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Am J Physiol Cell Physiol 283: C463-C471, 2002; doi:10.1152/ajpcell.00299.2001
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Vol. 283, Issue 2, C463-C471, August 2002

Attenuation of cAMP accumulation in adult rat cardiac fibroblasts by IL-1beta and NO: role of cGMP-stimulated PDE2

Åsa B. Gustafsson1 and Laurence L. Brunton2

1 Biomedical Sciences Graduate Program, 2 Departments of Pharmacology and Medicine, University of California at San Diego, La Jolla, California 92093

Treatment of cultured adult rat cardiac fibroblasts with interleukin-1beta (IL-1beta ) induces the inducible nitric oxide synthase (iNOS) expression, increases nitric oxide (NO) and cGMP production, and attenuates cAMP accumulation in response to isoproterenol by ~50%. Reduced cAMP accumulation is due to NO production: the effect is mimicked by NO donors and prevented by NG-monomethyl-L-arginine, an NOS inhibitor. Effects of NO are not restricted to the beta -adrenergic response; the response to forskolin is similarly diminished. NO donors only slightly (12%) decrease forskolin-stimulated adenylyl cyclase (AC) activity in cardiac fibroblast plasma membranes, suggesting that the main effect of NO is not a direct one on AC. An inhibitor of soluble guanylyl cyclase inhibits the effects of IL-1beta and NO donors; inhibition of cGMP-dependent protein kinase is without effect. 3-Isobutyl-1-methylxanthine, a nonspecific phosphodiesterase (PDE) inhibitor, and erythro-9-(2-hydroxy-3-nonyl)adenine, a specific inhibitor of the cGMP-stimulated PDE (PDE2), completely restore cAMP accumulation in sodium nitroprusside-treated fibroblasts and largely reverse the attenuated response in IL-1beta -treated fibroblasts. Although NO reportedly acts by reducing AC activity in some cells, in cardiac fibroblasts NO production decreases cAMP accumulation largely by the cGMP-mediated activation of PDE2.

nitric oxide; interleukin-1beta ; phosphodiesterase 2; guanosine 3',5'-cyclic monophosphate; soluble guanylyl cyclase


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