Hormone Action on Liver Adenyl Cyclase Activity

Hepp, K.; Edel, R. K.; Wieland, O.

doi:10.1111/j.1432-1033.1970.tb01150.x

Cited by 52 publications

(21 citation statements)

References 25 publications

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“…1.). Enzyme activity was dependent on Mg2+ in a manner characteristic of adenylate cyclase from other tissues [7,8], demonstrating optimal activity when the Mg2+ concentration was 5 times that of ATP.…”

Section: Resultsmentioning

confidence: 99%

Calcium ion: A modulator of parotid adenylate cyclase activity

1974

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Section: Resultsmentioning

confidence: 99%

Calcium ion: A modulator of parotid adenylate cyclase activity

1974

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“…One unit of activity for insulin-like material is that which has an effect equivalent to one unit of insulin. The sources of all other enzymes and chemicals have been described [15].…”

Section: Hormones and Chemicalsmentioning

confidence: 99%

“…Phosphodiesterase Activity The procedures for the adenylate cyclase assay have been described [15]. The standard assay system contained: 20 mM Tris-HC1, pH 7.4; 4.5 mM MgC1,; 5 mM 3':5'-AMP; 0.45 mM [ N -~~P ] A T P (2-5 pCi), 6 mM potassium phosphoenoZpyruvate and 5 pg pyruvic kinase, or 10mM creatine phosphate and 300 pg/ml creatine kinase as ATP-regenerating system.…”

Section: Assay Of Adenylate-cyclase Andmentioning

confidence: 99%

“…Concentration of protein was 50-100pg per fraction in the adenylate cyclase test, and 50-200 pg in the phosphodiesterase reaction. For preincubation experiments, the standard procedure [15] for preparation of the particulate fraction was followed to the first sedimentation step a t 40000 x g for 20 min. The pellet was resuspended in 4 vols 20 mM Tris-HC1, p H 7.4, by hand in a teflon/glass homogenizer.…”

Section: Preparation Of Liversmentioning

confidence: 99%

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Adenylate Cyclase and Insulin Action

Hepp

1972

European Journal of Biochemistry

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Activation of adenylate cyclase in a particle preparation from mouse liver was studied after previous exposure to synthetic glucagon and NaF, and following extensive washing of the preparation. Activation by glucagon was maintained, but fully abolished when GTP was preincubated with the hormone. ATP reduced the effect of glucagon and NaF. The effect of submaximal concentrations of glucagon was significantly inhibited in the presence of physiological amounts of insulin (50–100 μU/ml). Increasing the concentration of insulin led to a disappearance of this effect. Whereas reduction of the basal adenylate cyclase activity was observed, no effect was obtained under maximal stimulation by NaF. Nonsuppressible insulin‐like material, a polypeptide with a molecular weight of approx. 7000, which mimics insulin in a number of metabolic effects, was also found to inhibit the basal as well as the glucagon‐stimulated adenylate cyclase. In contrast to insulin, no paradoxical decrease was seen with higher concentrations. The effects of high concentrations of NaF were not inhibited by insulin‐like material. After previous incubation with insulin‐like material its effect was maintained in the subsequent assay suggesting that the substance binds to liver membranes. In mouse myocardium, insulin‐like material caused no reduction in norepinephrine‐stimulated adenylate cyclase activity. Cyclic‐AMP phosphodiesterase activity, as measured with 1.13 μM substrate, was not influenced by insulin or insulin‐like material. It is unlikely that increased breakdown of cyclic AMP during the adenylate cyclase reaction is responsible for the observed effect of insulin or insulin‐like material. Diabetes, induced by streptozotocin, led to a marked increase in the sensitivity of the adenylate cyclase system to maximal glucagon stimulation. In contrast, the sensitivity of the system to NaF remained unchanged. Insulin treatment of diabetic animals in vivo led to a reversal of the glucagon effect towards the values in the control group. It is suggested that both insulin and insulin‐like material directly affect the adenylate cyclase system by interference with the transmission of the glucagon signal between the receptor and the catalytic enzyme unit. This effect may be of fundamental physiological significance in the mechanism of action of insulin.

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“…Hepp et al (4). The amounts of glucagon, norepinephrine and BPHPP in the 0.1 ml reaction mixture were 10 µg, 50 nmoles and 0.2 pmoles, respectively.…”

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confidence: 99%

Effect of 2-(4-Benzyl-Piperidino)-1-(4-Hydroxyphenyl)-1-Propanol on Adenylate Cyclase and 3′,5′-Cyclic Amp Phosphodiesterase in Vitro

Yamashita

Kawai

Hotta

1976

Japanese Journal of Pharmacology

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It is well established that some vasodilator drugs like the nicotinic acid derivative exert marked effects through relaxation of vascular smooth muscle. Carron et al. (1) reported the synthesis and pharmacological characteristics of 2-piperidinoalkanol derivatives, and found 2-(4-benzyl-piperidino)-1-(4-hydroxyphenyl)-1-propanol-L(=)-tartrate (BPHPP) to be a most potent vasodilator. The mechanisms of the pharmacological actions, however, remain unknown. 2-Piperidinoalkanol derivatives also display some prevailing a-adrenergic blocking effects; BPHPP has been found to be antagonistic to the epinephrine-induced contractions of the seminal vesicles (1). Since adenylate cyclase is stimulated by epinephrine, glucagon and other hormones (2), and since the biological effects of these hormones are due to the elevation of intracellular cyclic adenosine 3',5'-monophosphate (cyclic AMP) levels in the target organs (3), studies concerning the participation of BPHPP in the hormone-stimulating adenylate cyclase system are deemed worthy of interest.During the course of the inv(,stigation of BPHPP on cyclic AMP metabolism, we observed that this agent inhibits both activities of adenylate cyclase and cyclic AMP phos phodiesterase in vitro.Male rats of the Wistar strain, weighing from 180 to 200 g, were maintained on an

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Hormone Action on Liver Adenyl Cyclase Activity

Cited by 52 publications

References 25 publications

Calcium ion: A modulator of parotid adenylate cyclase activity

Calcium ion: A modulator of parotid adenylate cyclase activity

Adenylate Cyclase and Insulin Action

Effect of 2-(4-Benzyl-Piperidino)-1-(4-Hydroxyphenyl)-1-Propanol on Adenylate Cyclase and 3′,5′-Cyclic Amp Phosphodiesterase in Vitro

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