Abstract
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 language | English (US) |
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Pages (from-to) | 414-418 |
Number of pages | 5 |
Journal | Acta Physiologica Sinica |
Volume | 53 |
Issue number | 6 |
State | Published - 2001 |
Externally published | Yes |
Keywords
- Corticosterone
- Nongenomication
- PC12 cells
- Protein kinase C (PKC)
- p38
ASJC Scopus subject areas
- General Medicine