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

Research output: Contribution to journalArticlepeer-review

32 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)210-214
Number of pages5
JournalFEBS Letters
Volume492
Issue number3
DOIs
StatePublished - Mar 16 2001
Externally publishedYes

Keywords

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

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

Fingerprint

Dive into the research topics of 'Corticosterone-induced rapid phosphorylation of p38 and JNK mitogen-activated protein kinases in PC12 cells'. Together they form a unique fingerprint.

Cite this