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

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ACTA PHYSIOLOGICA SINICA
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Volume 53, Issue 06, 2001
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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 G6976, 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.

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