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Rapid activation of p38 mitogen-activated protein kinase by corticosterone in PC12 cells

Li Xiaoyu, Qiu Jian, Xiao Lin, Zhu Jianqin, Chen Yizhang

Department of Biological Science and Technology,Nanjing University.Nanjing 210093,Jiangsu；China；Department of Physiology,Second Military Medical University.Shanghai 200433

Abstract

The present study using immunoblot showed that corticosterone (B) could induce a rapid activation of p38 in PC12 cells. The dose- and time-response curves were bell-shaped with a maximal activation at 10~(-9)mol/L and 15 min respectively. The activation was not affected by steroid nuclear receptor antagonist RU38486. Bovine serum albumin coupled B (B-BSA) could induce phosphorylation of p38. Tyrosine kinase inhibitor genistein failed to block the phosphorylation, a fact suggesting that the tyrosine kinase activity is not involved in the pathway. On the other hand, phorbol 12-myristate 13-acetate (PMA), a protein kinase C (PKC) activator, could mimic the actions of B, while Goo6976, a PKC inhibitor, could completely abolish the phosphorylation induced by B. These results clearly demonstrate that B activates p38 MAPK readily via a putative membrane receptor through a PKC-dependent pathway.

Key words: Corticosterone;Nongenomication;p38;Protein kinase C(PKC);PC12 cells

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Citing This Article：

Li Xiaoyu, Qiu Jian, Xiao Lin, Zhu Jianqin, Chen Yizhang. Rapid activation of p38 mitogen-activated protein kinase by corticosterone in PC12 cells. Acta Physiol Sin 2001; 53 (6): (in Chinese with English abstract).