Reduction of myocardial infarction by postischemic administration of the calpain inhibitor A-705253 in comparison to the Na+/H+ exchange inhibitor Cariporide® in isolated perfused rabbit hearts
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Christiane Neuhof
Abstract
The calpain inhibitor A-705253 and the Na+/H+-exchange inhibitor Cariporide® were studied in isolated perfused rabbit hearts subjected to 60 min occlusion of the ramus interventricularis of the left coronary artery (below the origin of the first diagonal branch), followed by 120 min of reperfusion. The inhibitors were added to the perfusion fluid solely or in combination at the beginning of reperfusion. Hemodynamic monitoring and biochemical analysis of perfusion fluid from the coronary outflow were performed. Myocardial infarct size and area at risk (transiently not perfused myocardium) were determined from left ventricular slices after a special staining procedure with Evans blue and 2,3,5-triphenyltetrazolium chloride. The infarcted area (dead myocardium) was 72.7±4.0% of the area at risk in untreated controls, but was significantly smaller in the presence of the inhibitors. The largest effect was observed with 10-6 M A-705253, which reduced the infarcted area to 49.2±4.1% of the area at risk, corresponding to a reduction of 33.6%. Cariporide® at 10-6 M reduced the infarct size to the same extent. The combination of both inhibitors, however, did not further improve cardioprotection. No significant difference was observed between the experimental groups in coronary perfusion, left ventricular pressure, heart rate, or in the release of lactate dehydrogenase and creatine kinase from heart muscle.
©2008 by Walter de Gruyter Berlin New York
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- Role of tissue kallikrein-related peptidases in cervical mucus remodeling and host defense
- Novel Techniques
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- Acknowledgment
- Acknowledgment
- Contents Volume 389, 2008
- Contents Biological Chemistry, Volume 389, 2008
- Author Index
- Author Index
- Subject Index
- Subject Index
Artikel in diesem Heft
- Review
- Reflections on the tissue kallikrein and kallikrein-related peptidase family – from mice to men – what have we learnt in the last two decades?
- Protein Structure and Function
- N-terminal polyglutamine-containing fragments inhibit androgen receptor transactivation function
- Molecular Medicine
- Quantitative expression analysis and prognostic significance of the novel apoptosis-related gene BCL2L12 in colon cancer
- Proteolysis
- Interaction of angiotensin-converting enzyme (ACE) with membrane-bound carboxypeptidase M (CPM) – a new function of ACE
- S1′ and S2′ subsite specificities of human plasma kallikrein and tissue kallikrein 1 for the hydrolysis of peptides derived from the bradykinin domain of human kininogen
- T-SP1: a novel serine protease-like protein predominantly expressed in testis
- Reduction of myocardial infarction by postischemic administration of the calpain inhibitor A-705253 in comparison to the Na+/H+ exchange inhibitor Cariporide® in isolated perfused rabbit hearts
- Role of tissue kallikrein-related peptidases in cervical mucus remodeling and host defense
- Novel Techniques
- An efficient fluorimetric method to measure the viability of intraerythrocytic Plasmodium falciparum
- Acknowledgment
- Acknowledgment
- Contents Volume 389, 2008
- Contents Biological Chemistry, Volume 389, 2008
- Author Index
- Author Index
- Subject Index
- Subject Index
