Human gastric mucosal adenylate cyclase: Activation by histamine-H2-receptor stimulation and inhibition by cimetidine in vitro and in peptic ulcer patients

1979 ◽  
Vol 15 (3) ◽  
pp. 147-151 ◽  
Author(s):  
H. -J. Ruoff ◽  
M. Becker ◽  
B. Painz ◽  
M. Rack ◽  
K. -Fr. Sewing ◽  
...  
Keyword(s):  
Peptic Ulcer ◽  
Adenylate Cyclase ◽  
Receptor Stimulation ◽  
Histamine H2 Receptor ◽  
H2 Receptor ◽  
Cyclase Activation ◽  
Adenylate Cyclase Activation

scholarly journals A pharmacologically distinct cyclic AMP receptor is responsible for the regulation of gp80 expression in Dictyostelium discoideum.

1990 ◽  
Vol 10 (7) ◽  
pp. 3297-3306 ◽  
Author(s):  
P C Ma ◽  
C H Siu
Keyword(s):  
Cyclic Amp ◽  
Adenylate Cyclase ◽  
Dictyostelium Discoideum ◽  
Surface Glycoprotein ◽  
Intracellular Camp ◽  
Cell Surface Glycoprotein ◽  
Cyclase Activation ◽  
Adenylate Cyclase Activation ◽  
Camp Receptor

The EDTA-resistant cell-cell adhesion expressed at the aggregation stage of Dictyostelium discoideum is mediated by a cell surface glycoprotein of Mr 80,000 (gp80). The expression of gp80 is developmentally regulated by cyclic AMP (cAMP). In vitro nuclear run-on experiments show that transcription of the gp80 gene is initiated soon after the onset of development. The basal level of gp80 transcription is significantly augmented by exogenous cAMP pulses. Interestingly, in analog studies, 2'-deoxy-cAMP, 8-bromo-cAMP, and N6-monobutyryl-cAMP are all capable of inducing a rapid accumulation of gp80 mRNA, suggesting the presence of a unique cAMP receptor that responds equally well to these analogs. To determine whether intracellular cAMP plays a role in the regulation of gp80 expression, caffeine was used to block cAMP-induced receptor-mediated adenylate cyclase activation. Expression of gp80 mRNA was blocked in caffeine-treated cells but could be substantially restored by treatment with exogenous cAMP pulses, suggesting that adenylate cyclase activation is not required. gp80 expression was also examined in the signal transduction mutants synag 7 and frigid A. In both mutants, gp80 was expressed at the basal level. Pulses of cAMP as well as 2'-deoxy-cAMP and N6-monobutyryl-cAMP were capable of restoring the normal level of gp80 expression in synag 7 cells. These results, taken together, indicate bimodal regulation of gp80 expression during development and the involvement of a novel cAMP receptor in the transmembrane signalling pathway that regulates gp80 gene expression.

A pharmacologically distinct cyclic AMP receptor is responsible for the regulation of gp80 expression in Dictyostelium discoideum

1990 ◽  
Vol 10 (7) ◽  
pp. 3297-3306
Author(s):  
P C Ma ◽  
C H Siu
Keyword(s):  
Cyclic Amp ◽  
Adenylate Cyclase ◽  
Dictyostelium Discoideum ◽  
Surface Glycoprotein ◽  
Intracellular Camp ◽  
Cell Surface Glycoprotein ◽  
Cyclase Activation ◽  
Adenylate Cyclase Activation ◽  
Camp Receptor

The EDTA-resistant cell-cell adhesion expressed at the aggregation stage of Dictyostelium discoideum is mediated by a cell surface glycoprotein of Mr 80,000 (gp80). The expression of gp80 is developmentally regulated by cyclic AMP (cAMP). In vitro nuclear run-on experiments show that transcription of the gp80 gene is initiated soon after the onset of development. The basal level of gp80 transcription is significantly augmented by exogenous cAMP pulses. Interestingly, in analog studies, 2'-deoxy-cAMP, 8-bromo-cAMP, and N6-monobutyryl-cAMP are all capable of inducing a rapid accumulation of gp80 mRNA, suggesting the presence of a unique cAMP receptor that responds equally well to these analogs. To determine whether intracellular cAMP plays a role in the regulation of gp80 expression, caffeine was used to block cAMP-induced receptor-mediated adenylate cyclase activation. Expression of gp80 mRNA was blocked in caffeine-treated cells but could be substantially restored by treatment with exogenous cAMP pulses, suggesting that adenylate cyclase activation is not required. gp80 expression was also examined in the signal transduction mutants synag 7 and frigid A. In both mutants, gp80 was expressed at the basal level. Pulses of cAMP as well as 2'-deoxy-cAMP and N6-monobutyryl-cAMP were capable of restoring the normal level of gp80 expression in synag 7 cells. These results, taken together, indicate bimodal regulation of gp80 expression during development and the involvement of a novel cAMP receptor in the transmembrane signalling pathway that regulates gp80 gene expression.

scholarly journals Interaction between the two signal transduction systems of the histamine H2 receptor: desensitizing and sensitizing effects of histamine stimulation on histamine-dependent cAMP production in Chinese hamster ovary cells

1996 ◽  
Vol 320 (1) ◽  
pp. 27-32 ◽  
Author(s):  
Yasushi FUKUSHIMA ◽  
Tomoichiro ASANO ◽  
Hideki KATAGIRI ◽  
Makoto AIHARA ◽  
Toshihito SAITOH ◽  
...  
Keyword(s):  
Adenylate Cyclase ◽  
Chinese Hamster Ovary ◽  
Chinese Hamster Ovary Cells ◽  
Chinese Hamster ◽  
Camp Production ◽  
Histamine H2 Receptor ◽  
H2 Receptor ◽  
H2 Receptors ◽  
Sensitizing Effect ◽  
Pkc Activation

The histamine H2 receptor is a member of the family of G-protein-coupled receptors and is linked to the activation of adenylate cyclase phospholipase C (PLC). In this study we examined the effects of protein kinase C (PKC) activation in Chinese hamster ovary (CHO) cells stably expressing canine histamine H2 receptors. Pretreatment with 100 nM phorbol 12-myristate 13-acetate at 37 °C for 15 min led to significant potentiation of histamine-dependent and forskolin-dependent cAMP production, whereas the biologically inactive phorbol ester, 4α-phorbol 12,13-didecanoate, was without effect. These potentiating effects were abolished by preincubation with 0.5 µM bisindolylmaleimide, a PKC inhibitor. Thus the activation of PKCs seems to be involved in the potentiation of cAMP production by acting on a post-receptor mechanism. Preincubation of a CHO cell line, CHO-H2R, with 10 µM histamine for 30 min had two effects. Maximal histamine-dependent cAMP production and forskolin-dependent cAMP production were potentiated by 36% and 105.2% respectively. The other effect was a desensitization of the histamine-dependent adenylate cyclase response as demonstrated by a three-fold increase in EC50. Administration of 0.5 µM bisindolylmaleimide before preincubation of CHO-H2R with 10 µM histamine did not alter the desensitizing effect on cAMP production, but did abolish the sensitizing effect. Preincubation of CHO-H2R cells with 10 nM histamine resulted in moderate potentiation, which was also abolished by bisindolylmaleimide, but not in desensitization of the histamine-dependent cAMP production. Thus these results suggest that preincubation with histamine had a sensitizing effect on cAMP production mediated by PLC and PKC activation, as well as a desensitizing effect on the H2 receptor. The former effect is dependent on the intensity of PLC and PKC signals delivered by H2 receptors. The latter effect requires a higher concentration of histamine.

scholarly journals Effects of Topical Adenosine Analogs and Forskolin on Rat Pial Arterioles in vivo

1991 ◽  
Vol 11 (1) ◽  
pp. 72-76 ◽  
Author(s):  
Setsuro Ibayashi ◽  
Al C. Ngai ◽  
Joseph R. Meno ◽  
H. Richard Winn
Keyword(s):  
Adenylate Cyclase ◽  
Adenosine Analogs ◽  
Cyclase Activation ◽  
Window Technique ◽  
Adenylate Cyclase Activation ◽  
Pial Arterioles ◽  
Adenosine Agonists ◽  
Cerebral Vasodilation

We utilized the closed window technique to study the in vivo responses of rat pial arterioles to superfused adenosine agonists. Adenosine and its analogs dilated pial arterioles and exhibited the following order of potency: 5′ N-ethylcarboxamide adenosine (NECA) > 2-chloroadenosine (2-CADO) > adenosine = R-N6-phenylisopropyladenosine ( R-PIA) = S-PIA > N6-cyclohexyladenosine (CHA). This potency profile suggests that cerebral vasodilation is mediated through the A2 receptor. Forskolin (10−9 M) potentiated the vasodilation caused by 10−6 M NECA, thus implicating adenylate cyclase activation during NECA-induced vasodilation and providing further support for involvement of the A2 receptor.

Six git genes encode a glucose-induced adenylate cyclase activation pathway in the fission yeast Schizosaccharomyces pombe

1993 ◽  
Vol 105 (4) ◽  
pp. 1095-1100 ◽  
Author(s):  
S.M. Byrne ◽  
C.S. Hoffman
Keyword(s):  
Adenylate Cyclase ◽  
Schizosaccharomyces Pombe ◽  
Glucose Repression ◽  
Signal Transduction Pathway ◽  
Activation Pathway ◽  
Cyclase Activation ◽  
Adenylate Cyclase Activation ◽  
Before And After ◽  
Dependent Protein ◽  
Camp Levels

An important eukaryotic signal transduction pathway involves the regulation of the effector enzyme adenylate cyclase, which produces the second messenger, cAMP. Previous genetic analyses demonstrated that glucose repression of transcription of the Schizosaccharomyces pombe fbp1 gene requires the function of adenylate cyclase, encoded by the git2 gene. As mutations in git2 and in six additional git genes are suppressed by exogenous cAMP, these ‘upstream’ git genes were proposed to act to produce a glucose-induced cAMP signal. We report here that assays of cAMP levels in wild-type and various mutant S. pombe cells, before and after exposure to glucose, show that this is the case. The data suggest that the cAMP signal results from the activation of adenylate cyclase. Therefore these ‘upstream’ git genes appear to encode a glucose-induced adenylate cyclase activation pathway. Assays of cAMP on a strain carrying a mutation in the git6 gene, which acts downstream of adenylate cyclase, indicate that git6 may function to feedback regulate adenylate cyclase activity. Thus git6 may encode a cAMP-dependent protein kinase.

Effects of Adenylate Cyclase Activation on Electrical Resistance of Scala Media

1993 ◽  
Vol 113 (sup501) ◽  
pp. 76-79 ◽  
Author(s):  
Katsumi Doi ◽  
Nozomu Mori ◽  
Toru Matsunaga
Keyword(s):  
Adenylate Cyclase ◽  
Electrical Resistance ◽  
Cyclase Activation ◽  
Adenylate Cyclase Activation
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