RECONSTITUTION OF NO SYNTHASE WITH SOLUBLE GUANYLATE CYCLASE SUGGESTS INVOLVEMENT OF THIOL NITROSATION IN NO/cGMP SIGNALLING
نویسندگان
چکیده
منابع مشابه
Inactivation of soluble guanylate cyclase by stoichiometric S-nitrosation.
Dysfunction of vascular nitric oxide (NO)/cGMP signaling is believed to contribute essentially to various cardiovascular disorders. Besides synthesis and/or bioavailability of endothelial NO, impaired function of soluble guanylate cyclase (sGC) may play a key role in vascular dysfunction. Based on the proposal that desensitization of sGC through S-nitrosation contributes to vascular NO resistan...
متن کاملBiochemistry of soluble guanylate cyclase.
Nitric oxide (NO) functions in biology as both a critical cytotoxic agent and an essential signaling molecule. The toxicity of the diatomic gas has long been accepted; however, it was not known to be a signaling molecule until it was identified as the endothelium-derived relaxing factor (EDRF). Since this discovery, the physiological signaling pathways that are regulated by NO have been the foc...
متن کاملNO resistance in angiotensin II–induced hypertension is associated with S-nitrosation of soluble guanylyl cyclase
Background We recently discovered that soluble guanylyl cyclase (sGC) activity is modulated by S-nitrosation, the addition of a NO moiety to the free thiol of cysteines (Cys). Pathologically, we observed that exposure to low, therapeutic levels of nitroglycerin in rats led to decreased vascular response to NO in the arterioles of hamster cheek pouch, which correlated with S-nitrosation and dese...
متن کاملStructural studies of soluble guanylate cyclase
Soluble guanylate cyclase (sGC) is the primary receptor for nitric oxide (NO), which enhances GTP to cGMP conversion by sGC ~200-fold. The second messenger, cGMP, further modulates the activity of kinases and ion channels and ultimately induces smooth muscle relaxation and vasodilation. In cases of endothelial dysfunction, diminished NO production and insufficient output of the NOsGC-cGMP pathw...
متن کاملRegulation of Soluble Guanylate Cyclase Activity
Alterations of the chemical structure of protoporphyrin IX markedly altered the activation of soluble guanylate cyclase purified from bovine lung. Hydrophobic side chains at positions 2 and 4 and vicinal propionic acid residues at positions 6 and 7 of the porphyrin ring (protoporphyrin IX, mesoporphyrin IX) were essential for maximal enzyme activation (K. = 7-8 nM; V, = 6-8 Kmol of cGMP/min/mg)...
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ژورنال
عنوان ژورنال: Japanese Journal of Pharmacology
سال: 1997
ISSN: 0021-5198
DOI: 10.1016/s0021-5198(19)31267-3