Homodimerization of Soluble Guanylyl Cyclase Subunits
نویسندگان
چکیده
منابع مشابه
Forced Homodimerization by Site-Directed Mutagenesis Alters Guanylyl Cyclase Activity
Natriuretic peptides mediate their physiologic effects through activation of membrane-bound, guanylyl cyclase–coupled receptors (NPRs). Receptor dimerization is an important feature of signal transduction. This study was aimed at characterizing structurally important residues of the extracellular ligand-binding domain of NPR-B for receptor dimerization and cGMP generation. Deletion mutagenesis ...
متن کاملNucleotidyl 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...
متن کاملNucleotidyl 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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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 (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: Journal of Biological Chemistry
سال: 1999
ISSN: 0021-9258
DOI: 10.1074/jbc.274.26.18149