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

Xiaoyu Li, Jian Qiu, Jianwen Wang, Yongping Zhong, Jianqin Zhu, Yizhang Chen

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Abstract

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.

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Keywords

  • c-Jun NH-terminal protein kinase
  • Corticosterone
  • Non-genomic
  • p38
  • PC12 cell
  • Protein kinase C

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Corticosterone-induced rapid phosphorylation of p38 and JNK mitogen-activated protein kinases in PC12 cells. / Li, Xiaoyu; Qiu, Jian; Wang, Jianwen; Zhong, Yongping; Zhu, Jianqin; Chen, Yizhang.

In: FEBS Letters, Vol. 492, No. 3, 16.03.2001, p. 210-214.

Research output: Contribution to journalArticle