scholarly journals Metabolism of hexose phosphate esters. 1. Metabolism in normal and alloxan-diabetic rabbits. 2. Metabolism in isolated rat diaphragm and the influence of insulin

1953 ◽  
Vol 54 (4) ◽  
pp. 529-539 ◽  
Author(s):  
Anne Beloff-Chain ◽  
E. B. Chain ◽  
D. Bovet ◽  
F. Pocchiari ◽  
R. Catanzaro ◽  
...  
1970 ◽  
Vol 119 (1) ◽  
pp. 27-30 ◽  
Author(s):  
Anne Beloff-Chain ◽  
E. B. Chain ◽  
K. A. Rookledge

1. The influence of insulin on the metabolism of [1-14C]glucosamine by diaphragm muscle from normal rats and rats rendered diabetic with streptozotocin has been studied. 2. The glucosamine was converted into glucosamine 1-phosphate, glucosamine 6-phosphate, glycogen, lactate and small amounts of other unidentified intermediates. 3. Insulin increased the incorporation of 14C into glycogen in both the normal and diabetic muscle, but did not increase the formation of the glucosamine phosphate esters. 4. The 14C content in the glycogen was present partly as glucose and partly as glucosamine; there was significantly more [14C]glucose in the glycogen of the diabetic muscle than in that of the normal muscle.


1967 ◽  
Vol 54 (4) ◽  
pp. 645-662 ◽  
Author(s):  
Å. Hjalmarson ◽  
K. Ahrén

ABSTRACT The effect of growth hormone (GH) in vitro on the rate of intracellular accumulation of the non-utilizable amino acid α-aminoisobutyric acid (AIB) was studied in the intact rat diaphragm preparation. Bovine or ovine GH (25 μg/ml incubation medium) markedly stimulated the accumulation of AIB-14C by diaphragms from hypophysectomized rats, while there was no or only a very slight effect on diaphragms from normal rats. In diaphragms from rats with the pituitary gland autotransplanted to the kidney capsule GH in vitro stimulated the accumulation of AIB-14C significantly more than in diaphragms from normal rats but significantly less than in diaphragms from hypophysectomized rats. Injections of GH intramuscularly for 4 days to hypophysectomized rats made the diaphragms from these rats less sensitive or completely insensitive to GH in vitro. These results indicate strongly that the relative insensitivity to GH in vitro of diaphragms from normal rats is due to the fact that the muscle tissues from these rats has been exposed to the endogenously secreted GH. The results show that GH can influence the accumulation of AIB-14C in the isolated rat diaphragm in two different ways giving an acute or »stimulatory« effect and a late or »inhibitory« effect, and that it seems to be a time-relationship between these two effects of the hormone.


1951 ◽  
Vol 189 (1) ◽  
pp. 59-63
Author(s):  
Niels. Haugaard ◽  
Julian B. Marsh ◽  
William C. Stadie

1952 ◽  
Vol 197 (1) ◽  
pp. 151-166 ◽  
Author(s):  
C.R. Park ◽  
David H. Brown ◽  
Marvin. Cornblath ◽  
William H. Daughaday ◽  
M.E. Krahl

1975 ◽  
Vol 78 (2) ◽  
pp. 392-400
Author(s):  
Arne T. Hostmark ◽  
Ole Grønnerød ◽  
Robert S. Horn

ABSTRACT The antagonism between insulin and selective adrenergic stimulation on the converting systems for glycogen synthetase and phosphorylase has been investigated in the isolated rat diaphragm. Insulin significantly inhibited stimulation by terbutaline and noradrenaline of phosphorylase b to a conversion as well as stimulation of glycogen synthetase I to D conversion by these agents. The inhibition by insulin was stronger on the synthetase system than on the phosphorylase system. The insulin effect was not dependent upon the presence of glucose. In diaphragms from 24 h fasted rats the response of the phosphorylase system to both agonists decreased. Inhibition by insulin of terbutaline stimulated phosphorylase conversion was maintained upon fasting while no effect of insulin against stimulation by noradrenaline could be obtained in diaphragms from fasted rats. The effects of fasting and insulin were not influenced by beta adrenergic antagonists (practolol and butoxamine). The results indicate a difference in sensitivity of the synthetase and phosphorylase systems to insulin and suggest that noradrenaline and terbutaline influence glycogen metabolism by differing mechanisms.


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