The metabolism of the tonic and tetanic muscles I. Glycolytic metabolism

Domonkos, J

doi:10.1016/0003-9861(61)90118-7

Cited by 23 publications

(4 citation statements)

References 17 publications

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“…The relative contribution of the two forms of ghosghorylase in determining the rate of glycogenolysis in red and white muscle has not been assessed. However, it is of interest that red muscle, which converted little of its phosphorylase b to a under the present conditions, is also known to have a slower glycogenolytic rate than white rnuscle (3,9). The conversion of most of the white muscle enzyme to the a form appears to be an appropriate response in a tissue that relies on glycolysis to provide energy for its characteristic short intense bouts of anaerobic work.…”

Section: Di~cussionmentioning

confidence: 84%

Glycogen Phosphorylase and Glycogen Synthetase Activity in Red and White Skeletal Muscle of the Guinea Pig

Stubbs¹,

Blanchaer²

1965

Can. J. Biochem.

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Glycogen phosphorylase (a-1,4-glucan: orthophosphate glucosyltransferase) and glycogen synthetase {UBPG:a-1,Q-glucan a-4-glucosyltransfepase) have been examined in red and white skeletal mmcle of the guinea pig. Histochemically phosphorylase was foulid to be more active in white than in red muscle fibers but no difference in glycogen synthetase could be detected between the fiber types. H s~~v e r , quantitative determinations showed that total glycogen synthetase activity (I + D) was higher in red than in white muscle (1.48 f 0.14 S.E.M. vs. 0.71 f 0.09 yrnslee/minute per g wet weight a t 37'). The converse reIatiotnship held for total phosphorylase activity (a -+ +b), which was greater in white than in red muscle (19.24 f 2.93 vs. 10.43 f 2.84 Irmoles/minute per g wet weight a t 38"). The phosphsr$ase a level of 3.63 f 8.96 in red muscle a t rest was simiiar to that of 5.44 f 1.19 in resting white muscle. Stimulation produced a significant csnversion of phosphsrylase 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 phosphory-lase a activities of red and white muscle were respectively 3.72 f 1.88 and 16.66 f 1.79. After stimulation the glycogen synthetase values in white and red muscle were 1.82 % 0.07 and 1.72 f 0.11 respectively. lSupprted by grants from the C a d i a n Muscular Dystrophy Association and the Medical Research Council of Canada. This work was submitted by S. St. George Stubbs in partial fulfillment of the requirements f a the degree of B.Sc (Med.).

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Section: Di~cussionmentioning

confidence: 84%

Glycogen Phosphorylase and Glycogen Synthetase Activity in Red and White Skeletal Muscle of the Guinea Pig

Stubbs¹,

Blanchaer²

1965

Can. J. Biochem.

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“…So for example, the smooth muscle may show the characteristics of the aerobic type (cf. [45][46][47]. I n this connection, the investigated activity ratios of hexokinase are surprising.…”

Section: Discussionmentioning

confidence: 99%

Metabolic Differentiation of Distinct Muscle Types at the Level of Enzymatic Organization

Bass¹,

Brdiczka

Eyer

et al. 1969

European Journal of Biochemistry

624

245

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Activity levels of glycogen phosphorylase, hexokinase, triosephosphate dehydrogenase, lactate dehydrogenase, citrate synthase, 3-hydroxyacyl-CoA dehydrogenase, glycerolphosphate dehydrogenase (mitochondrial), and hexosediphosphatase have been determined in white (fast) muscles, red (slow) muscles, heart and smooth muscle of higher animals. The activities of these enzymes are taken as relative measures of metabolic capacities. Their ratios are interpreted as representing relations of different metabolic pathways or systems. I n all muscles investigated comparable ratios exist for phosphorylase/triosephosphate dehydrogenase (glycogenolysis/glycolysis), glycerolphosphate dehydrogenase/triosephosphate dehydrogenase (mitochondrial glycerolphosphate oxidation/glycolysis), triosephosphate dehydrogenase/lactate dehydrogenase (glycolysis/lactate fermentation), hexokinaselcitrate synthase (glucose phosphorylation/citric acid cycle) and 3-hydroxyacyl-CoA dehydrogenase/citrate synthase (fatty acid oxidation/citric acid cycle). With respect to the constancy of these ratios, consistent characteristics exist in the organization of the enzyme activity pattern. It is suggested that the more or less invariable coordination of these metabolic systems is not subject to metabolic differentiation. On the contrary, metabolic Werentiation is reflected by extreme variations of the following ratios : triosephosphate dehydrogenase/3-hydroxyacyl-CoA dehydrogenase (glycolysis/fatty acid oxidation), triosephosphate dehydrogenase/citrate synthase (glycolysis/citric acid cycle), lactate dehydrogenaselcitrate synthase (lactate fermentation/citric acid cycle), phosphorylase/hexokinase (glycogenolysis/glucose phosphorylation), and hexosediphosphatase/hexokinase (gluconeogenesis/ glucose phosphorylation). These variable enzyme activity ratios are discriminative magnitudes and make it possible to discern distinct metabolic types of muscle. White (fast) muscle is characterized by high capacities of glycogenolysis, glycolysis and lactate fermentation, whereas the capacities of glucose phosphorylation, citric acid cycle and fatty acid oxidation are low. Red (slow) muscles, heart and smooth muscle show inverse characteristics. I n white (fast) muscle, high activities of hexosediphosphatase and of mitochondrial glycerolphosphate dehydrogenase indicate that gluconeogenesis starting from glycerolphosphate or triosephosphate is probably important in this muscle type, and compensates for its low capacity of glucose phosphorylation.Enzymes. Adenylate deaminase, or AMP aminohydrolase (EC 3.5.4.6) ; adenylate kinase, or ATP: AMP phosphotransferase (EC 2.7.4.3) ; citrate synthase, or citrate oxaloacetate lyase (CoA-acetylating) (EC 4.1.3.7) ; glucosephosphate isomerase, or ~-glucose-B-phosphate ketol-isomerase (EC 5.3.1.9); glucose-6-phosphate dehydrogenase, or n-glucose-&phosphate: NADP oxidoreductase (EC 1.1.1.49); glycerolphosphate dehydrogenase, or ~-glycerol-3-phosphate: (acceptor) oxidoreductase (EC 1.1.99.5); 3-hydroxyacyl-CoA dehydrogenase, or L-3-hydro...

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“…Par ailleurs, l'utilisation du glycogène dépend de façon caractéristique du type de muscle (Villa Moruzzi et al, 1981 ) : glycogénolyse et glycolyse, mesurées par la production de pyruvate et de lactate, sont deux fois plus élevées dans les muscles blancs que dans les muscles rouges (Domonkos, 1961 ;Bocek et al, 1966). Ce (Opie et Newsholme, 1967), n'en incorpore que très peu (McLane et Holloszy, 1979).…”

Section: A) Propriétés Des Fibres Musculairesunclassified

Propriétés des fibres musculaires squelettiques. 1. Influence de l'innervation motrice

Bacou¹,

Vigneron²

1988

Reprod. Nutr. Dévelop.

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The metabolism of the tonic and tetanic muscles I. Glycolytic metabolism

Cited by 23 publications

References 17 publications

Glycogen Phosphorylase and Glycogen Synthetase Activity in Red and White Skeletal Muscle of the Guinea Pig

Glycogen Phosphorylase and Glycogen Synthetase Activity in Red and White Skeletal Muscle of the Guinea Pig

Metabolic Differentiation of Distinct Muscle Types at the Level of Enzymatic Organization

Propriétés des fibres musculaires squelettiques. 1. Influence de l'innervation motrice

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