Chelerythrine, a protein kinase C inhibitor, interacts with cyclic nucleotide phosphodiesterases.

Article Details

Citation
Copy to clipboard

Eckly-Michel AE, Le Bec A, Lugnier C

Chelerythrine, a protein kinase C inhibitor, interacts with cyclic nucleotide phosphodiesterases.

Eur J Pharmacol. 1997 Apr 11;324(1):85-8. doi: 10.1016/s0014-2999(97)00149-0.

PubMed ID
9137917 [ View in PubMed
]
Abstract

Chelerythrine, a potent inhibitor of protein kinase C, was evaluated for its effect on cyclic nucleotide phosphodiesterases (PDE) isolated from bovine aorta. Chelerythrine activated basal PDE2 and inhibited activated PDE2, PDE4 and PDE5. The effect of chelerythrine (10 microM) was also investigated on vasorelaxation induced by a beta-adrenoceptor agonist or a PDE3 inhibitor. Chelerythrine attenuated the isoprenaline-mediated relaxation whereas it potentiated the relaxation induced by SK & F 94120 (5-(4)acetamidophenyl)pyrazin-2(1 H)-one, a PDE3 inhibitor). The present study demonstrates that chelerythrine, at a concentration generally reported in the literature to inhibit protein kinase C, interacts with cyclic nucleotide phosphodiesterases and consequently modulates vasorelaxation. These results cast some doubt on the use of chelerythrine as a specific inhibitor of protein kinase C.

DrugBank Data that Cites this Article

Drugs