© 2005 European Society of Cardiology
Enhanced myocardial cathepsin B expression in patients with dilated cardiomyopathy
a Shanghai Institute of Cardiovascular Diseases, Zhongshan Hospital, Fudan University Fenglin Road 180, Shanghai 200032, P.R. China
b The First Affiliated Hospital, Nanhua University Hengyang of Hunan Province, China
* Corresponding author. Tel.: +86 21 64041990 2745; fax: +86 21 64223006. E-mail address: gejunbo{at}zshospital.net (J. Ge).
| Abstract |
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Objective: Cathepsin B is a prominent lysosomal protease and is involved in apoptosis as well as degradation of myofibrillar proteins in myocardial infarction. The aim of this study was to investigate myocardial cathepsin B expression in failing and non-failing human hearts.
Methods: Tissue samples were taken from transplanted left ventricles from 20 patients with dilated cardiomyopathy and 5 non-failing donor hearts that could not be transplanted for technical reasons. Myocardial cathepsin B expression was determined by immunohistochemistry, the reverse transcription–polymerase chain reaction (RT–PCR) and Western blotting. Apoptosis was assessed by TUNEL staining.
Results: Positive cathepsin B staining was found in failing and non-failing hearts. The expression of cathepsin B at mRNA and protein levels was significantly higher in failing hearts compared with non-failing hearts. Correlation analysis revealed that cathepsin B at mRNA and protein levels negatively correlated with EF (r=0.66, p=0.002 and r=0.492, p=0.028, respectively) in patients with heart failure. The apoptotic index was 0.015±0.006 in failing hearts and 0.002±0.001 in non-failing hearts (p<0.01).
Conclusion: Increased myocardial expression of cathepsin B was found in patients with heart failure suggesting that cathepsin B might play a role in the genesis and development of heart failure.
Key Words: Cathepsin B Dilated cardiomyopathy Heart failure Apoptosis
Received November 12, 2004; Revised July 3, 2005; Accepted September 8, 2005
1 Junbo Ge, Gang Zhao and Rhuizen Chen contributed equally to this work.
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