Corticosterone‐induced rapid phosphorylation of p38 and JNK mitogen‐activated protein kinases in PC12 cells

FEBS Letters

Zhu, Jianqin²  Li, Xiaoyu¹  Wang, Jianwen³  Qiu, Jian³  Zhong, Yongping³  Chen, Yizhang¹ 

[1] Institute of Neuroscience, Second Military Medical University, 800 Xiang Ying Road, Shanghai 200433, PR China;Department of Biological Science and Technology, Nanjing University, Nanjing 210093, PR China;Department of Physiology, Second Military Medical University, Shanghai 200433, PR China

关键词: Corticosterone;    Non-genomic;    p38;    c-Jun NH2-terminal protein kinase;    Protein kinase C;    PC12 cell;    B;    corticosterone;    B-BSA;    bovine serum albumin-coupled corticosterone;    MAPK;    mitogen-activated protein kinase;    Erk;    extracellular signal-regulated kinase;    JNK;    c-Jun NH2-terminal protein kinase;    PKC;    protein kinase C;    PKA;    protein kinase A;    PMA;    phorbol 12-myristate 13-acetate;    DMEM;    Dulbecco's modified Eagle's medium;    NGF;    nerve growth factor;    RTK;    receptor tyrosine kinase;   

DOI  :  10.1016/S0014-5793(01)02254-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The present study showed that corticosterone (B) could induce a rapid activation of p38 and c-Jun NH₂-terminal protein kinase (JNK) in PC12 cells. The dose–response and time–response curves were bell-shaped with maximal activation at 10⁻⁹ M and at 15 min. RU38486 had no effect, and bovine serum albumin-coupled B could induce the activation. Genistein failed to block the phosphorylation, suggesting the pathway was not involved in tyrosine kinase activity. Phorbol 12-myristate 13-acetate could mimic, while Gö6976 could abolish the actions. These results demonstrated that B might act via a putative membrane receptor to activate p38 and JNK rapidly through a protein kinase C-dependent pathway.

【 授权许可】

Unknown