Abstract We investigated the inhibitory role of the nitric oxide (NO)–cGMP–protein kinase G (PKG) pathway on receptor-activated TRPC6 channels in both a heterologous expression system (HEK293 cells) and A7r5 vascular myocytes. The aim of the present study was to examine the role of protein kinase G (G-kinase) in the mechanism of endogenous nitric oxide (NO) deficiency-induced supersensitivity to the nitrovasodilator sodium nitroprusside (SNP) in isolated rat pulmonary artery. Zhang P(1), Ma Y(1), Wang Y(1), Ma X(1), Huang Y(2), Li RA(3), Wan S(4), Yao X(5). Protein Kinase G. Protein kinase G is activated by cGM P. Nitric oxide and atrial naturetic factor (ANF), or atrionatrin, are signaling molecules that lead to an elevation of cGM P. Thus, E 2 (inactive) + 4 cGMP E 2-cGMP 4 (active). Nitric oxide and protein kinase G act on TRPC1 to inhibit 11,12-EET-induced vascular relaxation. Rochus Franzen, Doriano Fabbro, Armaz Aschrafi, Josef Pfeilschifter, Andrea Huwiler

While protein kinase G is activated allosterically, other protein kinases are activated by covalent modification (phosphorylation). Recent studies have demonstrated that nitric oxide (NO) activates transient receptor potential vanilloid subtype 1 (TRPV1) via S-nitrosylation of the channel protein. Protein kinase G (PKG), a recognized downstream mediator of nitric oxide, is a key regulator of cardiovascular physiology and pathology. NO also modulates various cellular functions via activation of the soluble guanylyl cyclase (sGC)/protein kinase G (PKG) pathway and the direct modification of proteins. High-level stimulation of cyclic guanosine monophosphate/PKG signaling using high concentrations of nitric oxide donors, mimicking pathological conditions, induces apoptosis in vascular smooth muscle cells.


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