purified sGC can act as detector for NO-like bioactivity generated from nitrite and glycerol trinitrate and for NO released by heart and liver mitochondria
the soluble guanylate cyclase is a target for compounds used in therapy of heart failure, e.g. nitric oxide-independent, soluble guanylate cyclase activator cinaciguat, BAY 58-2667, that induces vasodilation preferentially in diseased vessels, overview
different roles of the natriuretic peptide and NO systems. In acute heart failure, the natriuretic peptide system plays a role in maintaining sodium excretion and glomerular filtration rate, while the function of the NO system is in the maintenance of renal blood flow. These two cGMP activating systems function through two distinct GC enzymes, playing a key role in maintaining renal function in acute heart failure
guanylyl cyclase activity is related to intracellular Ca2+ mobilization and this Ca2+-cGMP cross-talk may in turn be associated with parasite infectivity
limited species differences in sGC subunit distribution of primates and rodents. NO-cGMP signaling pathway may be involved in important brain functions such as memory formation, sensory processing, and behavior
limited species differences in sGC subunit distribution of primates and rodents. NO-cGMP signaling pathway may be involved in important brain functions such as memory formation, sensory processing, and behavior
sensitivity of guanylyl cyclase heme nitrosylation as well as oxygen-dependent NO consumption may be particularly adapted to direct itinerant endothelial cells into hypoxic tissues in the setting of inflammation, wound healing, and cancer
targeting soluble guanylate cyclase with BAY 41-2272 may represent a therapy in the management of voiding disturbances associated with impaired NO-cGMP signaling
the enzyme stimulation, e.g. by riociguat, is a strategy in treatment of pulmonary hypertension, moderate-to-severe phenotype, associated with impaired production of the vasodilator nitric oxide, study of safety, tolerability and efficacy in patients
in red blood cells, an intact soluble guanylate cyclaseC/PDE5/PKG-dependent signaling pathway exists, which remains fully responsive to NO and guanylate cyclase stimulators/activators in patients with endothelial dysfunction
guanylyl cyclase activity is related to intracellular Ca2+ mobilization and this Ca2+-cGMP cross-talk may in turn be associated with parasite infectivity
the enzyme is a favorable optogenetic tool for non-invasive, cell-selective, and spatio-temporally precise modulation of cAMP/cGMP with light. The rhodopsin domain from Catenaria is more photostable than that from Blastocladiella, and the signaling state persists longer, both of which are highly desirable traits for optogenetic applications
the enzyme is a favorable optogenetic tools for non-invasive, cell-selective, and spatio-temporally precise modulation of cAMP/cGMP with light. The rhodopsin domain from Catenaria is more photostable than that from Blastocladiella, and the signaling state persists longer, both of which are highly desirable traits for optogenetic applications
the enzyme is a favorable optogenetic tool for non-invasive, cell-selective, and spatio-temporally precise modulation of cAMP/cGMP with light. The rhodopsin domain from Catenaria is more photostable than that from Blastocladiella, and the signaling state persists longer, both of which are highly desirable traits for optogenetic applications
activators of sGC may be beneficial in the treatment of a range of diseases including systemic and pulmonary hypertension, heart failure, atherosclerosis, peripheral arterial occlusive disease, thrombosis and renal fibrosis, overview
alternative splicing can regulate endogenous ANP/GC-A signaling, thus, angiotensin II-induced alternative splicing of GC-A may represent a mechanism for reducing the sensitivity to atrial natriuretic peptide
pharmacological approaches do not allow cell specific manipulation of cyclic nucleotides in tissue and lack precision in space and time, limitations that can be overcome using the light-activated enzyme
pharmacological approaches do not allow cell specific manipulation of cyclic nucleotides in tissue and lack precision in space and time, limitations that can be overcome using the light-activated enzyme
pharmacological approaches do not allow cell specific manipulation of cyclic nucleotides in tissue and lack precision in space and time, limitations that can be overcome using the light-activated enzyme
bronchial smooth muscle cGMP-, but not cAMP-dependent, relaxant response is developmentally regulated and significantly reduced in the adult rat, correlates with the higher expression of the two isoforms and higher activity of sGC in newborn rat bronchial tissue
coexistence of homologous and heterologous desensitization of GC-A in the same cell type, these reactions are mediated by different pathways, cross talk between phospholipid and natriuretic peptide signaling
differences in the effects of ATP on signal transduction of GC-coupled natriuretic peptide receptor A between Wistar Kyoto and spontaneously hypertensive rats
GCC is involved in cytosolic apical sorting signals in epithelial cells, apical sorting determinant for GCC is a region of 11 highly conserved amino acids (PTPPTVENQQR) in the COOH terminus, which are essential for the normal polarization of GCC in MDCK cells. This sequence is sufficient to selectively target an unpolarized reporter protein, interleukin-2 receptor alpha-chain, to the apical membrane
residues H104, Y140, the YxS/TxR motif and missing cysteines Cys78 and Cys214 are conserved in all the insect atypical sGC subunits. Atypical sGCs can function as O2 sensors and can modulate sensitivity to sweet tastants
segments spanning amino acids alpha1 363-372, alpha1 403-422, alpha1 440-459, beta1 212-222, beta1 304-333, beta1 344-363, and beta1 381-400 within the predicted dimerization region are involved in the process of heterodimerization and therefore in expression of functional sGC
two nucleotide-binding sites with high and low affinity for GMP-CPP, one of the two sites constitutes the substrate site responsible for catalysis. The other site is the pseudosymmetric site, which exclusively serves as the binding site for YC-1 or BAY 41-2272