-induced cardiac dysfunction via stabilization of troponin I and T

Xi-Yuan Lu, Le Chen, Xiao-Long Cai and Huang-Tian Yang*

Laboratory of Molecular Cardiology, Institute of Health Sciences (IHS), Institutes for Biological Sciences (SIBS), Chinese Academy of Sciences (CAS) and Shanghai Jiao Tong University School of Medicine (SJTUSM), 225 Chong Qing Nan Rd, Build. No. 1 of Institute of Health Sciences, Rm. 613, Shanghai 200025, China

* Corresponding author. Tel: +86 21 63852593; fax: +86 21 63852593. E-mail address: htyang{at}sibs.ac.cn

Aims: Heat shock protein 27 (Hsp27) renders cardioprotection from ischaemia/reperfusion (I/R) injury, but little is known about its role in myofilaments. We proposed that increased expression of Hsp27 may improve post-ischaemic contractile dysfunction by preventing I/R-induced cardiac troponin I (cTnI) and troponin T (cTnT) degradation.

Methods and results: Adenovirus-mediated Hsp27 overexpression improved contractile function in perfused rat hearts subjected to global no-flow I/R (30-min/30-min). Such improvement was further confirmed in Hsp27-overexpressing cardiomyocytes subjected to simulated I/R (20-min/30-min). Moreover, these cells showed restored myofilament response to Ca2+ but not intracellular Ca2+ transients. The protection correlated with attenuation of I/R-induced cTnI and cTnT degradation. Confocal microscopy revealed co-localization of Hsp27 with these proteins. Co-immunoprecipitation and pull-down assays further confirmed that Hsp27 interacted with the COOH-terminus of cTnI and the NH2-terminus of cTnT and that Hsp27 overexpression decreased the interaction between µ-calpain (a protease mediating proteolysis of cTnI and cTnT) and cTnI or cTnT under I/R.

Conclusion: The findings reveal a novel role of Hsp27 in the protection of cTnI and cTnT from I/R-induced degradation by preventing their proteolytic cleavage via interacting with these proteins. Such protection may result in restored post-ischaemic myofilament response to Ca2+ and improved post-ischaemic contractile function.

KEYWORDS Heat shock protein 27; Ischaemia/reperfusion; Contraction; Troponin I; Troponin T

Time for primary review: 31 days


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