Molecular Scanning of the α Subunit of the Stimulatory G Protein Gene in Essential Hypertension

1995 ◽  
Vol 88 (s32) ◽  
pp. 24P-24P
Author(s):  
H Jia ◽  
AD Hingorani ◽  
PA Stevens ◽  
S Monteith ◽  
MJ Brown
Keyword(s):  
Essential Hypertension ◽  
G Protein ◽  
Protein Gene ◽  
Α Subunit ◽  
Stimulatory G Protein

Altered myocardial Gs protein and adenylyl cyclase signaling in rats exposed to chronic hypoxia and normoxic recovery

2003 ◽  
Vol 94 (6) ◽  
pp. 2423-2432 ◽  
Author(s):  
Markéta Hrbasová ◽  
Jiri Novotny ◽  
Lucie Hejnová ◽  
František Kolář ◽  
Jan Neckář ◽  
...  
Keyword(s):  
Adenylyl Cyclase ◽  
G Protein ◽  
Contractile Function ◽  
Left Ventricular ◽  
Adaptation To Hypoxia ◽  
Adrenergic Stimulation ◽  
Α Subunit ◽  
Stimulatory G Protein ◽  
Membrane Bound ◽  
The Right

The present work has analyzed the consequences of chronic intermittent high-altitude hypoxia for functioning of the G protein-mediated adenylyl cyclase (AC) signaling system in the right (RV) and left ventricular (LV) myocardium in rats. Adaptation to hypoxia did not appreciably affect the number of β-adrenoceptors and the content of predominantly membrane-bound α-subunit (Gsα) of the stimulatory G protein, but it raised the amount of cytosolic Gsα in RV. The levels of myocardial inhibitory Gα protein were not altered. Activity of AC stimulated by GTP, fluoride, forskolin, or isoprotertenol was reduced by ∼50% in RV from chronically hypoxic rats, and a weaker depression was also found in LV. In addition, hypoxia significantly diminished a functional activity of membrane-bound Gsα in both RV and LV. The RV baseline contractile function was markedly increased in chronically hypoxic animals, and its sensitivity to β-adrenergic stimulation was decreased. Animals recovering from hypoxia for 5 wk still exhibited markedly elevated levels of cytosolic Gsα and significantly lower activity of AC in RV than did age-matched controls, but contractile responsiveness to β-agonists was normal.

scholarly journals Receptor-Mediated Adenylyl Cyclase Activation Through XLαs, the Extra-Large Variant of the Stimulatory G Protein α-Subunit

2002 ◽  
Vol 16 (8) ◽  
pp. 1912-1919 ◽  
Author(s):  
Murat Bastepe ◽  
Yasemin Gunes ◽  
Beatriz Perez-Villamil ◽  
Joy Hunzelman ◽  
Lee S. Weinstein ◽  
...  
Keyword(s):  
Adenylyl Cyclase ◽  
G Protein ◽  
Adrenergic Receptor ◽  
Α Subunit ◽  
Exon 2 ◽  
Amino Terminal ◽  
Stimulatory G Protein ◽  
Β2 Adrenergic Receptor ◽  
Carboxyl Terminal ◽  
G Protein Α Subunit

Abstract XLαs, the large variant of the stimulatory G protein α subunit (Gsα), is derived from GNAS1 through the use of an alternative first exon and promoter. Gsα and XLαs have distinct amino-terminal domains, but are identical over the carboxyl-terminal portion encoded by exons 2–13. XLαs can mimic some functions of Gsα, including βγ interaction and adenylyl cyclase stimulation. However, previous attempts to demonstrate coupling of XLαs to typically Gs-coupled receptors have not been successful. We now report the generation of murine cell lines that carry homozygous disruption of Gnas exon 2, and are therefore null for endogenous XLαs and Gsα (GnasE2−/E2−). GnasE2−/E2− cells transfected with plasmids encoding XLαs and different heptahelical receptors, including the β2-adrenergic receptor and receptors for PTH, TSH, and CRF, showed agonist-mediated cAMP accumulation that was indistinguishable from that observed with cells transiently coexpressing Gsα and these receptors. Our findings thus indicate that XLαs is capable of functionally coupling to receptors that normally act via Gsα.

scholarly journals Ric-8B Stabilizes the α Subunit of Stimulatory G Protein by Inhibiting Its Ubiquitination

2010 ◽  
Vol 285 (15) ◽  
pp. 11114-11120 ◽  
Author(s):  
Yusuke Nagai ◽  
Akiyuki Nishimura ◽  
Kenji Tago ◽  
Norikazu Mizuno ◽  
Hiroshi Itoh
Keyword(s):  
G Protein ◽  
Α Subunit ◽  
Stimulatory G Protein

scholarly journals Adenylyl cyclases (ACs) (version 2019.4) in the IUPHAR/BPS Guide to Pharmacology Database

2019 ◽  
Vol 2019 (4) ◽  
Author(s):  
Carmen W. Dessauer ◽  
Rennolds Ostrom ◽  
Roland Seifert ◽  
Val J. Watts
Keyword(s):  
Cyclic Amp ◽  
Adenylyl Cyclase ◽  
G Protein ◽  
Adenylyl Cyclases ◽  
Adenylyl Cyclase Activity ◽  
Α Subunit ◽  
Soluble Adenylyl Cyclase ◽  
Catalytic Domains ◽  
Stimulatory G Protein ◽  
Membrane Spanning

Adenylyl cyclase, E.C. 4.6.1.1, converts ATP to cyclic AMP and pyrophosphate. Mammalian membrane-delimited adenylyl cyclases (nomenclature as approved by the NC-IUPHAR Subcommittee on Adenylyl cyclases [9]) are typically made up of two clusters of six TM domains separating two intracellular, overlapping catalytic domains that are the target for the nonselective activators Gαs (the stimulatory G protein α subunit) and forskolin (except AC9, [21]). adenosine and its derivatives (e.g. 2',5'-dideoxyadenosine), acting through the P-site,are inhibitors of adenylyl cyclase activity [27]. Four families of membranous adenylyl cyclase are distinguishable: calmodulin-stimulated (AC1, AC3 and AC8), Ca2+- and Gβγ-inhibitable (AC5, AC6 and AC9), Gβγ-stimulated and Ca2+-insensitive (AC2, AC4 and AC7), and forskolin-insensitive (AC9) forms. A soluble adenylyl cyclase (AC10) lacks membrane spanning regions and is insensitive to G proteins.It functions as a cytoplasmic bicarbonate (pH-insensitive) sensor [5].

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