GLYCOGEN PHOSPHORYLASE AND GLYCOGEN SYNTHETASE ACTIVITY IN RED AND WHITE SKELETAL MUSCLE OF THE GUINEA PIG

1965 ◽  
Vol 43 (4) ◽  
pp. 463-468 ◽  
Author(s):  
Sydney St. George Stubbs ◽  
M. C. Blanchaer
Keyword(s):  
Skeletal Muscle ◽  
Guinea Pig ◽  
Glycogen Phosphorylase ◽  
White Muscle ◽  
Synthetase Activity ◽  
Fiber Types ◽  
Phosphorylase Activity ◽  
Glycogen Synthetase ◽  
Red Muscle ◽  
Wet Weight

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.

Regulation of glycolytic enzymes during anoxia in the turtle Pseudemys scripta

1989 ◽  
Vol 257 (2) ◽  
pp. R278-R283 ◽  
Author(s):  
S. P. Brooks ◽  
K. B. Storey
Keyword(s):  
Heart Muscle ◽  
Glycogen Phosphorylase ◽  
White Muscle ◽  
Fold Increase ◽  
Glycolytic Enzymes ◽  
Phosphorylase Activity ◽  
Enzyme Form ◽  
Red Muscle ◽  
Km Value ◽  
Glycogen Phosphorylase Activity

The glycolytic enzymes glycogen phosphorylase, phosphofructokinase (PFK), and pyruvate kinase (PK) were assessed in liver, heart, red muscle, and white muscle of aerobic and 5-h anoxic turtles (Pseudemys scripta) for changes in total activity and kinetic parameters. Anoxia induced statistically significant changes in these glycolytic enzymes in each of the four organs assayed. Compared with normoxic controls, anoxic liver showed a 3.3-fold increase in glycogen phosphorylase activity, a 1.5-fold increase in the PFK I50 value for citrate (concentration that inhibits initial activity by 50%), a 1.5-fold increase in the PFK Michaelis constant (Km) value for fructose 6-phosphate (P), and an increased maximal activity of PK. Anoxic heart muscle showed a 2.6-fold decrease in glycogen phosphorylase activity and, for PFK, a 1.7-fold decrease in the Km value for ATP and a twofold increase in the I50 value for citrate. In anoxic white muscle, PFK showed a fivefold lower Km value for fructose-6-P and a threefold lower activator concentration producing half-maximal activation (A50) for potassium phosphate than the aerobic enzyme form. Changes in anoxic white muscle PK included a twofold increase in the Km value for ADP and a 1.7-fold decrease in the I50 value for alanine. In red muscle, anoxia affected only the Km value for ATP, which was 50% higher than the value for the aerobic enzyme form. Fructose 2,6-diphosphate (P2) levels also decreased in heart muscle and increased in red and white muscle during anoxia.(ABSTRACT TRUNCATED AT 250 WORDS)

Isozymes of lactic dehydrogenase in skeletal muscle

1962 ◽  
Vol 202 (5) ◽  
pp. 827-829 ◽  
Author(s):  
M. C. Blanchaer ◽  
M. Van Wijhe
Keyword(s):  
Skeletal Muscle ◽  
Guinea Pig ◽  
Dehydrogenase Activity ◽  
White Muscle ◽  
Lactic Dehydrogenase ◽  
Human Muscle ◽  
Isozyme Pattern ◽  
Rabbit Muscle ◽  
Red Muscle ◽  
Dehydrogenase Isozyme

The lactic dehydrogenase (LD) isozyme patterns of red and white muscle of the guinea pig, rabbit, and mouse were examined by electrophoresis in barbiturate-buffered agar. Red muscle consistently yielded five bands of lactic dehydrogenase activity, but white muscle usually produced only two bands corresponding to isozymes IV and V. Traces of isozyme III were noted occasionally in the white muscle of the rabbit and mouse, but bands I and II were absent from the white muscle of all three species. Crystalline rabbit muscle lactic dehydrogenase produced an isozyme pattern resembling that of a mixture of red and white rabbit muscle. The lactic dehydrogenase isozyme pattern of human muscle reported by previous workers resembles that of a mixture of the red and white muscle patterns.

Effect of short-term vitamin E deficiency on guinea pig skeletal muscle myoglobin

1959 ◽  
Vol 197 (2) ◽  
pp. 491-493 ◽  
Author(s):  
A. D. Bender ◽  
D. D. Schottelius ◽  
B. A. Schottelius
Keyword(s):  
Skeletal Muscle ◽  
Vitamin E ◽  
Guinea Pig ◽  
Guinea Pigs ◽  
Short Term ◽  
Vitamin E Deficiency ◽  
Deficient Diet ◽  
Wet Weight ◽  
Masseter Muscles ◽  
Nitrogen Percentage

Myoglobin concentration was determined in gastrocnemius and masseter muscles of guinea pigs maintained up to 15 days on vitamin E-deficient and vitamin E-supplemented diets. A statistically significant increase in myoglobin was noted in muscles of animals on the deficient diet for 15 days. That the increase was real and not apparent was attested by studies of total nitrogen, noncollagen nitrogen, percentage of solids and muscle wet weight, all of which were the same in control and experimental muscles. Histological sections and creatine excretion studies confirmed the impression of mild, incipient nutritional dystrophy.

Intensity and duration of exercise effects on skeletal muscle cAMP, phosphorylase, and glycogen

1989 ◽  
Vol 66 (1) ◽  
pp. 190-194 ◽  
Author(s):  
A. H. Goldfarb ◽  
J. F. Bruno ◽  
P. J. Buckenmeyer
Keyword(s):  
Skeletal Muscle ◽  
Glycogen Phosphorylase ◽  
Fiber Types ◽  
Cyclic Monophosphate ◽  
Duration Effect ◽  
Fast Twitch ◽  
Camp Levels

To gain further insights into the mechanisms regulating skeletal muscle glycogenolysis during exercise, glycogen, phosphorylase, and adenosine 3',5'-cyclic monophosphate (cAMP) were determined in fast-twitch white (FTW) and fast-twitch red (FTR) muscle from groups of rats that ran for 0, 5, 10, 15, or 30 min at either 15 or 30 m/min. Glycogen degradation demonstrated an intensity and duration response in both fiber types. cAMP increased in both fiber types by 5 min and remained elevated at all times measured. FTW muscle cAMP levels were independent of both intensity and duration of exercise. FTR muscle cAMP levels were higher from 10 to 30 min at the 30-m/min intensity compared with the 15-m/min intensity. The ratio of the activity of phosphorylase in the presence of 2 mM AMP X 100 (phosphorylase a%) remained elevated at 20–22% independent of intensity and duration in FTW muscle; however, phosphorylase a% demonstrated an intensity and duration effect in FTR muscle. Glycogenolytic rates decreased with time, even though both cAMP and phosphorylase a% remained elevated in both fiber types. These data suggest that cAMP and phosphorylase a activation can be maintained during exercise in skeletal muscle but indicate a dissociation of these factors from glycogenolysis.

scholarly journals Low intrinsic running capacity is associated with reduced skeletal muscle substrate oxidation and lower mitochondrial content in white skeletal muscle

2011 ◽  
Vol 300 (4) ◽  
pp. R835-R843 ◽  
Author(s):  
Donato A. Rivas ◽  
Sarah J. Lessard ◽  
Misato Saito ◽  
Anna M. Friedhuber ◽  
Lauren G. Koch ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Insulin Sensitivity ◽  
Aerobic Capacity ◽  
Artificial Selection ◽  
White Muscle ◽  
Metabolic Diseases ◽  
Metabolic Health ◽  
Mitochondrial Content ◽  
Red Muscle ◽  
Selection For

Chronic metabolic diseases develop from the complex interaction of environmental and genetic factors, although the extent to which each contributes to these disorders is unknown. Here, we test the hypothesis that artificial selection for low intrinsic aerobic running capacity is associated with reduced skeletal muscle metabolism and impaired metabolic health. Rat models for low- (LCR) and high- (HCR) intrinsic running capacity were derived from genetically heterogeneous N:NIH stock for 20 generations. Artificial selection produced a 530% difference in running capacity between LCR/HCR, which was associated with significant functional differences in glucose and lipid handling by skeletal muscle, as assessed by hindlimb perfusion. LCR had reduced rates of skeletal muscle glucose uptake (∼30%; P = 0.04), glucose oxidation (∼50%; P = 0.04), and lipid oxidation (∼40%; P = 0.02). Artificial selection for low aerobic capacity was also linked with reduced molecular signaling, decreased muscle glycogen, and triglyceride storage, and a lower mitochondrial content in skeletal muscle, with the most profound changes to these parameters evident in white rather than red muscle. We show that a low intrinsic aerobic running capacity confers reduced insulin sensitivity in skeletal muscle and is associated with impaired markers of metabolic health compared with high intrinsic running capacity. Furthermore, selection for high running capacity, in the absence of exercise training, endows increased skeletal muscle insulin sensitivity and oxidative capacity in specifically white muscle rather than red muscle. These data provide evidence that differences in white muscle may have a role in the divergent aerobic capacity observed in this generation of LCR/HCR.

Influence of acclimation temperature on mitochondrial DNA, RNA, and enzymes in skeletal muscle

1998 ◽  
Vol 275 (3) ◽  
pp. R905-R912 ◽  
Author(s):  
Brendan James Battersby ◽  
Christopher D. Moyes
Keyword(s):  
Skeletal Muscle ◽  
Mitochondrial Dna ◽  
Steady State ◽  
Muscle Fiber ◽  
Copy Number ◽  
White Muscle ◽  
Fiber Types ◽  
Mitochondrial Enzymes ◽  
Dna Copy Number ◽  
Mitochondrial Content

Skeletal muscle fibers typically undergo modifications in their mitochondrial content, concomitant with alterations in oxidative metabolism that occur during the development of muscle fiber and in response to physiological stimuli. We examined how cold acclimation affects the mitochondrial properties of two fish skeletal muscle fiber types and how the regulators of mitochondrial content differed between tissues. After 2 mo of acclimation to either 4 or 18°C, mitochondrial enzyme activities in both red and white muscle were higher in cold-acclimated fish. No significant differences were detected between acclimation temperatures in the abundance of steady-state mitochondrial mRNA (cytochrome- c oxidase 1, subunit 6 of F0F1-ATPase), rRNA (16S), or DNA copy number. Steady-state mRNA for nuclear-encoded respiratory (adenine nucleotide translocase 1) and glycolytic genes showed high interindividual variability, particularly in the cold-acclimated fish. Although mitochondrial enzymes were 10-fold different between the two muscle types, mitochondrial DNA copy number differed only 4-fold. The relative abundance of mitochondrial mRNA and nuclear mRNA in red and white muscle reflected the differences in copy number of their respective genes. These data suggest that the response to physiological stimuli and determination of tissue-specific mitochondrial properties likely result from the regulation of nuclear-encoded genes.

EFFECTS OF FEEDING AND FOOD DEPRIVATION ON OXYGEN CONSUMPTION, MUSCLE PROTEIN CONCENTRATION AND ACTIVITIES OF ENERGY METABOLISM ENZYMES IN MUSCLE AND BRAIN OF SHALLOW-LIVING (SCORPAENA GUTTATA) AND DEEP-LIVING (SEBASTOLOBUS ALASCANUS) SCORPAENID FISHES

1993 ◽  
Vol 181 (1) ◽  
pp. 213-232 ◽  
Author(s):  
T. H. Yang ◽  
G. N. Somero
Keyword(s):  
Skeletal Muscle ◽  
Metabolic Rate ◽  
Food Deprivation ◽  
Enzyme Activities ◽  
Protein Concentration ◽  
White Muscle ◽  
Muscle Protein ◽  
Metabolism Enzymes ◽  
Red Muscle ◽  
Ad Libitum

The effects of feeding and fasting were examined on the deep-living short-spine thornyhead (Sebastolobus alascanus) and the confamilial shallow-living spotted scorpionfish (Scorpaena guttata) to determine whether the low metabolic rate of the deeper-living species was in part a consequence of food deprivation in its habitat. Laboratory acclimation for periods of 90–115 days under either ad libitum feeding or complete fasting did not lead to similar rates of respiration in individuals of the two species held under identical conditions. Respiration of fish fed ad libitum was 52 % (S. guttata) or 68 % (S. alascanus) higher than for fasted fish of the same species. Furthermore, the metabolic rates of freshly collected specimens of S. alascanus resembled those of laboratory-fasted fish. In white skeletal muscle, both total protein concentration and the activities of four enzymes of ATP metabolism, lactate dehydrogenase (LDH) and pyruvate kinase (PK) of glycolysis, malate dehydrogenase (MDH) and citrate synthase (CS, a citric acid cycle indicator), were lower in S. alascanus than in S. guttata. Within a species, protein concentration and activities of the four enzymes in white muscle, but not in brain, were higher in fed than in starved fish, although these differences were greater in S. alascanus than in S. guttata. During fasting, LDH and PK activity in white muscle of S. alascanus decreased much more than MDH and CS activity; decreases in enzyme activities in red muscle were smaller than those in white muscle. Activities of enzymes in white skeletal muscle of field-collected S. alascanus generally resembled those of the fasted specimens. In contrast, red muscle of field- collected S. alascanus, compared with that of either fed or starved laboratory-held specimens, had a highly glycolytic poise (high LDH and PK activities relative to MDH and CS activities), which may suggest that muscle enzyme activities in the field-collected fish reflect adaptation to the low oxygen level in its adult habitat, the oxygen minimum layer. The strong correlations found between tissue biochemical properties and respiration rate allow us to develop a predictive index for metabolic rate from simple biochemical analyses, e.g. white muscle protein content or CS activity. We conclude that the low metabolic rate of S. alascanus is due to at least four depth-related factors: reduced abundance of food, low temperature, low ambient oxygen concentration and darkness, which may select for reduced locomotory activity.

scholarly journals Role of insulin on exercise-induced GLUT-4 protein expression and glycogen supercompensation in rat skeletal muscle

2004 ◽  
Vol 96 (2) ◽  
pp. 621-627 ◽  
Author(s):  
Chia-Hua Kuo ◽  
Hyonson Hwang ◽  
Man-Cheong Lee ◽  
Arthur L. Castle ◽  
John L. Ivy
Keyword(s):  
Skeletal Muscle ◽  
Protein Expression ◽  
Muscle Glycogen ◽  
White Muscle ◽  
Insulin Response ◽  
Exercise Session ◽  
Carbohydrate Supplementation ◽  
Glut 4 ◽  
Red Muscle

The purpose of this study was to investigate the role of insulin on skeletal muscle GLUT-4 protein expression and glycogen storage after postexercise carbohydrate supplementation. Male Sprague-Dawley rats were randomly assigned to one of six treatment groups: sedentary control (Con), Con with streptozocin (Stz/C), immediately postexercise (Ex0), Ex0 with Stz (Stz/Ex0), 5-h postexercise (Ex5), and Ex5 with Stz (Stz/Ex5). Rats were exercised by swimming (2 bouts of 3 h) and carbohydrate supplemented immediately after each exercise session by glucose intubation (1 ml of a 50% wt/vol). Stz was administered 72-h before exercise, which resulted in hyperglycemia and elimination of the insulin response to the carbohydrate supplement. GLUT-4 protein of Ex0 rats was 30% above Con in fast-twitch (FT) red and 21% above Con in FT white muscle. In Ex5, GLUT-4 protein was 52% above Con in FT red and 47% above Con in FT white muscle. Muscle glycogen in FT red and white muscle was also increased above Con in Ex5 rats. Neither GLUT-4 protein nor muscle glycogen was increased above Con in Stz/Ex0 or Stz/Ex5 rats. GLUT-4 mRNA in FT red muscle of Ex0 rats was 61% above Con but only 33% above Con in Ex5 rats. GLUT-4 mRNA in FT red muscle of Stz/C and Stz/Ex0 rats was similar but significantly elevated in Ex5/Stz rats. These results suggest that insulin is essential for the increase in GLUT-4 protein expression following postexercise carbohydrate supplementation.

A METHODOLOGICAL STUDY IN MEASURING T3 AND T4 CONCENTRATION IN RED AND WHITE SKELETAL MUSCLE AND PLASMA OF EUTHYROID RATS

1979 ◽  
Vol 90 (1) ◽  
pp. 81-89 ◽  
Author(s):  
J. W. Janssen ◽  
C. van Hardeveld ◽  
A. A. H. Kassenaar
Keyword(s):  
Skeletal Muscle ◽  
White Muscle ◽  
Female Rats ◽  
Normal Female ◽  
Tissue Samples ◽  
Tissue Extracts ◽  
Red Muscle ◽  
The Mean ◽  
Ethanol Extracts ◽  
Altered Thyroid

ABSTRACT T3 and T4 concentrations were determined in plasma and red and white skeletal muscle of the rat. Because of the small tissue samples (± 300 mg), the ultra-sensitive Wick radioimmunoassay (RIA) for serum was adapted for determination in ethanol extracts. The dilution curves of the plasma and tissue extracts showed excellent parallelism with the standard curves for both T3 and T4. The mean T4 level found in female rats (n = 6) was 22.6 ± 5.2 ng/ml in plasma and did not differ significantly between red (1.85 ± 0.28 ng/g) and white (1.90 ± 0.25 ng/g) skeletal muscle. The mean T3 level in 11 normal female rats was 0.629 ± 0.098 ng/ml in the plasma and was significantly higher in the red muscle (2.07 ± 0.26 ng/g) than in the white muscle (1.65 ± 0.20 ng/g). The higher T3 levels found in the red muscle as compared with the white muscle may help to elucidate the different responsiveness of these muscle types observed in altered thyroid states.

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