Journal
APOPTOSIS
Volume 21, Issue 8, Pages 887-895Publisher
SPRINGER
DOI: 10.1007/s10495-016-1262-1
Keywords
Apoptosis; Canstatin; Dynamin related protein 1; Isoproterenol; Mitochondrial fission
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Funding
- Kitasato University Research Grant for Young Researchers
- JSPS KAKENHI Grant [24780289]
- Grants-in-Aid for Scientific Research [24780289] Funding Source: KAKEN
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Canstatin, a non-collagenous fragment, is cleaved from type IV collagen alpha 2 chain, an essential component of basement membrane surrounding cardiomyocytes. Although canstatin is known as an endogenous anti-angiogenic factor, its effects on cardiomyocytes have not been clarified. This study examined the effects of canstatin on isoproterenol-induced apoptosis in differentiated H9c2 cardiomyoblasts. Retinoic acid was used to differentiate H9c2 myoblast to cardiomyocyte-like phenotype. Cell viability was determined by a cell counting assay. Western blotting was performed to detect expression of cleaved casepase-3 and phosphorylation of dynamin related protein (Drp) 1 at Ser637 which regulates mitochondrial fission. Mito Sox Red staining was performed to examine a mitochondria-dependent production of reactive oxygen species (ROS). Mitochondrial morphology was detected by Mito Tracker Red staining. Isoproterenol (100 mu M, 48 h) significantly decreased cell viability and increased cleaved caspase-3 expression, which were inhibited by canstatin (10-250 ng/ml) in a concentration-dependent manner. Canstatin suppressed the isoproterenol-induced mitochondrial fission but not ROS. Canstatin also inhibited the isoproterenol-induced dephosphorylation of Drp1 at Ser637. In conclusion, canstatin inhibits isoproterenol-induced apoptosis through the inhibition of mitochondrial fission via the suppression of dephosphorylation of Drp1 at Ser637 in differentiated H9c2 cardiomyoblasts.
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