Receptor guanylyl cyclase (RGC) family in GtoPdb v.2021.3

The mammalian genome encodes seven guanylyl cyclases, GC-A to GC-G, that are homodimeric transmembrane receptors activated by a diverse range of endogenous ligands. These enzymes convert guanosine-5'-triphosphate to the intracellular second messenger cyclic guanosine-3',5'-monophosphate (cyclic GMP). GC-A, GC-B and GC-C are expressed predominantly in the cardiovascular system, skeletal system and intestinal epithelium, respectively. GC-D and GC-G are found in the olfactory neuropepithelium and Grueneberg ganglion of rodents, respectively. GC-E and GC-F are expressed in retinal photoreceptors.

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Receptor guanylyl cyclase (RGC) family (version 2019.4) in the IUPHAR/BPS Guide to Pharmacology Database

IUPHAR/BPS Guide to Pharmacology CITE ◽

10.2218/gtopdb/f1022/2019.4 ◽

2019 ◽

Vol 2019 (4) ◽

Author(s):

Annie Beuve ◽

Peter Brouckaert ◽

John C. Burnett, Jr. ◽

Andreas Friebe ◽

John Garthwaite ◽

...

Keyword(s):

Cyclic Gmp ◽

Guanylyl Cyclase ◽

Enzyme Activities ◽

Second Messenger ◽

Mammalian Genome ◽

Soluble Receptor ◽

Guanylyl Cyclases

The mammalian genome encodes transmembrane and soluble receptor guanylyl cyclases, both of which have enzyme activities which convert guanosine-5'-triphosphate to the intracellular second messenger cyclic guanosine-3',5'-monophosphate (cyclic GMP).

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EFFECTS OF LIGHT ON CYCLIC GMP METABOLISM IN RETINAL PHOTORECEPTORS

Journal of Neurochemistry ◽

10.1111/j.1471-4159.1976.tb10399.x ◽

1976 ◽

Vol 27 (3) ◽

pp. 717-722 ◽

Cited By ~ 57

Author(s):

G. Krishna ◽

N. Krishnan ◽

R. T. Fletcher ◽

G. Chader

Keyword(s):

Cyclic Gmp ◽

Retinal Photoreceptors

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Enzymatic Relay Mechanism Stimulates Cyclic GMP Synthesis in Rod Photoresponse: Biochemical and Physiological Study in Guanylyl Cyclase Activating Protein 1 Knockout Mice

PLoS ONE ◽

10.1371/journal.pone.0047637 ◽

2012 ◽

Vol 7 (10) ◽

pp. e47637 ◽

Cited By ~ 37

Author(s):

Clint L. Makino ◽

Xiao-Hong Wen ◽

Elena V. Olshevskaya ◽

Igor V. Peshenko ◽

Andrey B. Savchenko ◽

...

Keyword(s):

Cyclic Gmp ◽

Guanylyl Cyclase ◽

Knockout Mice ◽

Physiological Study

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Asterosap, an Egg Jelly Peptide, Elevate Intracellular Ca2+ and Activate the Motility of Spermatozoa

Progressive Agriculture ◽

10.3329/pa.v19i1.17358 ◽

2013 ◽

Vol 19 (1) ◽

pp. 79-88 ◽

Cited By ~ 1

Author(s):

MS Islam ◽

T Akhter ◽

M Matsumoto

Keyword(s):

Plasma Membrane ◽

Cyclic Gmp ◽

Guanylyl Cyclase ◽

Acrosome Reaction ◽

Nickel Chloride ◽

Selective Inhibitor ◽

Ion Flux ◽

Intracellular Ca ◽

A Cell ◽

Egg Jelly

Components from the outer envelopes of the egg that influence the flagellar beating and acrosome reaction of spermatozoa are regulated by ion flux across the plasma membrane. Asterosap, a sperm-activating peptide from the starfish egg jelly layer, causes a transient increase in intracellular cyclic GMP (cGMP) through the activation of the asterosap receptor, a guanylyl cyclase (GC), and causes an increase in intracellular Ca2+. Here we describe the pathway of asterosap-induced Ca2+ elevation using different Ca2+ channel antagonists. Fluo-4 AM, a cell permeable Ca2+ sensitive dye was used to determine the channel caused by the asterosap-induced Ca2+ elevation in spermatozoa. Different L-type Ca2+ channel antagonists, a non specific Ca2+ channel antagonist (nickel chloride), and a store-operated Ca2+ channel (SOC) antagonist do not show any significant response on asterosap-induced Ca2+ elevation, whereas KB-R7943, a selective inhibitor against Na+/Ca2+ exchanger (NCX) inhibited effectively. We also analyzed the flagellar movement of spermatozoa in artificial seawater (ASW) containing the asterosap at 100 nM ml?1. We found that spermatozoa swam vigorously with more symmetrical flagellar movement in asterosap than in ASW and KB-R7943 significantly inhibited the flagellar movement.DOI: http://dx.doi.org/10.3329/pa.v19i1.17358 Progress. Agric. 19(1): 79 - 88, 2008

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Effects of the soluble guanylyl cyclase activator, YC-1, on vascular tone, cyclic GMP levels and phosphodiesterase activity

British Journal of Pharmacology ◽

10.1038/sj.bjp.0702495 ◽

1999 ◽

Vol 127 (1) ◽

pp. 195-203 ◽

Cited By ~ 138

Author(s):

Jan Galle ◽

Ulrike Zabel ◽

Ulrich Hübner ◽

Armin Hatzelmann ◽

Birgit Wagner ◽

...

Keyword(s):

Cyclic Gmp ◽

Guanylyl Cyclase ◽

Vascular Tone ◽

Soluble Guanylyl Cyclase ◽

Phosphodiesterase Activity ◽

Cyclase Activator

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Abstract 556: The Soluble Guanylyl Cyclase Activator Bay 60-2770 Inhibits Arterial Smooth Muscle Cell Migration in Protein Kinase G-dependent Manner

Arteriosclerosis Thrombosis and Vascular Biology ◽

10.1161/atvb.36.suppl_1.556 ◽

2016 ◽

Vol 36 (suppl_1) ◽

Author(s):

Andrew Holt ◽

Danielle Martin ◽

Patti Shaver ◽

Shaquria Adderley ◽

Joshua Stone ◽

...

Keyword(s):

Smooth Muscle ◽

Cell Migration ◽

Protein Kinase ◽

Cyclic Gmp ◽

Guanylyl Cyclase ◽

Soluble Guanylyl Cyclase ◽

Protein Kinase G ◽

Growth Disorders ◽

Arterial Smooth Muscle ◽

Cyclase Activator

Atherosclerotic lower extremity peripheral artery disease (PAD) is among the most prevalent, morbid and mortal of all cardiovascular disorders. Pathologic arterial smooth muscle (ASM) cell migration is a major component of atherogenic PAD and efforts aimed at attenuating its progression are clinically essential. Cyclic nucleotide signaling has long been studied for its growth-mitigating properties in the setting of PAD and other vascular growth disorders. In this study we hypothesized that the novel, heme-independent soluble guanylyl cyclase activator BAY 60-2770 (BAY) inhibits ASM cell migration through phosphorylation of the protein kinase G (PKG) target and actin-binding protein vasodilator-stimulated phosphoprotein (VASP). In a rat model of injury-induced arterial growth, BAY significantly reduced neointima formation and luminal narrowing compared to vehicle (Veh)-treated control arteries after 2 weeks. Using rat and human ASM cells BAY significantly attenuated cell migration, reduced G:F actin, and increased cyclic GMP content, PKG activity and phosphorylated VASP at Ser239 (pVASP.S239) compared to Veh controls. Using site-directed mutagenesis, both full-length VASP-overexpressing (wild type, WT) and VASP.S239 phosphorylation-resistant mutants showed significantly reduced cell migration compared to naïve controls, however, there was no effect on cell migration between either VASP transfected group in the presence of BAY. Interestingly, both VASP mutants showed significantly increased PKG activity compared to naïve cells, and in turn pharmacologic PKG blockade in the presence of BAY fully reversed the inhibitory effect of BAY alone on cell migration. These data suggest BAY has capacity to inhibit ASM cell migration through cyclic GMP/PKG/VASP signaling yet through mechanisms independent of pVASP.S239. Findings from this study implicate BAY via cyclic GMP/PKG/VASP as a potential pharmacotherapeutic agent against aberrant ASM growth disorders such as PAD.

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Hereditary Retinal Disease-Related Retinal Detachment; Risk Factors, Pathogenesis, Clinic, and Management

Güncel Retina Dergisi (Current Retina Journal) ◽

10.37783/crj-0219 ◽

2020 ◽

pp. 193-200

Keyword(s):

Risk Factors ◽

Retinal Detachment ◽

Cardiovascular System ◽

Proliferative Vitreoretinopathy ◽

Delayed Diagnosis ◽

Retinal Disease ◽

Skeletal System ◽

Younger Age ◽

Hereditary Retinal Disease

Hereditary retinal disease (HRD) is a group of pathologies characterized by histologically abnormally developing vitreous gel associated with peripheral retinal degenerative or proliferative changes. In HRD alterations in the structure of the vitreous with abnormal vitreoretinal adhesions can predispose to developing Retinal Detachment (RD). Many HRD is seen with a part of syndromes most of which have systemic abnormalities affecting the joints, skeletal system, and cardiovascular system. Due to delayed diagnosis in younger age patients, without prominent symptoms, most patients with HR presented with proliferative vitreoretinopathy PVR and macula-involving RD.

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Cytoprotective effect of 1-nitro-2-phenylethane in mice pancreatic acinar cells subjected to taurocholate: Putative role of guanylyl cyclase-derived 8-nitro-cyclic-GMP

Biochemical Pharmacology ◽

10.1016/j.bcp.2014.07.030 ◽

2014 ◽

Vol 91 (2) ◽

pp. 191-201 ◽

Cited By ~ 9

Author(s):

François Cosker ◽

Francisco J.B. Lima ◽

Saad Lahlou ◽

Pedro J.C. Magalhães

Keyword(s):

Cyclic Gmp ◽

Guanylyl Cyclase ◽

Acinar Cells ◽

Pancreatic Acinar Cells ◽

Cytoprotective Effect ◽

Putative Role

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Effect of inhibitors of glutathione S-transferase on glyceryl trinitrate activity in isolated rat aorta

Canadian Journal of Physiology and Pharmacology ◽

10.1139/y93-025 ◽

1993 ◽

Vol 71 (2) ◽

pp. 179-184 ◽

Cited By ~ 19

Author(s):

Rita Nigam ◽

Tracy Whiting ◽

Brian M. Bennett

Keyword(s):

Glyceryl Trinitrate ◽

Cyclic Gmp ◽

Guanylyl Cyclase ◽

Rat Aorta ◽

Supernatant Fraction ◽

Organic Nitrates ◽

Transferase Activity ◽

Glutathione S Transferase ◽

Glutathione S Transferases

We investigated the role of glutathione S-transferases (enzymes known to biotransform organic nitrates) in the vascular action of glyceryl trinitrate (GTN). Relaxation of phenylephrine-contracted rat aortic strips was assessed in the presence or absence of the glutathione S-transferase inhibitors Basilen Blue, bromosulfophthalein, Rose Bengal, hematin, chlorotriphenyltin, and (octyloxy)benzoylvinylglutathione. Whereas none of the inhibitors increased the EC50 for GTN relaxation, glutathione S-transferase activity in the 100 000 × g supernatant fraction of rat aorta was inhibited markedly by most of the inhibitors. In addition, GTN-stimulated activation of aortic guanylyl cyclase in broken-cell preparations was attenuated by all of the glutathione S-transferase inhibitors, suggesting a direct inhibitory action on guanylyl cyclase. In other experiments using aortic strips preexposed to phenylephrine, the inhibitors had no effect on GTN-induced cyclic GMP accumulation or on vascular biotransformation of GTN. In contrast, both Basilen Blue and bromosulfophthalein significantly inhibited GTN-induced relaxation of K+-contracted aortic strips, and Basilen Blue significantly inhibited GTN biotransformation in aortic strips preexposed to 25 mM K+. This may be due to a more favourable electrochemical gradient for entry of the inhibitors into membrane-depolarized tissues. We conclude that vascular glutathione S-transferases play a role in mediating the vasodilator actions of GTN in intact tissues in vitro, but that this appears to depend upon the nature of the contractile agent used in such studies.Key words: glyceryl trinitrate, glutathione S-transferase, cyclic GMP, vascular smooth muscle, biotransformation.

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