scholarly journals Effects of noradrenaline on the activation and the stability of brain adenylate cyclase

1977 ◽  
Vol 166 (3) ◽  
pp. 473-483 ◽  
Author(s):  
S Brydon-Golz ◽  
H Ohanian ◽  
A Bennun
Keyword(s):  
Adenylate Cyclase ◽  
Rat Brain ◽  
Half Life ◽  
Brain Cortex ◽  
Corpus Striatum ◽  
Cyclase Activity ◽  
Adenylate Cyclase Activity ◽  
Strong Inhibition ◽  
The Stability ◽  
Stimulation Of

At constant 1 mM-ATP, the Mg2+-saturation curves for adenylate cyclase (EC 4.6.1.1) particulate preparations obtained from corpus striatum and cortex tissues of rat brain show that addition of 0.1 mM-noradrenaline increases the apparent Vmax. for Mg2+ by 300% in corpus striatum particles, and by 280% in cortex particles. At 10 mM-MgCl2, the addition of 0.1 mM-noradrenaline increased by 800% the adenylate cyclase activity of corpus striatum particles. At all Mg2+ concentrations, the addition of 0.3 mM-CaCl2 suppressed the noradrenaline-induced stimulation of adenylate cyclase of corpus striatum particles, and even resulted in a strong inhibition of the activating effect of Mg2+ itself on adenylate cyclase of corpus striatum particles, and even resulted in a strong inhibition of the activating effect of Mg2+ itself on adenylate cyclase activity of cortex particles. The addition of noradrenaline during a 3 h preincubation of particle preparations of brain cortex at 38 degrees C decreased by more than 4-fold the half-life of the decay of adenylate cyclase activity. The addition of MgATP protected against noradrenaline-induced inactivation.

Corticotropin releasing factor receptor-mediated stimulation of adenylate cyclase activity in the rat brain

1986 ◽  
Vol 381 (1) ◽  
pp. 49-57 ◽  
Author(s):  
F. Mia Chen ◽  
Louise M. Bilezikjian ◽  
Marilyn H. Perrin ◽  
Jean Rivier ◽  
Wylie Vale
Keyword(s):  
Adenylate Cyclase ◽  
Rat Brain ◽  
Corticotropin Releasing Factor ◽  
Cyclase Activity ◽  
Adenylate Cyclase Activity ◽  
Stimulation Of

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.

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