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

Xiao Yu Li, Jian Qiu, Lin Xiao, Jian Qin Zhu, Yi Zhang Chen

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4 Scopus citations


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 Go6976, 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.

Original languageEnglish (US)
Pages (from-to)414-418
Number of pages5
JournalActa Physiologica Sinica
Issue number6
StatePublished - Dec 1 2001



  • Corticosterone
  • Nongenomication
  • PC12 cells
  • Protein kinase C (PKC)
  • p38

ASJC Scopus subject areas

  • Medicine(all)

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