scholarly journals Glycogen Synthetase Activity in Skeletal Muscle

1965 ◽  
Vol 240 (2) ◽  
pp. 588-593 ◽  
Author(s):  
William H. Danforth
1965 ◽  
Vol 43 (4) ◽  
pp. 463-468 ◽  
Author(s):  
Sydney St. George Stubbs ◽  
M. C. Blanchaer

Glycogen phosphorylase (α-1,4-glucan:orthophosphate glucosyltransferase) and glycogen synthetase (UDPG:α-1,4-glucan α-4-glucosyltransferase) have been examined in red and white skeletal muscle of the guinea pig. Histochemically phosphorylase was found to be more active in white than in red muscle fibers but no difference in glycogen synthetase could be detected between the fiber types. However, quantitative determinations showed that total glycogen synthetase activity (I + D) was higher in red than in white muscle (1.46 ± 0.14 S.E.M. vs. 0.71 ± 0.09 μmoles/minute per g wet weight at 37°). The converse relationship held for total phosphorylase activity (a + b), which was greater in white than in red muscle (19.24 ± 2.93 vs. 10.43 ± 2.34 μmoles/minute per g wet weight at 30°). The phosphorylase a level of 3.63 ± 0.96 in red muscle at rest was similar to that of 5.44 ± 1.19 in resting white muscle. Stimulation produced a significant conversion of phosphorylase b to a only in white muscle. After 30 seconds stimulation with 1-volt impulses of 20 milliseconds duration at a rate of 20 pulses per second, the phosphorylase a activities of red and white muscle were respectively 3.72 ± 1.88 and 16.66 ± 1.79. After stimulation the glycogen synthetase values in white and red muscle were 1.02 ± 0.07 and 1.72 ± 0.11 respectively.


1967 ◽  
Vol 242 (6) ◽  
pp. 1227-1231
Author(s):  
Enrique Belocopitow ◽  
Maria del Carmen Garcia Fernandez ◽  
Lutz Birnbaumer ◽  
Héctor N. Torres

1998 ◽  
Vol 275 (2) ◽  
pp. E359-E365 ◽  
Author(s):  
Jia-Li Luo ◽  
Folke Hammarqvist ◽  
Kerstin Andersson ◽  
Jan Wernerman

To gain insight into cellular metabolism underlying the glutathione (GSH) alterations induced by surgical trauma, we assessed postoperative skeletal muscle GSH metabolism and its redox status in 10 patients undergoing elective abdominal surgery. Muscle biopsy specimens were taken from the quadriceps femoris muscle before and at 24 and 72 h after surgery. GSH concentrations decreased by 40% at 24 h postoperatively compared with the paired preoperative values ( P < 0.001) and remained low at 72 h ( P < 0.01). The concentration of GSH disulfide (GSSG) did not significantly change throughout the study period, whereas the total GSH (as GSH equivalent) concentration decreased after surgery. Of the GSH constituent amino acids, the concentration of cysteine remained unchanged throughout the study period (from 28.2 ± 10.1 preoperatively to 29.4 ± 13.9 at 24 h postoperatively and to 28.3 ± 15.6 μmol/kg wet wt at 72 h postoperatively). Despite a reduction in glutamate concentration by 40% 24 h after surgery, no correlation was established between GSH and glutamate concentrations postoperatively. Activity of γ-glutamylcysteine synthetase did not change significantly after surgery, whereas GSH synthetase activity decreased postoperatively (from 66.4 ± 19.1 preoperatively to 41.0 ± 10.5 24 h postoperatively, P < 0.01, and to 46.0 ± 11.7 μU/mg protein 72 h postoperatively, P < 0.05). The decrease of GSH was correlated to the reduced GSH synthetase activity seen at 24 h postoperatively. These results indicate that the skeletal muscle GSH pool is diminished in patients after surgical trauma. The depletion of the GSH pool is associated with a decreased activity of GSH synthetase, indicating a decreased GSH synthetic capacity in skeletal muscle tissue.


1971 ◽  
Vol 122 (4) ◽  
pp. 697-699 ◽  
Author(s):  
A Margreth ◽  
S Di Mauro ◽  
A Tartarini ◽  
G Salviati

Nutrition ◽  
2006 ◽  
Vol 22 (7-8) ◽  
pp. 778-785 ◽  
Author(s):  
Carole Pinel ◽  
Véronique Coxam ◽  
Michelle Mignon ◽  
Daniel Taillandier ◽  
Christine Cubizolles ◽  
...  

1965 ◽  
Vol 97 (1) ◽  
pp. 32-36 ◽  
Author(s):  
HG Sie ◽  
A Hablanian

1. Ethionine-treated mice showed a marked depletion in liver glycogen, a decrease of glycogen-synthetase activity, an increase in activity of glucose 6-phosphate dehydrogenase and the solubilization of phosphorylase. 2. The administration of cortisol or glucose did not alleviate these changes but the effect of ethionine was completely prevented in animals given methionine as well as ethionine. 3. The activities of the following enzymes were unchanged: hexokinase, glucokinase, glucose 6-phosphatase, phosphoglucomutase, 6-phosphogluconate dehydrogenase, UDP-glucose pyrophosphorylase, UDP-glucose dehydrogenase and pyruvate kinase.


1968 ◽  
Vol 158 (3) ◽  
pp. 465-467 ◽  
Author(s):  
Hibbard E. Williams ◽  
Ulla I. Lundholm

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