Thiol-dependent redox modulation of soluble guanylyl cyclase

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Thiol-dependent redox modulation of soluble guanylyl cyclase

Background Following prolonged exposure to NO, soluble guanylyl cyclase (sGC) becomes desensitized and fails to respond to additional NO stimulation. We showed that sGC is desensitized by S-nitrosylation in vitro, in primary smooth muscle cells (SMC) and in tissues and identified two cysteines (Cys) targeted by this post-translational modification that are involved in sGC desensitization [1]. W...

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Nucleotidyl cyclase activity of soluble guanylyl cyclase in intact cells.

Soluble guanylyl cyclase (sGC) is activated by nitric oxide (NO) and generates the second messenger cyclic GMP (cGMP). Recently, purified sGC α1β1 has been shown to additionally generate the cyclic pyrimidine nucleotides cCMP and cUMP. However, since cyclic pyrimidine nucleotide formation occurred only the presence of Mn(2+) but not Mg(2+), the physiological relevance of these in vitro findings...

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Nucleotidyl cyclase activity of recombinant soluble guanylyl cyclase

Background The ubiquitously expressed soluble guanylyl cyclase (sGC) converts guanosine 5'-triphosphate (GTP) to guanosine 3':5'-cyclic monophosphate (cGMP). The heterodimeric protein is activated by nitric oxide (NO). sGC plays a key role in the regulation of vascular tone and neurotransmission. Hence, sGC is an important target for the treatment of cardiovascular diseases e.g. pulmonary hyper...

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Regulation of soluble guanylyl cyclase by phosphorylation

Results In vitro kinase assays revealed that the α1, but not the β1, subunit of sGC is a PKG substrate and that the phosphorylation site is located within the first 360 residues of the α1. A constitutively active form of PKG stimulated incorporation of 32P into the α1 subunit in vivo. In addition, PKG could be detected in sGC immunoprecipitates, suggesting that the two proteins interact in cell...

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Soluble guanylyl cyclase activation promotes angiogenesis.

Soluble guanylyl cyclase (sGC) is a cGMP-generating enzyme carrying a heme prosthetic group that functions as a nitric oxide (NO) sensor. sGC is present in most cells types, including the vascular endothelium, where its biological functions remain largely unexplored. Herein, we have investigated the role of sGC in angiogenesis and angiogenesis-related properties of endothelial cells (EC). Initi...

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ژورنال

عنوان ژورنال: BMC Pharmacology

سال: 2009

ISSN: 1471-2210

DOI: 10.1186/1471-2210-9-s1-s4