G-Proteins and Type III Adenylyl Cyclase During Rat Olfactory Epithelium Ontogeny

1994 ◽  
pp. 141-144 ◽  
Author(s):  
Bert P. M. Menco ◽  
Francesca D. Tekula ◽  
Albert I. Farbman ◽  
Waleed Danho

Neuron ◽  
2000 ◽  
Vol 27 (3) ◽  
pp. 487-497 ◽  
Author(s):  
Scott T. Wong ◽  
Kien Trinh ◽  
Beth Hacker ◽  
Guy C.K. Chan ◽  
Graeme Lowe ◽  
...  


1992 ◽  
Vol 12 (10) ◽  
pp. 4687-4693
Author(s):  
G Kalinec ◽  
A J Nazarali ◽  
S Hermouet ◽  
N Xu ◽  
J S Gutkind

The discovery of mutated, GTPase-deficient alpha subunits of Gs or Gi2 in certain human endocrine tumors has suggested that heterotrimeric G proteins play a role in the oncogenic process. Expression of these altered forms of G alpha s or G alpha i2 proteins in rodent fibroblasts activates or inhibits endogenous adenylyl cyclase, respectively, and causes certain alterations in cell growth. However, it is not clear whether growth abnormalities result from altered cyclic AMP synthesis. In the present study, we asked whether a recently discovered family of G proteins, Gq, which does not affect adenylyl cyclase activity, but instead mediates the activation of phosphatidylinositol-specific phospholipase C harbors transforming potential. We mutated the cDNA for the alpha subunit of murine Gq in codons corresponding to a region involved in binding and hydrolysis of GTP. Similar mutations unmask the transforming potential of p21ras or activate the alpha subunits of Gs or Gi2. Our results show that when expressed in NIH 3T3 cells, activating mutations convert G alpha q into a dominant acting oncogene.



2011 ◽  
Vol 31 (17) ◽  
pp. 6576-6586 ◽  
Author(s):  
T. R. Henion ◽  
A. A. Faden ◽  
T. K. Knott ◽  
G. A. Schwarting


1998 ◽  
Vol 804 (1) ◽  
pp. 52-62 ◽  
Author(s):  
Kimberly A Leite-Morris ◽  
Gary B Kaplan ◽  
Jonathan G Smith ◽  
Mary T Sears


1998 ◽  
Vol 274 (2) ◽  
pp. H416-H423 ◽  
Author(s):  
Sujata Persad ◽  
Heinz Rupp ◽  
Rashi Jindal ◽  
Jugpal Arneja ◽  
Naranjan S. Dhalla

From the role of oxidative stress in cardiac dysfunction, we investigated the effect of H2O2, an activated species of oxygen, on β-adrenoceptors, G proteins, and adenylyl cyclase activities. Rat heart membranes were incubated with different concentrations of H2O2before the biochemical parameters were measured. Both the affinity and density of β1-adrenoceptors were decreased, whereas the density of the β2-adrenoceptors was decreased and the affinity was increased by 1 mM H2O2. Time- and concentration-dependent biphasic changes in adenylyl cyclase activities in the absence or presence of isoproterenol were observed when membranes were incubated with H2O2; however, activation of the enzyme by isoproterenol was increased or unaltered. The adenylyl cyclase activities in the absence or presence of forskolin, NaF, and Gpp(NH)p were depressed by H2O2. Catalase alone or in combination with mannitol was able to significantly decrease the magnitude of alterations due to H2O2. The cholera toxin-stimulated adenylyl cyclase activity and ADP ribose labeling of Gs proteins were decreased by treatment with 1 mM H2O2, whereas Gi protein activities, as reflected by pertussis toxin-stimulation of adenylyl cyclase and ADP ribosylation, were unaltered. The Gs and Gi protein immunoreactivities, estimated by labeling with respective antibodies, indicate a decrease in binding to the 45-kDa band of Gs protein, whereas no change in the binding of antibodies to the 52-kDa band of Gs protein or the 40-kDa subunit of Gi protein was evident when the membranes were treated with 1 mM H2O2. These results suggest that H2O2in high concentrations may attenuate the β-adrenoceptor-linked signal transduction in the heart by changing the functions of Gs proteins and the catalytic subunit of the adenylyl cyclase enzyme.



2000 ◽  
Vol 57 (4) ◽  
pp. 820-825 ◽  
Author(s):  
Michael L. Bayewitch ◽  
Igal Nevo ◽  
Tomer Avidor-Reiss ◽  
Rivka Levy ◽  
William F. Simonds ◽  
...  


1992 ◽  
Vol 57 (0) ◽  
pp. 145-148 ◽  
Author(s):  
H.R. Bourne ◽  
K.D. Lustig ◽  
Y.H. Wong ◽  
B.R. Conklin
Keyword(s):  




1995 ◽  
Vol 268 (2) ◽  
pp. L221-L229 ◽  
Author(s):  
H. Kume ◽  
K. Mikawa ◽  
K. Takagi ◽  
M. I. Kotlikoff

We have examined the functional consequences of G protein coupling to calcium-activated potassium (KCa) channels using isometric tension records from guinea pig tracheal smooth muscle. After incubation with 1 microgram/ml pertussis toxin (PTX) for 6 h, the contraction response to 1 microM methacholine (MCh) was suppressed by 31.7 +/- 5.0% (n = 10). Similarly, the contraction was inhibited by 29.1 +/- 5.0% (n = 6) after application of 0.1 microM AF-DX 116, an M2-selective muscarinic receptor antagonist. Cholera toxin (CTX, 2.0 micrograms/ml for 6 h), which activates the stimulatory G protein of adenylyl cyclase (Gs), also suppressed contraction by 43.9 +/- 3.3% (n = 11). The inhibitory effects of PTX, AF-DX 116, or CTX were reversed in the presence of 100 nM charybdotoxin (ChTX), a selective KCa channel inhibitor. These findings suggest that disruption of inhibitory coupling between muscarinic receptor and KCa channels mediated by PTX-sensitive G proteins, or KCa channel activation induced by Gs/adenylyl cyclase-linked processes, antagonizes muscarinic contraction. The isoproterenol concentration-inhibition curves for precontracted trachea (1 microM MCh) were shifted to the left after perfusion with PTX or AF-DX 116, and the leftward shift of the curve was blocked by ChTX. Thus direct or indirect regulation of KCa channels mediated by the inhibitory guanine nucleotide binding protein (Gi) and Gs may play a functionally important role in the mechanical antagonism by the two receptor agonists.



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