Abstract
Aim:
To explore whether overexpression of the small heat shock protein HSP20 in rat cardiomyocytes protects against simulated ischemia/reperfusion (SI/R) injury.
Methods:
Recombinant adenovirus expressing HSP20 was used to infect rat H9c2 cardiomyocytes at high efficiency, as assessed by green fluorescent protein. H9c2 cells were subjected to SI/R stress; survival was estimated through assessment of lactate dehydrogenase and cell apoptosis through caspase-3 activity.
Results:
Overexpression of HSP20 decreased lactate dehydrogenase release by 21.5% and caspase-3 activity by 58.8%. Pretreatment with the protein kinase C inhibitor Ro-31-8220 (0.1 μmol/L) for 30 min before SI/R canceled the protective effect of HSP20. The selective mitochondrial K+ATP channel inhibitor 5-hydroxydecanoate (100 μmol/L) had a similar effect. However, the non-selective K+ATP channel inhibitor glibenclamide (100 μmol/L) had no significant effect.
Conclusion:
These data indicate that the protective effect of HSP20 in vitro is primarily due to reduced necrotic and apoptotic death of cardiomyocytes, possibly via the protein kinase C/mitochondrial K+ATP pathway.
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Project supported by the National Basic Research Program of China (No G2000056908) awarded to Xian Wang.
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Zhu, Yh., Wang, X. Overexpression of heat-shock protein 20 in rat heart myogenic cells confers protection against simulated ischemia/reperfusion injury. Acta Pharmacol Sin 26, 1076–1080 (2005). https://doi.org/10.1111/j.1745-7254.2005.00137.x
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DOI: https://doi.org/10.1111/j.1745-7254.2005.00137.x


