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Am J Physiol Regul Integr Comp Physiol (January 8, 2004). doi:10.1152/ajpregu.00482.2003
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Submitted on August 22, 2003
Accepted on January 6, 2004

Cytochrome P-450 Metabolites in Endothelin Stimulated Cardiac Hormone Secretion

Sook Jeong Lee1, Carol S Landon1, Stanley J Nazian1, and John R Dietz1*

1 Department of Physiology and Biophysics, Uiversity of South Florida, Cardiac Hormone Center, College of Medicine, Tampa, FL, USA

* To whom correspondence should be addressed. E-mail: jdietz{at}hsc.usf.edu.

We examined the role of cytochrome P-450-arachidonate (CYP450-AA) metabolites in endothelin-1 (ET-1) stimulated atrial natriuretic peptide (ANP) and proANP 1-30 secretion from the heart. 17-octadecynoic acid (17-ODYA), 10-5M, significantly inhibited ANP secretion stimulated by ET-1 (10-8M) in the isolated perfused rat atria and inhibited proANP 1-30 secretion stimulated by ET-1 (10-8M) or 20-hydroxyeicosatetraenoic acid in cultured neonatal rat ventricular myocytes (NRVM). In NRVM, 17-ODYA significantly (p < 0.05) increased secretion of cyclic AMP (cAMP) but had no significant effect on the secretion of cyclic GMP from NRVM. Staurosporine, an inhibitor of protein kinase C completely blocked the inhibitory action of 17-ODYA, whereas a protein kinase A inhibitor, H-89 (5x10-5M), did not significantly attenuate the effects of 17-ODYA. The results show that the inhibitory action of 17-ODYA on ET-1 augmented ANP secretion is mediated through cAMP and suggest that CYP450-AA may play an important role in ET-1 induced cardiac hormone secretion.




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