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Journal ArticleDOI

The activation of liver glycogen phosphorylase by vasopressin

Stefaan Keppens, +1 more
- 01 Mar 1975 - 
- Vol. 51, Iss: 1, pp 29-32
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TLDR
The glycogenolytic effect of vasopressin is due to the activation of glycogen phosphorylase, the rate limiting enzyme in glycogen degradation, which is apparently not mediated by cyclic AMP.
About
This article is published in FEBS Letters.The article was published on 1975-03-01. It has received 79 citations till now. The article focuses on the topics: Glycogen phosphorylase & Glycogen synthase.

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Citations
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Journal ArticleDOI

Ectopic and abnormal hormone receptors in adrenal Cushing's syndrome.

TL;DR: The mechanism by which cortisol is produced in adrenal Cushing's syndrome, when ACTH is suppressed, was previously unknown and was referred to as being “autonomous.” More recently several investigators have shown that some steroid-producing adrenal tumors or hyperplasias are under the control of ectopic (or aberrant, illicit, inappropriate) membrane hormone receptors.
Journal ArticleDOI

On the role of calcium as second messenger in liver for the hormonally induced activation of glycogen phosphorylase

TL;DR: The data are interpreted in favour of a role of calcium as the second messenger in liver for the three cyclic AMP-independent glycogenolytic hormones and as an additional messenger for glucagon which, via cyclicAMP, will make calcium available to the cytoplasm either from extracellular or from intracellular pools.
Book ChapterDOI

Phospholipid turnover in hormone action.

TL;DR: The signal-induced turnover of inositol phospholipids is a sign of the transmembrane control of cellular functions and proliferation through the activation of protein kinase C and the precise targets of protein Kinase C as well as those of Ca2+ in many tissues will be clarified by further investigations.
References
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Journal ArticleDOI

Purification and properties of rabbit skeletal muscle adenosine 3',5'-monophosphate-dependent protein kinases.

TL;DR: A modified procedure for purification of the adenosine 3',5'-monophosphate-dependent (cyclic AMP-dependent) protein kinase from rabbit skeletal muscle is described, which results in the separation of the enzyme into two peaks of activity on diethylaminoethylcellulose.
Journal ArticleDOI

Studies on the role of adenosine 3',5'-monophosphate in the hepatic actions of glucagon and catecholamines.

TL;DR: The hypothesis is discussed in terms of the hypothesis that glucagon and catecholamines act in the liver by increasing the concentration of free, metabolically active cyclic AMP, and that this represents only a small fraction of the total tissue cyclicAMP.
Journal ArticleDOI

The sequential inactivation of glycogen phosphorylase and activation of glycogen synthetase in liver after the administration of glucose to mice and rats. The mechanism of the hepatic threshold to glucose.

TL;DR: In some experiments, insulin caused a partial inactivation of phosphorylase in the liver of rats but more often was without effect, whereas a subsequent load of glucose caused the usual precipitous response, demonstrating that this effect of glucose was not mediated by insulin.
Journal ArticleDOI

Stimulation by vasopressin of glycogen breakdown and gluconeogenesis in the perfused rat liver.

TL;DR: The action of vasopressin on hepatic carbohydrate metabolism thus resembles that of glucagon; the minimum effective circulating concentrations of these hormones are of the same order (100pg/ml).
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