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Corticosterone‐induced rapid phosphorylation of p38 and JNK mitogen‐activated protein kinases in PC12 cells
Author(s) -
Li Xiaoyu,
Qiu Jian,
Wang Jianwen,
Zhong Yongping,
Zhu Jianqin,
Chen Yizhang
Publication year - 2001
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(01)02254-2
Subject(s) - p38 mitogen activated protein kinases , kinase , phosphorylation , mitogen activated protein kinase , mitogen activated protein kinase kinase , ask1 , map kinase kinase kinase , microbiology and biotechnology , protein kinase a , chemistry , map2k7 , protein kinase c , biology , cyclin dependent kinase 2
The present study showed that corticosterone (B) could induce a rapid activation of p38 and c‐Jun NH 2 ‐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.