Comparison of the effects of prostaglandin I2 and prostaglandin E2 stimulation of the rat kidney adenylate cyclase-cyclic AMP systems

1979 ◽  
Vol 582 (3) ◽  
pp. 496-503 ◽  
Author(s):  
C Herman
Keyword(s):  
Cyclic Amp ◽  
Adenylate Cyclase ◽  
Prostaglandin E2 ◽  
Rat Kidney ◽  
Prostaglandin I2 ◽  
Stimulation Of

Evidence for Two Separate Receptors Mediating The Stimulation of Platelet Adenylate Cyclase By Prostaglandin I2 (PGI2), PGD2 and PGE1

1979 ◽  
Author(s):  
D. C. B. Mils ◽  
D. E. Macfarlane
Keyword(s):  
Cyclic Amp ◽  
Adenylate Cyclase ◽  
Partial Agonist ◽  
Human Platelets ◽  
Intrinsic Activity ◽  
High Dose ◽  
Prostaglandin I2 ◽  
Subsequent Response ◽  
High Concentrations ◽  
Stimulation Of

Prostacyclin (PGI2), and prostaglandins D2 and E1, all inhibit aggregation of human platelets by stimulating adenylate cyclase. in platelets prelabelled with l4C adenine, PGI2 has a higher intrinsic activity than either PGD2 or PGE1, as well as a higher apparent affinity. PGE1 but not PGD2, inhibits the action of high concentrations of PGI2, both when added simultaneously with PGI2 and when added 3 min later. in the latter case the slow spontaneous fall in intracellular cyclic AMP is accelerated by PGE. but not by PGD2. PGF1α, at concentrations up to 100 μM neither stimulated the cyclase 1 by itself, nor did it inhibit the effects of PGI2, PGE1, or PGD2. PGF2α, which did cause a small increase in cyclic AMP, inhibited PGD2 strongly, PGE1 not at all, and PGI2 slightly at high concentrations. N0164, an inhibitor of aggregation induced by bis-enoic prostaglandins, inhibited cyclase stimulation by PGD2 but not by PGE1, PGE2, PGD1 or PGI2, though it reduced PGI2-induced inhibition of platelet aggregation. Preaddition of PGE1, but not of PGI2 or PGD2, at submaximal concentrations, inhibited subsequent response to high dose PGI2. The results suggest that PGE1 and PGD2 probably act on the same enzyme, but through a different receptor. PGE1 acts as a partial agonist for the receptor for PGI2, but in addition causes a tachyphylaxis not seen with PGI2 or with PGD2.

Evidence for two Separate Receptors Mediating the Stimulation of Platelet Adenylate Cyclase by Prostaglandin I2 (PCI2), PGD2 and PCE1

1979 ◽  
Author(s):  
D.C.B. Mills ◽  
D.E. Macfarlane
Keyword(s):  
Cyclic Amp ◽  
Adenylate Cyclase ◽  
Partial Agonist ◽  
Human Platelets ◽  
Intrinsic Activity ◽  
High Dose ◽  
Prostaglandin I2 ◽  
Subsequent Response ◽  
High Concentrations ◽  
Stimulation Of

Prostacyclin (PGI2), and prostaglandins D2 and E1, all inhibit aggregation of human platelets by stimulating adenylate cyclase. In platelets prelabelled with 14C adenine, PGI2 has a higher intrinsic activity than either PGD2 or PGE1α, as well as a higher apparent affinity. PGE1, but not PGD2, inhibits the action of high concentrations of PGI2, both when added simultaneously with PGI2 and when added 3 min later. In the latter case the slow spontaneous fall in intracellular cyclic AMP Is accelerated by PGEj but not by PCD2. PGF2, at concentrations up to 100 μM neither stimulated the cyclase by itself, nor did it Inhibit the effects of PGI2, PCE, or PCD2. PCF2α which did cause a small increase in cyclic AMP, inhibited PGD2 strongly, PGE1 not at all, and PCI2 slightly at high concentrations. N0164, an inhibitor of aggregation induced by bls-enoic prostaglandins, inhibited cyclase stimulation by PGD2 but not by PGE1, PGE2, PGD1, or PGI2, though it reduced PGI2-induced inhibition of platelet aggregation. Preaddition of PGE1, but not of PG2, or PGD2, at submaximal concentrations, inhibited subsequent response to high dose PGI2. The results suggest chat PGE1 and PCD2 probably act on the same enzyme, but through a different receptor. PGE1 acts as a partial agonist for the receptor for PCI2, but In addition causes a tachyphylaxis not seen with PCI2, or with, PGD2.

Interaction between parathyroid hormone and prostaglandin E1 on cyclic AMP metabolism in rat kidney

1980 ◽  
Vol 93 (3) ◽  
pp. 339-345 ◽  
Author(s):  
Naokazu Nagata ◽  
Yuriko Ono ◽  
Narimichi Kimura
Keyword(s):  
Parathyroid Hormone ◽  
Cyclic Amp ◽  
Adenylate Cyclase ◽  
Rat Kidney ◽  
Prostaglandin E ◽  
Cortical Tissue ◽  
Newborn Rat ◽  
Simultaneous Addition ◽  
Renal Cortical Tissue ◽  
Subsequent Addition

Abstract. The interaction between parathyroid hormone (PTH) and prostaglandin E1 (PGE1) in influencing cyclic AMP metabolism in rat renal cortical tissue was examined. PTH and PGE1 stimulated additively the adenylate cyclase activity in the homogenate of the tissue. Both PTH and PGE1 enhanced the level of cyclic AMP in the incubated renal cortical tissue, but the effect of their simultaneous addition did not exceed the effect induced by PTH alone. Cyclic AMP accumulated in the incubation medium by stimulation by PTH was decreased by the simultaneous addition of PGE1. When the tissue was pre-incubated for 30 min with 2 to 10 μg/ml of PGE1, the magnitude of the increase of cyclic AMP caused by PTH subsequently added was lessened. However, the response to PTH of adenylate cyclase preparation obtained from the homogenate of PGE1-pre-treated tissue was not decreased. When first PTH was added to the incubating renal cortical tissue, the subsequent addition of PGE1 accelerated the decrease of cyclic AMP content in the tissue and decreased the amount of cyclic AMP released from the tissue. The interaction of PTH and PGE1 on cyclic AMP metabolism in the renal cortical tissue was in contrast to that seen in newborn rat calvaria where PGE1 and PTH acted additively in enhancing the level of cyclic AMP.

scholarly journals Interactions between adenylate cyclase and the yeast GTPase-activating protein IRA1.

1991 ◽  
Vol 11 (9) ◽  
pp. 4591-4598 ◽  
Author(s):  
M R Mitts ◽  
J Bradshaw-Rouse ◽  
W Heideman
Keyword(s):  
Cyclic Amp ◽  
Adenylate Cyclase ◽  
Adenylate Cyclase System ◽  
Gtpase Activating Protein ◽  
Yeast Saccharomyces Cerevisiae ◽  
Strong Candidate ◽  
Sepharose 4B ◽  
Stimulation Of ◽  
Cyclic Amp Synthesis

The adenylate cyclase system of the yeast Saccharomyces cerevisiae contains many proteins, including the CYR1 polypeptide, which is responsible for catalyzing the formation of cyclic AMP from ATP, RAS1 and RAS2 polypeptides, which mediate stimulation of cyclic AMP synthesis by guanine nucleotides, and the yeast GTPase-activating protein analog IRA1. We have previously reported that adenylate cyclase is only peripherally bound to the yeast membrane. We have concluded that IRA1 is a strong candidate for a protein involved in anchoring adenylate cyclase to the membrane. We base this conclusion on the following criteria: (i) a disruption of the IRA1 gene produced a mutant with very low membrane-associated levels of adenylate cyclase activity, (ii) membranes made from these mutants were incapable of binding adenylate cyclase in vitro, (iii) IRA1 antibodies inhibit binding of adenylate cyclase to the membrane, and (iv) IRA1 and adenylate cyclase comigrate on Sepharose 4B.

scholarly journals Stimulation of Cyclic AMP Formation by Pituitary Adenylate Cyclase-Activating Polypeptide Is Attenuated by Glutamate in Rat Brain Slices

1995 ◽  
Vol 67 (4) ◽  
pp. 399-402
Author(s):  
Kaoru Kondo ◽  
Hitoshi Hashimoto ◽  
Kazuko Sakata ◽  
Hiroshi Saga ◽  
Jun-ichi Kitanaka ◽  
...  
Keyword(s):  
Cyclic Amp ◽  
Adenylate Cyclase ◽  
Rat Brain ◽  
Brain Slices ◽  
Pituitary Adenylate Cyclase ◽  
Stimulation Of

scholarly journals Stimulation of Adenylate Cyclase by Ca2+ and Calmodulin in Rat Islets of Langerhans: Explanation for the Glucose-induced Increase in Cyclic AMP Levels

Diabetes ◽  
1980 ◽  
Vol 29 (1) ◽  
pp. 74-77 ◽  
Author(s):  
G. W. G. Sharp ◽  
D. E. Wiedenkeller ◽  
D. Kaelin ◽  
E. G. Siegel ◽  
C. B. Wollheim
Keyword(s):  
Cyclic Amp ◽  
Adenylate Cyclase ◽  
Islets Of Langerhans ◽  
Rat Islets ◽  
Rat Islets Of Langerhans ◽  
Stimulation Of

Prostaglandin E2-binding sites and cAMP production in porcine fundic mucosa

1981 ◽  
Vol 241 (4) ◽  
pp. G313-G320
Author(s):  
B. L. Tepperman ◽  
B. D. Soper
Keyword(s):  
Adenylate Cyclase ◽  
Prostaglandin E2 ◽  
Binding Site ◽  
Binding Sites ◽  
Biologically Active ◽  
Cyclase Activity ◽  
Adenylate Cyclase Activity ◽  
Scatchard Analysis ◽  
Fundic Mucosa ◽  
Stimulation Of

Biologically active [3H]prostaglandin E2 (PGE2) bound rapidly and specifically to membrane fractions from hog fundic mucosa. Optimal binding occurred in the 30,000-g membrane preparation at 37 degrees C (pH 5.0). Scatchard analysis of specific PgE2 binding revealed the presence of a heterogeneous population of binding sites with Kd values and binding site concentrations of approximately 1 X 10(-9) M and 1 fmol/mg prot and 2 X 10(-8) M and 20 fmol/mg prot, respectively. Specific binding was inhibited by the following agents in descending order of potency: PGE1, PGA2, PGD2, 6-keto-PGF1 alpha, and thromboxane B2. Trypsin treatment or boiling reduced or abolished specific PGE2 binding. PGE2 stimulated cAMP formation in the 2,500-g fraction, with an approximate Km of 1 X 10(-6) M, but stimulation of adenylate cyclase activity by PG was not evident in the 16,000-g or 30,000-g tissue preparations. These results suggest that a specific PGE2-binding site exists in the 16,000-g and 30,000-g fractions of porcine fundic mucosa, although an increase in cAMP-forming capacity could not b of 1 X 10(-6) M, but stimulation of adenylate cyclase activity by PG was not evident in the 16,000-g or 30,000-g tissue preparations. These results suggest that a specific PGE2-binding site exists in the 16,000-g and 30,000-g fractions of porcine fundic mucosa, although an increase in cAMP-forming capacity could not b of 1 X 10(-6) M, but stimulation of adenylate cyclase activity by PG was not evident in the 16,000-g or 30,000-g tissue preparations. These results suggest that a specific PGE2-binding site exists in the 16,000-g and 30,000-g fractions of porcine fundic mucosa, although an increase in cAMP-forming capacity could not be localized in these fractions in vitro.

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