scholarly journals Biochemistry of dystrophic muscle. 2. Some enzyme changes in dystrophic mouse muscle

1963 ◽  
Vol 88 (1) ◽  
pp. 64-68 ◽  
Author(s):  
RJ Pennington
Keyword(s):  
Dystrophic Muscle ◽  
Mouse Muscle ◽  
Dystrophic Mouse ◽  
Enzyme Changes

Enzyme studies of skeletal muscle in mice with hereditary muscular dystrophy

1963 ◽  
Vol 205 (5) ◽  
pp. 897-901 ◽  
Author(s):  
Marilyn W. McCaman
Keyword(s):  
Skeletal Muscle ◽  
Muscular Dystrophy ◽  
Glutathione Reductase ◽  
Enzyme Activities ◽  
Lactic Dehydrogenase ◽  
Normal Muscle ◽  
Dystrophic Muscle ◽  
Nerve Section ◽  
Mouse Muscle ◽  
Dystrophic Mouse

The activities of 20 enzymes in normal, heterozygous, and dystrophic mouse muscle were studied by means of quantitative microchemical methods. Enzyme activities in normal and heterozygous muscle were essentially the same. In dystrophic muscle glucose-6-P dehydrogenase, 6-P-gluconic dehydrogenase, glutathione reductase, peptidase, ß-glucuronidase, and glucokinase activities were significantly higher than in normal muscle, while α-glycero-P dehydrogenase and lactic dehydrogenase activities were significantly lower. The pattern of enzyme activities found in normal gastrocnemius denervated by nerve section was strikingly similar to that in dystrophic muscle.

ALDOLASE ACTIVITY IN NORMAL AND DYSTROPHIC MOUSE MUSCLE

1964 ◽  
Vol 42 (9) ◽  
pp. 1301-1305 ◽  
Author(s):  
U. Srivastava ◽  
L. Berlinguet
Keyword(s):  
Nitrogen Content ◽  
Total Nitrogen ◽  
Total Nitrogen Content ◽  
Dystrophic Muscle ◽  
Mouse Muscle ◽  
Dystrophic Mouse ◽  
Aldolase Activity ◽  
Dystrophic Mice

Aldolase activity and nitrogen content of the muscle were determined in hereditary muscular dystrophic mice and their normal litter mates at various ages. Aldolase activity was found to decrease in dystrophic muscle when expressed per mg of wet tissue but showed an increase at later stages of the disease when expressed per mg of total nitrogen in muscle. Total nitrogen content of dystrophic muscle decreased considerably during the evolution of the disease. In normal mice, the muscle aldolase activity increases with age.

PROTEOLYTIC ENZYMES IN NORMAL AND DYSTROPHIC MOUSE MUSCLE

1966 ◽  
Vol 44 (5) ◽  
pp. 613-623 ◽  
Author(s):  
L. Berlinguet ◽  
U. Srivastava
Keyword(s):  
Proteolytic Enzymes ◽  
Chemical Change ◽  
Optimum Conditions ◽  
Normal Muscle ◽  
Dystrophic Muscle ◽  
Muscle Enzymes ◽  
Mouse Muscle ◽  
Ph Values ◽  
Dystrophic Mouse ◽  
Dystrophic Mice

Proteolytic enzymes extracted from normal and dystrophic mouse muscle were studied, and optimum conditions for their activities were established. It was found that these enzymes were active at two pH values, 7.5 and 9. In normal and dystrophic mice, the enzymatic activity increased with age. When the activities of dystrophic muscle enzymes were compared with those of normal muscle enzymes, the increase was most significant in animals 60–90 days of age. The results obtained when the enzymes extracted from normal or dystrophic muscle were incubated with substrates from normal or dystrophic muscle indicate that the defect in the muscle is due to an increase in the activities of the proteolytic enzymes rather than to a chemical change in the muscle proteins.

scholarly journals Comparison of the protein-synthesizing machinery in the skeletal muscle of normal and dystrophic Bar Harbor mice

1969 ◽  
Vol 115 (3) ◽  
pp. 377-382 ◽  
Author(s):  
D. C. Watts ◽  
J. D. Reid
Keyword(s):  
Normal Mouse ◽  
Gradient Centrifugation ◽  
Absolute Difference ◽  
Similar Data ◽  
Dystrophic Muscle ◽  
Mouse Muscle ◽  
Dystrophic Mouse ◽  
Dna And Rna ◽  
Leg Muscle ◽  
Standard Protein

1. Although the total weight of leg muscle increased with the age of a normal mouse the DNA and RNA content per leg did not change significantly. 2. The weight of leg muscle from a dystrophic mouse was only about 45% of that from a normal mouse but the DNA and RNA contents were the same and hence similar DNA/RNA ratios were obtained. 3. The total ribosome contents of normal and dystrophic mice were the same on a whole-leg basis, and for both the free ribosomes were about 60% of the total. However, comparison with similar data from liver suggested that some loss of ribosomes occurred during the isolation procedure. 4. The polyribosome patterns obtained by density-gradient centrifugation were the same for normal and dystrophic muscle, and comparable polyribosome fractions of different sizes obtained from such gradients had similar capacities for the incorporation of radioactive amino acids in a standard protein-synthesizing system. 5. By using a standard protein-synthesizing system with normal polyribosomes similar extents of incorporation were found with normal- or dystrophic-muscle pH5 fraction or partially purified transfer RNA preparation. 6. It is concluded that there is no absolute difference between the protein-synthesizing systems of normal and dystrophic mouse muscle and that the observed apparent differences result from concentration differences caused by changes in muscle volume. 7. A possible cause of the failure of dystrophic muscle to resynthesize myofibrils is also suggested.

CHOLINESTERASE AND MONOAMINE OXIDASE ACTIVITIES IN SKELETAL MUSCLE OF NORMAL AND HEREDITARY DYSTROPHIC MICE

1967 ◽  
Vol 45 (4) ◽  
pp. 573-580 ◽  
Author(s):  
Uma Srivastava ◽  
Louis Berlinguet
Keyword(s):  
Monoamine Oxidase ◽  
Total Nitrogen ◽  
Oxidase Activity ◽  
High Sensitivity ◽  
Lens Protein ◽  
Fresh Weight ◽  
Dystrophic Muscle ◽  
Mouse Muscle ◽  
Dystrophic Mouse ◽  
Amine Content

Acetyl- and butyryl-cholinesterase activities in dystrophic mouse muscle are increased significantly, whether the results are expressed in relation to (a) the fresh weight or (b) the total nitrogen, of the muscle. Activities of these enzymes do not show any change in normal and dystrophic mouse liver and brain. However, in dystrophic lens, the enzymatic activity is decreased when the results are expressed on the basis of fresh weight. This is because of a change in the chemical composition of the lens since no significant change in both enzymatic activities could be observed when the results were expressed on the basis of lens protein. This increase in the cholinesterase activity of dystrophic muscle is not incompatible with the change in the distribution pattern of these enzymes in the muscle noted by many workers, or to the high sensitivity of dystrophic muscle to acetylcholine.Monoamine oxidase activity in dystrophic mouse muscle showed a significant increase when the results are expressed in relation to (a) the fresh weight or (b) the total nitrogen, of the muscle. This increase in activity could be due to enzyme induction, i.e. increase in the amine content followed by an increase in monoamine oxidase activity in dystrophic muscle.

Phase portraits of dystrophic and nondystrophic mouse muscle-fiber action potentials

1965 ◽  
Vol 208 (4) ◽  
pp. 724-731 ◽  
Author(s):  
Titus C. Evans ◽  
Byron A. Schottelius
Keyword(s):  
Muscle Fiber ◽  
Action Potentials ◽  
Sodium Ion ◽  
Phase Portraits ◽  
Dystrophic Muscle ◽  
General Increase ◽  
Ion Conductance ◽  
Mouse Muscle ◽  
Intracellular Action ◽  
Fiber Action

Intracellular action potentials from normal, control nondystrophic and dystrophic mouse soleus muscle fibers were recorded in both voltage-time and phase-portrait plots. Flattening of a normally curved portion in certain dystrophic muscle-fiber phase portraits suggested a greater than usual secondary entry of sodium ions after the peak of the action potential. Low-chloride studies excluded an abnormal chloride current as the cause of the flattening. It appears that inactivation of sodium ion conductance may be delayed or reduced, or both, in certain fibers of mice with hereditary muscular dystrophy. This is consistent with a general increase in membrane permeability. No definite negative afterpotential was noted in most mouse muscle-fiber action potentials.

Serial passaging and differentiation of myogenic cells isolated from dystrophic mouse muscle

Nature ◽  
1977 ◽  
Vol 270 (5639) ◽  
pp. 725-727 ◽  
Author(s):  
DAVID YAFFE ◽  
ORA SAXEL
Keyword(s):  
Myogenic Cells ◽  
Mouse Muscle ◽  
Dystrophic Mouse

Effects of denervation on normal and dystrophic muscle: DNA and nucleotide enzymes

1965 ◽  
Vol 209 (3) ◽  
pp. 495-500 ◽  
Author(s):  
M. W. McCaman ◽  
R. E. McCaman
Keyword(s):  
Purine Nucleoside Phosphorylase ◽  
Nucleotide Metabolism ◽  
Purine Nucleoside ◽  
Denervated Muscle ◽  
Normal Muscle ◽  
Dystrophic Muscle ◽  
P Values ◽  
Nucleoside Phosphorylase ◽  
Dystrophic Mouse ◽  
Protein Versus

The activities of five enzymes associated with nucleotide metabolism, as well as values for protein and DNA-P, in homogenates from normal, dystrophic, and denervated (3–46 days) normal and dystrophic mouse gastrocnemii have been reported. When the data were expressed per muscle, the following observations were made: protein was much lower in dystrophic than in normal muscle and decreased in both muscles after denervation; DNA-P values remained relatively constant in normal muscle after denervation whereas the values in dystrophic muscle were slightly lower; adenylic deaminase activity decreased rapidly and profoundly after denervation of normal muscle, approaching values found in dystrophic muscle; purine nucleoside phosphorylase and 5-nucleotidase activities were similar in normal and dystrophic muscle and remained relatively constant after denervation; Ca- and Mg-ATPase activities were considerably lower in dystrophic muscle and decreased in both normal and dystrophic muscle after denervation. The different interpretations of the same data which are possible by expressing data per unit protein versus per muscle were discussed. These results confirm earlier studies which demonstrated the striking biochemical similarity between dystrophic and denervated muscle.

Sign in / Sign up

Export Citation Format

Share Document