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The Soluble Guanylyl Cyclase Activator YC-1 Increases Intracellular cGMP and cAMP via Independent Mechanisms in INS-1E Cells

The Journal of Pharmacology and Experimental Therapeutics, ISSN: 0022-3565, Vol: 338, Issue: 3, Page: 925-931
2011
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Article Description

In addition to increasing cGMP, the soluble guanylyl cyclase (sGC) activator 3-(5′-hydroxymethyl-2′-furyl)-1-benzylindazole (YC-1) can elevate intracellular cAMP levels. This response was assumed to be as a result of cGMP-dependent inhibition of cAMP phosphodiesterases; however, in this study, we show that YC-1-induced cAMP production in the rat pancreatic beta cell line INS-1E occurs independent of its function as a sGC activator and independent of its ability to inhibit phosphodiesterases. This YC-1-induced cAMP increase is dependent upon soluble adenylyl cyclase and not on transmembrane adenylyl cyclase activity. We previously showed that soluble adenylyl cyclase-generated cAMP can lead to extracellular signal-regulated kinase activation and that YC-1-stimulated cAMP production also stimulates extracellular signal-regulated kinase. Although YC-1 has been used as a tool for investigating sGC and cGMP-mediated pathways, this study reveals cGMP-independent pharmacological actions of this compound.

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