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In conclusion, rare coding variants in GUCY1A3 lead to reduced cGMP formation which can be rescued by a soluble guanylyl cyclase stimulator in vitro
Rs7692387 is located in an intronic site that modulates GUCY1A3 promoter activity. The transcription factor ZEB1 binds preferentially to the nonrisk allele, leading to an increase in GUCY1A3 expression, higher sGC (show SGCB Proteins) levels, and higher sGC (show SGCB Proteins) activity after stimulation.
Mutations in the GUCY1A3 gene are associated with moyamoya disease, achalasia, and hypertension.
Expression of the alpha1-A680T sGC (show SGCB Proteins) variant in reporter cells resulted in higher cyclic guanosine monophosphate production compared with the wild-type enzyme and the purified alpha1-A680T sGC (show SGCB Proteins) exhibited enhanced sensitivity to nitric oxide in vitro.
Dynamic interplay between hsp90 (show HSP90 Proteins), apo (show C9orf3 Proteins)-sGC (show SGCB Proteins)-beta1, and sGC (show SGCB Proteins)-alpha1 in response to NO is unprecedented and represent new steps by which cells can modulate the heme content and activity of sGC (show SGCB Proteins) for signaling cascades.
ZNF280B (show ZNF280B Proteins) upregulates GUCY1A3 expression and downregulates TP53 (show TP53 Proteins) in prostate cancer cells.
homozygous mutations in GUCY1A3, which encodes the alpha1 subunit of soluble guanylate cyclase, the major receptor for nitric oxide, might play a role in moyamoya and achalasia
The G-protein regulator LGN modulates the activity of the NO receptor soluble guanylate cyclase
GCS-alpha-1 regulation of p53 (show TP53 Proteins) activity is important in prostate cancer biology and may represent an important mechanism of p53 (show TP53 Proteins) down-regulation.
We concluded that the alpha-subunit (show POLG Proteins) and the beta(1)(191-619) domain exert structural strains on the heme domain.
Exogenous or paracrine sources of NO promote the specification towards the myocyte lineage and expression of cardiac sarcomeric proteins of adult cardiac progenitor cells. This is contingent upon the expression and activity of the alpha1 subunit of guanylyl cyclase in CPC that is necessary for NO-mediated inhibition of the canonical Wnt (show WNT2 Proteins)/beta-catenin (show CTNNB1 Proteins) pathway.
These data demonstrate that a reduction in cardiac sGC (show NPR1 Proteins) activity worsens doxorubicin-induced cardiotoxicity in mice and identify sGC (show NPR1 Proteins) as a potential therapeutic target.
We suggest that Gucy1a3 activity promotes the phenotypic switching of smooth muscle cells from a contractile to a synthetic state, fostering the formation of atherosclerosis.
The authors elucidated this dependency by showing that guanylate cyclase-1 is a novel rhodopsin-binding protein.
Cellular markers revealed that vascular SMC (show DYM Proteins) differentiation decreased, whereas myofibroblast activation increased in the hyperoxic sGC (show NPR1 Proteins)-alpha1 KO pup lung.
Soluble guanylate cyclase alpha1-deficient mice: a novel murine model for primary open angle glaucoma.
Male mice deficient in a NO receptor component, the alpha1 subunit of soluble guanylate cyclase (sGCalpha1), are prone to hypertension in some, but not all, mouse strains, suggesting that additional genetic factors contribute to the onset of hypertension
These data suggests a novel physiological role for PDE5 (show PDE5A Proteins) in restricting the effects of NOS3 (show NOS3 Proteins)/sGC (show NPR1 Proteins)/PKG (show PRKG1 Proteins) signaling pathway to modulating beta-AR stimulated I(Ca), while limiting effects on cardiac contraction.[sGC (show NPR1 Proteins)]
Pressure overload results in translocation of sGC (show NPR1 Proteins) out of membrane microdomains, depressing NO/heme-dependent activation in the heart, consistent with enhanced oxidation.
findings identify a crucial role of the NO/sGCalpha1beta1/cGMP pathway in modulating lymphatic vessel function [soluble guanylate cyclase alpha1beta1]
The N-terminal region of nitric oxide-sensitive guanylyl cyclase alpha 1 subunit(amino acids 61-128) is mandatory for quantitative dimerization.
Soluble guanylate cyclases are heterodimeric proteins that catalyze the conversion of GTP to 3',5'-cyclic GMP and pyrophosphate. The protein encoded by this gene is an alpha subunit of this complex and it interacts with a beta subunit to form the guanylate cyclase enzyme, which is activated by nitric oxide. Several transcript variants encoding a few different isoforms have been found for this gene.
guanylate cyclase 1, soluble, alpha 3
, guanylate cyclase soluble subunit alpha-3
, soluble guanylate cyclase large subunit alpha 1
, soluble guanylate cyclase 1 alpha 3
, guanylate cyclase soluble subunit alpha-3-like
, soluble guanylyl cyclase alpha subunit
, soluble guanylate cyclase large subunit
, alpha 1 sGC
, Guanylate cyclase soluble alpha 1 (GTP pyrophosphate - lyase)
, Guanylate cyclase, soluble, alpha 1 (GTP pyrophosphate - lyase)
, NO-sensitive GC alpha 1 subunit
, guanylate cyclase soluble subunit alpha-1
, larger subunit of soluble guanylyl cyclase
, nitric oxide-sensitive guanylyl cyclase alpha 1 subunit