In vitro and in vivo effects of a luteolytic prostaglandin (Estrumate, I.C.I. 80996) on rat ovarian adenylate cyclase activity

1981 ◽  
Vol 9 (1) ◽  
pp. 94-95 ◽  
Author(s):  
ALAN E. WAKELING ◽  
LESLIE R. GREEN
Keyword(s):  
Adenylate Cyclase ◽  
Cyclase Activity ◽  
Adenylate Cyclase Activity ◽  
In Vivo Effects

Protease effects on adenylate cyclase in potassium-depleted rabbit kidney

1988 ◽  
Vol 255 (5) ◽  
pp. F1033-F1039
Author(s):  
K. H. Raymond ◽  
S. D. Holland ◽  
T. K. Hymer ◽  
T. D. McKinney ◽  
M. S. Katz
Keyword(s):  
Adenylate Cyclase ◽  
Proteolytic Enzymes ◽  
Cyclase Activity ◽  
Adenylate Cyclase Activity ◽  
Rabbit Kidney ◽  
Potassium Depletion ◽  
Collecting Tubules ◽  
And Control

Potassium depletion in rabbits induces a renal concentrating defect in vivo and decreased hydrosmotic response to arginine vasopressin (AVP) in isolated cortical collecting tubules (CCT) perfused in vitro. The molecular basis of the AVP resistance in potassium depletion was investigated by comparing AVP-responsive adenylate cyclase activities in CCT from potassium-depleted and control rabbits. Vasopressin-responsive enzyme activity was impaired in CCT dissected from kidneys of potassium-depleted rabbits but not when kidneys were treated with collagenase to improve microdissection conditions. Potassium depletion also depressed parathyroid hormone (PTH)-stimulated adenylate cyclase activity in proximal straight tubules (PST) dissected from untreated but not collagenase-treated kidneys. Commercially available collagenase, which also contains other proteolytic enzymes, increased AVP-sensitive adenylate cyclase activity in control CCT, and trypsin treatment of CCT dissected without collagenase abolished the decrease in AVP-sensitive activity induced by potassium depletion. Inclusion of trypsin inhibitor during collagenase treatment of kidneys lowered AVP response in CCT from potassium-depleted rabbits. These results demonstrate that potassium depletion impairs hormone-sensitive adenylate cyclase of CCT (and PST) by a protease-sensitive mechanism.

EFFECT OF HUMAN CHORIONIC GONADOTROPHIN ON ADENYLATE CYCLASE ACTIVITY AND TESTOSTERONE CONTENT IN RAT TESTICULAR MITOCHONDRIA

1977 ◽  
Vol 75 (1) ◽  
pp. 119-126 ◽  
Author(s):  
SOREL SULIMOVICI ◽  
M. S. ROGINSKY
Keyword(s):  
Cyclic Amp ◽  
Adenylate Cyclase ◽  
Chorionic Gonadotrophin ◽  
Human Chorionic Gonadotrophin ◽  
Cyclase Activity ◽  
Adenylate Cyclase Activity ◽  
Dibutyryl Cyclic Amp ◽  
Trophic Hormone

The adenylate cyclase activity and the concentration of testosterone in testicular mitochondria from immature rats were measured after administration of human chorionic gonadotrophin (HCG) or dibutyryl cyclic AMP in vivo or in vitro. Intratesticular injection of HCG produced an increase in adenylate cyclase activity which preceded the rise in the level of testosterone, whereas addition of the trophic hormone in vitro resulted in simultaneous increases. Administration of dibutyryl cyclic AMP in vivo enhanced the testosterone content of the mitochondria. However, the cyclic nucleotide added in vitro at concentrations up to 5 mmol/l had no effect. Cycloheximide injected intraperitoneally before the administration of HCG abolished the stimulatory effect of the trophic hormone on the level of testosterone in the mitochondria, whereas chloramphenicol had no effect. These results, although they confirm the role of cyclic AMP as an intermediate in the stimulatory effect of HCG on the concentration of testosterone in rat testis, do not support a role for mitochondrial adenylate cyclase in this action. A protein regulator(s) formed extramitochondrially appears to be involved in the stimulatory effect of gonadotrophins on steroidogenesis.

Decrease in adenylate cyclase activity in dog livers during endotoxic shock

1983 ◽  
Vol 245 (5) ◽  
pp. R737-R742
Author(s):  
S. Ghosh ◽  
M. S. Liu
Keyword(s):  
Adenylate Cyclase ◽  
Plasma Membranes ◽  
Cyclase Activity ◽  
Adenylate Cyclase Activity ◽  
Guanine Nucleotide ◽  
Endotoxin Administration ◽  
Liver Plasma Membranes ◽  
Dog Liver

The effects of endotoxin administration on adenylate cyclase in dog liver plasma membranes were studied. The basal, fluoride-, guanine nucleotide-, isoproterenol-, and glucagon-stimulated adenylate cyclase activities were decreased by 61, 62, 69, 83, and 63%, respectively, 2 h after in vivo administration of endotoxin. Endotoxin (100 micrograms/ml) in vitro decreased the guanine nucleotide-, isoproterenol-, and glucagon-stimulated adenylate cyclase activities by 24, 25, and 21%, respectively. These data demonstrate that endotoxin administered in vivo or in vitro had an inhibitory effect on the adenylate cyclase enzyme system in dog liver plasma membranes. Because of the involvement of the adenylate cyclase-adenosine 3',5'-cyclic monophosphate (cAMP) system in the regulation of hepatic carbohydrate metabolism, the finding that endotoxin administration decreased adenylate cyclase activity in the liver should contribute to the understanding of the pathophysiology of altered hepatic glucose homeostasis during shock.

Cytochemical Evidence for Presynatic β-Adrenergic Regulation of Secretion in the Developing Rat Submandibular Gland

1977 ◽  
Vol 35 ◽  
pp. 430-431
Author(s):  
L.S. Cutler
Keyword(s):  
Cyclic Amp ◽  
Adenylate Cyclase ◽  
Submandibular Gland ◽  
Neonatal Rat ◽  
Cyclase Activity ◽  
Adenylate Cyclase Activity ◽  
Parotid Glands ◽  
Adrenergic Agonist ◽  
Rat Submandibular Gland

Many studies previously have shown that the B-adrenergic agonist isoproterenol and the a-adrenergic agonist norepinephrine will stimulate secretion by the adult rat submandibular (SMG) and parotid glands. Recent data from several laboratories indicates that adrenergic agonists bind to specific receptors on the secretory cell surface and stimulate membrane associated adenylate cyclase activity which generates cyclic AMP. The production of cyclic AMP apparently initiates a cascade of events which culminates in exocytosis. During recent studies in our laboratory it was observed that the adenylate cyclase activity in plasma membrane fractions derived from the prenatal and early neonatal rat submandibular gland was retractile to stimulation by isoproterenol but was stimulated by norepinephrine. In addition, in vitro secretion studies indicated that these prenatal and neonatal glands would not secrete peroxidase in response to isoproterenol but would secrete in response to norepinephrine. In contrast to these in vitro observations, it has been shown that the injection of isoproterenol into the living newborn rat results in secretion of peroxidase by the SMG (1).

scholarly journals Lysophosphatidylcholines can modulate the activity of the glucagon-stimulated adenylate cyclase from rat liver plasma membranes

1979 ◽  
Vol 178 (1) ◽  
pp. 217-221 ◽  
Author(s):  
M D Houslay ◽  
R W Palmer
Keyword(s):  
Adenylate Cyclase ◽  
Rat Liver ◽  
Plasma Membranes ◽  
Hormone Receptors ◽  
Cyclase Activity ◽  
Adenylate Cyclase Activity ◽  
Liver Plasma Membranes ◽  
Rat Liver Plasma Membranes ◽  
Increased Sensitivity

1. Synthetic lysophosphatidylcholines inhibit the glucagon-stimulated adenylate cyclase activity of rat liver plasma membranes at concentrations two to five times lower than those needed to inhibit the fluoride-stimulated activity. 2. Specific 125I-labelled glucagon binding to hormone receptors is inhibited at concentrations similar to those inhibiting the fluoride-stimulated activity. 3. At concentrations of lysophosphatidylcholines immediately below those causing inhibition, an activation of adenylate cyclase activity or hormone binding was observed. 4 These effects are essentially reversible. 5. We conclude that the increased sensitivity of glucagon-stimulated adenylate cyclase to inhibition may be due to the lysophosphatidylcholines interfering with the physical coupling between the hormone receptor and catalytic unit of adenylate cyclase. 6. We suggest that, in vivo, it is possible that lysophosphatidylcholines may modulate the activity of adenylate cyclase only when it is in the hormone-stimulated state.

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