scholarly journals Cyclic Adenosine Monophosphate (cAMP) Stimulation of the Kit Ligand Promoter in Sertoli Cells Requires an Sp1-Binding Region, a Canonical TATA Box, and a cAMP-Induced Factor Binding to an Immediately Downstream GC-Rich Element1

2003 ◽  
Vol 69 (6) ◽  
pp. 1979-1988 ◽  
Author(s):  
Paola Grimaldi ◽  
Federica Capolunghi ◽  
Raffaele Geremia ◽  
Pellegrino Rossi
Keyword(s):  
Sertoli Cells ◽  
Cyclic Adenosine Monophosphate ◽  
Adenosine Monophosphate ◽  
Tata Box ◽  
Binding Region ◽  
Factor Binding ◽  
Kit Ligand ◽  
Camp Stimulation ◽  
Stimulation Of

Protein kinase C activation and positive and negative agonist regulation of 3′, 5′-cyclic adenosine monophosphate levels in cultured rat Sertoli cells

1993 ◽  
Vol 128 (6) ◽  
pp. 568-572 ◽  
Author(s):  
Lars Eikvar ◽  
Kristin Austlid Taskén ◽  
Winnie Eskild ◽  
Vidar Hansson
Keyword(s):  
Sertoli Cells ◽  
Cyclic Adenosine Monophosphate ◽  
Adenosine Monophosphate ◽  
Dependent Manner ◽  
Camp Production ◽  
Camp Phosphodiesterase ◽  
Concentration Dependent Manner ◽  
Camp Formation ◽  
Pkc Activation ◽  
Stimulation Of

The present study examines the effects of 12-0-tetradecanoylphorbol-13-acetate (TPA) on agonist-regulated 3′, 5′-cyclic adenosine monophosphate (cAMP) formation and cAMP-mediated effects in cultured Sertoli cells from immature rats. Concentration-dependent stimulation of cAMP levels by follicle-stimulating hormone (FSH) was inhibited dramatically by the coaddition of 100 nmol/l TPA, which exerted a similar inhibition of glucagon- and isoproterenol-stimulated cAMP production. These results show that protein kinase C (PKC) activation by TPA attenuates Gs-protein-mediated agonist activation of cAMP production. (− )-N6(R)-Phenylisopropyladenosine (L-PIA), an A1-adenosine receptor agonist, inhibited cAMP stimulation by FSH in a concentration-dependent manner. When LPIA was added in increasing concentrations simultaneously with 100 nmol/l TPA, the L-PIA still inhibited FSH-stimulated cAMP production in a concentration-dependent manner. In the presence of TPA, the half-inhibitory concentration (IC50) for L-PIA inhibition of cAMP formation was reduced by more than one order of magnitude, indicating that PKC activation by TPA increases the sensitivity of Sertoli cells to G-protein-mediated agonist inhibition of cAMP production. The inhibitory effects of TPA on FSH-stimulated cAMP production were still observed when cAMP phosphodiesterase activity was inhibited by 1 mmol/l methylisobutylxanthine or when the activity of Gxi-protein was eliminated by pretreatment with 100 μg/l pertussis toxin. Taken together, the results indicate that PKC activation inhibits agonist-dependent stimulation of cAMP production by phosphorylation of components common to all the activating agonists used, and not via stimulation of Gi-protein activity or degradation of cAMP by cAMP phosphodiesterase activity. The increased sensitivity to L-PIA inhibition of cAMP formation induced by TPA may simply be a result of the reduced activity of the agonist-receptor/Gs-protein/C complex.

scholarly journals Increased intracellular cyclic adenosine monophosphate inhibits T lymphocyte-mediated cytolysis by two distinct mechanisms.

1988 ◽  
Vol 167 (6) ◽  
pp. 1963-1968 ◽  
Author(s):  
L S Gray ◽  
J Gnarra ◽  
E L Hewlett ◽  
V H Engelhard
Keyword(s):  
Cholera Toxin ◽  
T Lymphocyte ◽  
Pertussis Toxin ◽  
Target Cell ◽  
Cyclic Adenosine Monophosphate ◽  
Second Messenger ◽  
Adenosine Monophosphate ◽  
Dose Dependent Fashion ◽  
Dose Dependent ◽  
Stimulation Of

Cholera toxin (CT), but not pertussis toxin (PT), treatment of cloned murine CTL inhibited target cell lysis in a dose-dependent fashion. The effects of CT were mimicked by forskolin and cyclic adenosine monophosphate (cAMP) analogues. Inhibition of cytotoxicity by CT and cAMP analogs was mediated in part by attenuation of conjugate formation. Additionally, both CT and cAMP analogs blocked the increase in intracellular Ca2+ induced by stimulation of the TCR complex by mAbs. These findings indicate that cAMP inhibits the activity of CTL by two distinct mechanisms and suggests a role for this second messenger in CTL-mediated cytolysis.

Noradrenergic Stimulation of Cyclic Adenosine Monophosphate in Rat Purkinje Neurons: An Immunocytochemical Study

Science ◽  
1973 ◽  
Vol 179 (4073) ◽  
pp. 585-588 ◽  
Author(s):  
G. R. Siggins ◽  
E. F. Battenberg ◽  
B. J. Hoffer ◽  
F. E. Bloom ◽  
A. L. Steiner
Keyword(s):  
Cyclic Adenosine Monophosphate ◽  
Adenosine Monophosphate ◽  
Purkinje Neurons ◽  
Immunocytochemical Study ◽  
Stimulation Of

Identification, Characterization, and Hormonal Regulation of 3′,5′-Cyclic Adenosine Monophosphate Dependent Protein Kinases in Rat Sertoli Cells*

Endocrinology ◽  
1991 ◽  
Vol 129 (5) ◽  
pp. 2345-2354 ◽  
Author(s):  
BRYNJAR F. LANDMARK ◽  
BEATHE FAUSKE ◽  
WINNIE ESKILD ◽  
BJØRN SKÅLHEGG ◽  
SUZANNE M. LOHMANN ◽  
...  
Keyword(s):  
Protein Kinases ◽  
Sertoli Cells ◽  
Hormonal Regulation ◽  
Cyclic Adenosine Monophosphate ◽  
Adenosine Monophosphate ◽  
Dependent Protein

Effect of P1-purinergic agonist on thyrotropin stimulation of H2O2 generation in FRTL-5 and porcine thyroid cells

1994 ◽  
Vol 130 (2) ◽  
pp. 180-186 ◽  
Author(s):  
Ulla Björkman ◽  
Ragnar Ekholm
Keyword(s):  
Adenylate Cyclase ◽  
Primary Culture ◽  
Purinergic Receptor ◽  
Cyclic Adenosine Monophosphate ◽  
Adenosine Monophosphate ◽  
Camp Accumulation ◽  
High Concentration ◽  
Thyroid Cells ◽  
H2o2 Generation ◽  
Stimulation Of

Björkman U, Ekholm R. Effect of P1-purinergic agonist on thyrotropin stimulation of H2O2 generation in FRTL-5 and porcine thyroid cells. Eur J Endocrinol 1994;130:180–6. ISSN 0804–4643 Our previous studies have shown that the generation of H2O2 in FRTL-5 thyroid cells is regulated via both the adenylate cyclase/cyclic adenosine monophosphate (cAMP) and Ca2+/phosphatidylinositol pathway: thyrotropin (TSH) stimulates H2O2 generation through both pathways, via the former at a low concentration and via the latter at a high concentration. In porcine thyrocytes in primary culture H2O2 generation is stimulated only via the Ca2+/phosphatidylinositol route. In the present study we explored the effect of a P1-purinergic agonist (phenylisopropyladenosine, PIA) on stimulations induced by TSH and by adenosine triphosphate (ATP), an activator of the Ca2+/phosphatidylinositol cascade via the P2-purinergic receptor. In FRTL- 5 cells, PIA potentiated H2O2 generation stimulated by TSH at 10U/l (but not at 1 U/l), Ca2+ mobilization induced by TSH and Ca2+ mobilization induced by ATP at 1 μmol/l (but not 10 μmol/l). Phenylisopropyladenosine strongly inhibited TSH-induced cAMP accumulation in FRTL-5 cells. In pig thyrocytes, PIA had no effect on H2O2 generation stimulated by TSH or ATP and no effect on ATP-stimulated Ca2+ mobilization. Also, PIA did not inhibit TSH-stimulated cAMP accumulation in pig thyrocytes, and by itselfhad no effecton H2O2 generation or Ca2 + mobilization. Thus, in FRTL-5 cells, but not in porcine thyrocytes, PIA modulates TSH-stimulated H2O2 generation by enhancing the Ca2+/phosphatitylinositol route and inhibiting the adenylate cyclase/cAMP route of the TSH signal. The net result of this modulation apparently depends on the balance between inhibition of the cAMP route and enhancement of the Ca2+ route. This may explain the lack of potentiation observed by 1 U/1 TSH. Ragnar Ekholm, Department of Anatomy, Medicinaregatan 3, S-413 90 Göteborg, Sweden

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