Irreversible stimulation of adenylate cyclase activity of fat cell membranes by phosphoramidate and phosphonate analogs of GTP

1975 ◽  
Vol 23 (1) ◽  
pp. 249-278 ◽  
Author(s):  
Pedro Cuatrecasas ◽  
Vann Bennett ◽  
Steven Jacobs
Keyword(s):  
Adenylate Cyclase ◽  
Cell Membranes ◽  
Cyclase Activity ◽  
Adenylate Cyclase Activity ◽  
Fat Cell ◽  
Stimulation Of

Modulation of Adenylate Cyclase Activity in Liver and Fat Cell Membranes by Insulin

Science ◽  
1972 ◽  
Vol 175 (4024) ◽  
pp. 906-908 ◽  
Author(s):  
G. Illiano ◽  
P. Cuatrecasas
Keyword(s):  
Adenylate Cyclase ◽  
Cell Membranes ◽  
Cyclase Activity ◽  
Adenylate Cyclase Activity ◽  
Fat Cell

Stimulation of Thyroid Adenylate Cyclase Activity in Sera of Patients with Nonthyroidal Illness

1986 ◽  
pp. 385-389
Author(s):  
F. Kakezono ◽  
S. Yamashita ◽  
N. Yokoyama ◽  
S. Morita ◽  
S. Okamoto ◽  
...  
Keyword(s):  
Adenylate Cyclase ◽  
Cyclase Activity ◽  
Adenylate Cyclase Activity ◽  
Nonthyroidal Illness ◽  
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.

Variable Stimulation of Adenylate Cyclase Activity by Vasoactive Intestinal-Like Peptides and β-Adrenergic Agonists in Murine T Cell Lymphomas of Immature, Helper, and Cytotoxic Types

Immunobiology ◽  
1989 ◽  
Vol 179 (4-5) ◽  
pp. 422-431 ◽  
Author(s):  
Patrick Robberecht ◽  
Jacques Abello ◽  
Catherine Damien ◽  
Philippe De Neef ◽  
Eric Vervisch ◽  
...  
Keyword(s):  
T Cell ◽  
Adenylate Cyclase ◽  
Cyclase Activity ◽  
Adenylate Cyclase Activity ◽  
Adrenergic Agonists ◽  
T Cell Lymphomas ◽  
Stimulation Of
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