Activation of purified soluble guanylate cyclase by protoporphyrin IX.
نویسندگان
چکیده
منابع مشابه
Protoporphyrin IX generation from delta-aminolevulinic acid elicits pulmonary artery relaxation and soluble guanylate cyclase activation.
Protoporphyrin IX is an activator of soluble guanylate cyclase (sGC), but its role as an endogenous regulator of vascular function through cGMP has not been previously reported. In this study we examined whether the heme precursor delta-aminolevulinic acid (ALA) could regulate vascular force through promoting protoporphyrin IX-elicited activation of sGC. Exposure of endothelium-denuded bovine p...
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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 کاملGuanylate Cyclase From Bovine Lung
A kinetic characterization of the regulation of purified soluble guanylate cyclase from bovine lung by protoporphyrin M and hematin is reported. Purified guanylate cyclase was isolated with heme and had specific activities @mol of cGMP/min/mg of protein) of 0.1-0.2 and 0.3-0.6 in the presence of excess MgGTP and MnGTP, respectively, in the absence of added activators. Protoporphyrin IX, nitric ...
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: Proceedings of the National Academy of Sciences
سال: 1982
ISSN: 0027-8424,1091-6490
DOI: 10.1073/pnas.79.9.2870