Adenylate cyclase activation by the .beta.-adrenergic receptors as a diffusion-controlled process

Biochemistry ◽  
1979 ◽  
Vol 18 (5) ◽  
pp. 846-853 ◽  
Author(s):  
Emanuel Hanski ◽  
Gilad Rimon ◽  
Alexander Levitzki
Keyword(s):  
Adenylate Cyclase ◽  
Adrenergic Receptors ◽  
Beta Adrenergic Receptors ◽  
Beta Adrenergic ◽  
Cyclase Activation ◽  
Diffusion Controlled ◽  
Adenylate Cyclase Activation

scholarly journals Non-co-ordinate development of β-adrenergic receptors and adenylate cyclase in chick heart

1982 ◽  
Vol 204 (3) ◽  
pp. 825-830 ◽  
Author(s):  
R W Alexander ◽  
J B Galper ◽  
E J Neer ◽  
T W Smith
Keyword(s):  
Embryonic Development ◽  
Adenylate Cyclase ◽  
Adrenergic Receptors ◽  
Cardiac Tissue ◽  
Beta Adrenergic Receptors ◽  
In Ovo ◽  
Beta Adrenergic ◽  
Receptor Affinity ◽  
Chick Heart ◽  
Β Adrenergic Receptors

We have studied the properties of beta-adrenergic receptors and of their interaction with adenylate cyclase in the chick myocardium during embryogenesis. Between 4.5 and 7.5 days in ovo the number of receptors determined by (-)-[3H]dihydroalprenolol ([3H]DHA) binding is constant at approx. 0.36 pmol of receptor/mg of protein. By day 9 the density decreases significantly to 0.22 pmol of receptor/mg of protein. At day 12.5-13.5 the number was 0.14-0.18 pmol of receptor/mg of protein. This number did not change further up to day 16. The same results were obtained with guanosine 5'-[beta, gamma-imido]triphosphate (p[NH]ppG) added to the assay mixtures. There was no significant change in receptor affinity for the antagonist [3H]DHA between days 5.5 and 13. Despite the decrease in numbers of beta-adrenergic receptors, there was no change in basal, p[NH]ppG-, isoprenaline- or isoprenaline-plus-p[NH]ppG-stimulated adenylate cyclase activity between days 3 and 12 of development. We conclude that beta-adrenergic receptors and adenylate cyclase are not co-ordinately regulated during early embryonic development of the chick heart. Some of the beta-adrenergic receptors present very early in the ontogeny of cardiac tissue appear not to be coupled to adenylate cyclase since their loss is not reflected in decreased activation of the enzyme.

scholarly journals Characteristics of the β-adrenergic adenylate cyclase system of developing rabbit bone-marrow erythroblasts

1983 ◽  
Vol 210 (2) ◽  
pp. 559-566 ◽  
Author(s):  
M S Setchenska ◽  
H R V Arnstein
Keyword(s):  
Bone Marrow ◽  
Adenylate Cyclase ◽  
Adrenergic Receptors ◽  
Dissociation Constants ◽  
Cyclase Activity ◽  
Adenylate Cyclase Activity ◽  
Beta Adrenergic Receptors ◽  
Beta Adrenergic ◽  
Dividing Cells ◽  
Rabbit Bone

After fractionation of rabbit bone marrow into dividing (early) and non-dividing (late) erythroid cells, the adenylate cyclase activity of membrane ghosts was assayed in the presence of guanine nucleotides ((GTP and its analogue p[NH]ppG (guanosine 5′-[beta, gamma-imido]triphosphate))), the beta-adrenergic agonist L-isoprenaline (L-isoproterenol) and the antagonist L-propranolol. Both GTP and p[NH]ppG increased the adenylate cyclase activity of early and late erythroblasts, whereas the stimulating effect of the beta-adrenergic drug L-isoprenaline was limited to the immature dividing bone-marrow cells. The effect of L-isoprenaline was completely inhibited by the antagonist L-propranolol, confirming that the response was due to stimulation of beta-adrenergic receptors on the plasma membrane. The lack of response of non-dividing erythroblasts to beta-adrenergic stimuli is not due to loss of beta-receptors, since both dividing and non-dividing cells bind the selective ligand [125I]iodohydroxybenzylpindolol with almost equal affinities, the apparent dissociation constants, Kd, being 0.91 × 10(-8)M and 1.0 × 10(-8) M respectively. The number of beta-adrenergic receptors per cell was 2-fold higher in the dividing cells. No significant change in binding affinity for GTP and p[NH]ppG during erythroblast development was observed: the dissociation constants of both guanine nucleotides were almost identical with early and late erythroblast membrane preparations [2-3 (X 10(-7) M]. With dividing cells, however, in the presence of L-isoprenaline the dissociation constants of GTP and p[NH]ppG were lower (6 × 10(-8) M). The dose-response curves for isoprenaline competition in binding of [125I]iodohydroxybenzylpindolol by dividing cells showed that the EC50 (effective concentration for half maximum activity) value for isoprenaline was higher in the presence of p[NH]ppG. With non-dividing cells the EC50 value for isoprenaline was equal in the presence and in the absence of p[NH]ppG and similar to that observed with dividing-cell membranes in the presence of the nucleotide. Thus differentiation of rabbit bone-marrow erythroid cells seems to be accompanied by uncoupling of the beta-adrenergic receptors from the adenylate cyclase catalytic protein as well as by a decrease in the number of receptors per cell, but not by changes in the catecholamine and guanine-nucleotide-binding affinities.

beta-Adrenergic receptors in the developing rabbit lung

1981 ◽  
Vol 240 (4) ◽  
pp. E351-E357 ◽  
Author(s):  
J. A. Whitsett ◽  
M. A. Manton ◽  
C. Darovec-Beckerman ◽  
K. G. Adams ◽  
J. J. Moore
Keyword(s):  
Adenylate Cyclase ◽  
Adrenergic Receptors ◽  
Adrenergic Receptor ◽  
Cyclase Activity ◽  
Adenylate Cyclase Activity ◽  
Receptor Subtypes ◽  
Beta Adrenergic Receptors ◽  
Rabbit Lung ◽  
Beta Adrenergic ◽  
Beta 2

beta-Adrenergic receptors and catecholamine-sensitive adenylate cyclase were identified and partially characterized in membrane fractions of rabbit lungs from day 25 of gestation to adulthood with the beta-adrenergic antagonists (--)-[3H]dihydroalprenolol [(--)-[3H]DHA] and (--)-[125I]iodohydroxybenzylpindolol [(--)-[125I]HYP]. beta-Adrenergic receptor number (Bmax) increased 11.5-fold during this time period, increasing progressively during the latter days of gestation and the early neonatal period, from 37 +/- 10 fmol/mg protein at 25 days gestation to 425 +/- 51 fmol/mg in the adult rabbit lung (mean +/- SD). Receptor affinity for (--)-[3H]DHA (KD = 1.8 nM) or (--)-[125I]HYP (KD - 0.104 nM) and the proportion of beta 1- and beta 2-adrenergic receptor subtypes (60% beta 1 and 40% beta 2) did not change with advancing age. Basal adenylate cyclase activity in lung homogenates decreased significantly with increasing age, whereas the activity in the presence of catecholamine or NaF remained nearly constant. Catecholamines stimulated adenylate cyclase activity at all ages studied supporting a role of the maturation of beta-adrenergic receptors in the regulation of pulmonary function.

scholarly journals Cyclical antiidiotypic response to anti-hormone antibodies due to neutralization by autologous anti-antiidiotype antibodies that bind hormone.

1983 ◽  
Vol 157 (5) ◽  
pp. 1369-1378 ◽  
Author(s):  
P O Couraud ◽  
B Z Lü ◽  
A D Strosberg
Keyword(s):  
Adenylate Cyclase ◽  
Ligand Binding ◽  
Adrenergic Receptors ◽  
Hormone Receptors ◽  
Binding Activity ◽  
Functional Network ◽  
Beta Adrenergic Receptors ◽  
Beta Adrenergic ◽  
Ligand Binding Activity

Antiidiotype antibodies were raised against anti-catecholamine ligand antibodies. The antiidiotype response was shown to be cyclical and to correspond to the production of antibodies that could bind to catecholamine beta-adrenergic receptors and stimulate adenylate cyclase. Disappearance of these antibodies from the serum could be correlated with the appearance of a catecholamine ligand-binding activity corresponding to the synthesis of autologous anti-antiidiotype antibodies directed against the induced antiidiotypic molecules. Comparison of the injected versus the induced anti-ligand antibodies reveals striking differences in affinities but similarities in the ability to bind to the antiidiotype antibodies and to the ligand-containing affinity gel. The results support the existence of a functional network of idiotype antiidiotype interactions involving external as well as internal antigens, antibodies, and possibly other types of molecules involved in recognition phenomena, such as hormone receptors.

Sign in / Sign up

Export Citation Format

Share Document