Increased Muscle Phosphorylase Activity in the Starved Rat

Nature ◽  
1948 ◽  
Vol 162 (4130) ◽  
pp. 1002-1003 ◽  
Author(s):  
KNUD LUNDBÆK ◽  
EWALD S. GORANSON
Keyword(s):  
Phosphorylase Activity ◽  
Muscle Phosphorylase ◽  
Muscle Phosphorylase Activity

scholarly journals Glycogen storage disease associated with glycogen deposition in skeletal and heart muscle with low muscle phosphorylase activity.

1985 ◽  
Vol 74 (7) ◽  
pp. 945-951
Author(s):  
Tatsumi UCHIDA ◽  
Akio KODAMA ◽  
Masatoshi TAKEZAWA ◽  
Mikihiro KIJIMA ◽  
Yoshihiro MIYAZAKI ◽  
...  
Keyword(s):  
Glycogen Storage Disease ◽  
Heart Muscle ◽  
Storage Disease ◽  
Glycogen Storage ◽  
Phosphorylase Activity ◽  
Muscle Phosphorylase ◽  
Glycogen Deposition ◽  
Muscle Phosphorylase Activity

Phosphorylase and glycogen levels in skeletal muscle and liver of hibernating and nonhibernating bats

1959 ◽  
Vol 197 (5) ◽  
pp. 1059-1062 ◽  
Author(s):  
Samuel L. Leonard ◽  
William A. Wimsatt
Keyword(s):  
Skeletal Muscle ◽  
Muscle Glycogen ◽  
Liver Glycogen ◽  
Myotis Lucifugus ◽  
Phosphorylase Activity ◽  
Activity Ratios ◽  
Muscle Phosphorylase ◽  
Wet Weight ◽  
Muscle Phosphorylase Activity ◽  
Made In

Determinations of skeletal muscle and liver glycogen concentration and active a and total t phosphorylase activities were made in bats ( Myotis lucifugus) hibernating at 3°–5° and 20 hours after arousal at room temperature. After arousal, liver glycogen was decreased by half and muscle glycogen was increased over twofold. Concomitantly, muscle phosphorylase a was increased, phosphorylase t was unchanged and the ratio a/t was increased. In the liver, phosphorylase a, t and the ratios were increased upon arousal (calculated per unit of wet weight and per mg N). Epinephrine treatment was ineffective in the torpid hibernating bats, but in aroused bats, it decreased muscle and liver glycogen but increased muscle phosphorylase activity ratios only slightly. Histamine was ineffective in the aroused bats. Stimulating aroused bats to fly for short periods consistently resulted in lower muscle glycogen levels and in no change in muscle phosphorylase activity ratios. It is concluded that a) at least part of the increased muscle glycogen in the aroused bats comes from the liver, b) the changes in glycogen levels and phosphorylase activity are in some manner related and c) liver phosphorylase changes upon arousal, unlike that in muscle phosphorylase, involves an increase in total enzyme potential.

Regulation of muscle phosphorylase activity by carnosine and anserine

1982 ◽  
Vol 109 (3) ◽  
pp. 769-775 ◽  
Author(s):  
Peter Johnson ◽  
Joanne S. Fedyna ◽  
Andrew Schindzielorz ◽  
Cindylu Moritz Smith ◽  
Peter J. Kasvinsky
Keyword(s):  
Phosphorylase Activity ◽  
Muscle Phosphorylase ◽  
Muscle Phosphorylase Activity

McArdle Disease: Familial Variety of Muscle Phosphorylase Activity in Two Siblings

1984 ◽  
Vol 26 (1) ◽  
pp. 10-15
Author(s):  
Kihei Maekawa ◽  
Hiroshi Shimizu ◽  
Yoshikatsu Eto ◽  
Ikuya Nonaka
Keyword(s):  
Phosphorylase Activity ◽  
Mcardle Disease ◽  
Muscle Phosphorylase ◽  
Muscle Phosphorylase Activity

Regulation of glycogenolysis in human muscle at rest and during exercise

1982 ◽  
Vol 53 (3) ◽  
pp. 708-715 ◽  
Author(s):  
D. Chasiotis ◽  
K. Sahlin ◽  
E. Hultman
Keyword(s):  
Glycogen Phosphorylase ◽  
Total Activity ◽  
Human Muscle ◽  
Phosphorylase Activity ◽  
Michaelis Constant ◽  
Bicycle Exercise ◽  
Muscle Phosphorylase ◽  
Glycogen Utilization ◽  
Main Factors

The regulation of glycogenolysis in human muscle during isometric and dynamic exercise has been investigated. Total glycogen phosphorylase and synthase activities were unchanged during exercise. The fraction of phosphorylase in the alpha form at rest was estimated to be 20%, but the data indicate that the in vivo activity was low and critically dependent on the concentration of inorganic phosphate (Pi) in the muscle. Phosphorylase alpha increased initially 2.4-fold during isometric contraction and 1.6-fold during maximal bicycle exercise but reverted to or below the resting value at fatigue/exhaustion. At rest synthase I was 1713;48% of the total activity but decreased during exercise to about half of this value. The reciprocal changes in phosphorylase and synthase correlate with the enhanced rate of glycogenolysis during exercise. Michaelis constant (Km) for Pi was 27 mmol . l-1 for phosphorylase alpha and 7 mmol . l-1 for alpha + b. From consideration of the changes in Pi during exercise (to 20–30 mmol . l–1) it was concluded that Pi is one of the main factors determining phosphorylase activity and provides a link between phosphocreatine breakdown and glycogen utilization in muscle.

scholarly journals Adenovirus-mediated delivery into myocytes of muscle glycogen phosphorylase, the enzyme deficient in patients with glycogen-storage disease type V

1994 ◽  
Vol 304 (3) ◽  
pp. 1009-1014 ◽  
Author(s):  
S Baqué ◽  
C B Newgard ◽  
R D Gerard ◽  
J J Guinovart ◽  
A M Gómez-Foix
Keyword(s):  
Muscle Glycogen ◽  
Glycogen Phosphorylase ◽  
Recombinant Adenovirus ◽  
Genetic Diseases ◽  
C2c12 Myoblast ◽  
Mrna Levels ◽  
Phosphorylase Activity ◽  
Muscle Phosphorylase ◽  
The Impact

The feasibility of using adenovirus as a vector for the introduction of glycogen phosphorylase activity into myocytes has been examined. We used the C2C12 myoblast cell line to assay the impact of phosphorylase gene transfer on myocyte glycogen metabolism and to reproduce in vitro the two strategies proposed for the treatment of muscle genetic diseases, myoblast transplantation and direct DNA delivery. In this study, a recombinant adenovirus containing the muscle glycogen phosphorylase cDNA transcribed from the cytomegalovirus promoter (AdCMV-MGP) was used to transduce both differentiating myoblasts and nondividing mature myotube cells. Muscle glycogen phosphorylase mRNA levels and total phosphorylase activity were increased in both cell types after viral treatment although more efficiently in the differentiated myotubes. The increase in phosphorylase activity was transient (15 days) in myoblasts whereas in myotubes higher levels of phosphorylase gene expression and activity were reached, which remained above control levels for the duration of the study (20 days). The introduction of muscle phosphorylase into myotubes enhanced their glycogenolytic capacity. AdCMV MGP-transduced myotubes had lower glycogen levels under basal conditions. In addition, these engineered cells showed more extensive glycogenolysis in response to both adrenaline, which stimulates glycogen phosphorylase phosphorylation, and carbonyl cyanide m-chlorophenylhydrazone, a metabolic uncoupler. In conclusion, transfer of the muscle glycogen phosphorylase cDNA into myotubes confers an enhanced and regulatable glycogenolytic capacity. Thus this system might be useful for delivery of muscle glycogen phosphorylase and restoration of glycogenolysis in muscle cells from patients with muscle phosphorylase deficiency (McArdle's disease).

scholarly journals LOCALIZATION OF SKELETAL MUSCLE PHOSPHORYLASE USING A FLUORESCENT ANTIBODY TECHNIQUE AND ITS CORRELATION WITH HISTOCHEMICAL OBSERVATIONS

1965 ◽  
Vol 13 (6) ◽  
pp. 454-460 ◽  
Author(s):  
HAROLD F. DVORAK ◽  
RICHARD B. COHEN
Keyword(s):  
Striated Muscle ◽  
Fluorescent Antibody ◽  
Significant Inhibition ◽  
Fluorescent Antibody Technique ◽  
Rabbit Muscle ◽  
Phosphorylase Activity ◽  
Specific Staining ◽  
Antibody Technique ◽  
Specific Antisera ◽  
Muscle Phosphorylase

The Coons fluorescent antibody technique was employed to localize rabbit muscle phosphorylase within striated muscle cells. Pooled sera from guinea pigs sensitized against 2X crystallized rabbit phosphorylase a in complete Freund's adjuvant gave a single line of precipitation with the enzyme in Ouchterlony plates. Such sera, tagged with fluorescein isothiocyanate and applied to thin frozen sections of rabbit striated muscle, produced a specific, granular, fluorescing precipitate which was localized to the sarcoplasm between myofibrils. Preincubation with untagged specific antisera prevented specific staining. Appropriate control sera, similarly tagged, produced only slight nonspecific fluorescence. With properly absorbed specific antisera, staining was specific for striated muscle as opposed to rabbit liver or smooth muscle. The fluorescent antibody findings were correlated with those obtained by classical histochemieal studies of phosphorylase activity. In addition, application of antisera to sections of rabbit muscle before incubation in substrate resulted in significant inhibition of histochemically demonstrable phosphorylase activity whereas control sera had little or no inhibitory effect.

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