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Title of Journal: Mol Cell Biochem

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Abbravation: Molecular and Cellular Biochemistry

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Springer US

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DOI

10.1007/bf00576855

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ISSN

1573-4919

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Creactive protein augments hypoxiainduced apopto

Authors: Jin Yang Junhong Wang Shushu Zhu Xiangjian Chen Hengfang Wu Di Yang Jinan Zhang
Publish Date: 2007/12/29
Volume: 310, Issue: 1-2, Pages: 215-226
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Abstract

Creactive protein CRP is an important predictive factor for cardiac disorders including acute myocardial infarction Therapeutic inhibition of CRP has been shown to be a promising new approach to cardioprotection in acute myocardial infarction in rat models but the direct effects of CRP on cardiac myocytes are poorly defined In this study we investigated the effects of CRP on cardiac myocytes and its molecular mechanism involved Neonatal rat cardiac myocytes were exposed to hypoxia for 8 h Hypoxia induced myocyte apoptosis under serumdeprived conditions which was accompanied by cytochrome c release from mitochondria into cytosol as well as activation of Caspase9 Caspase3 Hypoxia also increased Bax and decreased Bcl2 mRNA and protein expression thereby significantly increasing Bax/Bcl2 ratio Cotreatment of CRP 100 μg/ml under hypoxia significantly increased the percentage of apoptotic myocytes translocation of cytochrome c Bax/Bcl2 ratio and the activity of Caspase9 and Caspase3 However no effects were observed on myocyte apoptosis when cotreatment of CRP under normoxia Furthermore Bcl2 overexpression significantly improved cellular viability through inhibition of hypoxia or cotreatment with CRP induced Bax/Bcl2 ratio changes and cytochrome c release from mitochondria to cytosol and significantly blocked the activity of Caspase9 and Caspase3 The present study demonstrates that CRP could enhance apoptosis in hypoxiastimulated myocytes through the mitochondriondependent pathway but CRP alone has no effects on neonatal rat cardiac myocytes under normoxia Bcl2 overexpression might prevent CRPinduced apoptosis by inhibiting cytochrome c release from the mitochondria and block activation of Caspase9 and Caspase3This work was supported by National Natural Science Foundation of China No 30570745 Postgraduate Innovation Projects of Jiangsu Province JX22013013 and “135” key laboratory of Jiangsu Province SK200205 We also thank Dr Wei Dong Nanjing University China for his MPEI

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