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.

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.

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.

BIOCHEMICAL CHANGES IN PROGRESSIVE MUSCULAR DYSTROPHY: VI. INCORPORATION OF URIDINE-2-14C INTO RNA OF VARIOUS TISSUE OF NORMAL AND DYSTROPHIC MICE

1967 ◽  
Vol 45 (9) ◽  
pp. 1419-1425 ◽  
Author(s):  
Uma Srivastava
Keyword(s):  
Muscular Dystrophy ◽  
Soluble Fraction ◽  
Normal Liver ◽  
Biochemical Changes ◽  
Normal Muscle ◽  
Dystrophic Muscle ◽  
Progressive Muscular Dystrophy ◽  
Dystrophic Mice

Normal and dystrophic mice were injected intravenously with uridine-2-14C at various stages of the disease. Radioactivity in the acid-soluble fraction of most of the tissues studied was unchanged or not significantly different in dystrophic animals. In vivo incorporation of uridine-2-14C into RNA increased in dystrophic muscle as compared to normal muscle at 30 days, remained the same at 60 days, and was reduced at 90 days. Similar results were also observed on the in vitro incorporation of uridine-2-14C catalyzed by homogenates of normal and dystrophic muscle. Dystrophic brain and pancreas showed a decrease in the incorporation at each stage investigated as compared to controls. No change in the incorporation was noted in dystrophic and normal liver, kidney, spleen, and heart. The decrease in uridine-2-14C incorporation in dystrophic muscle at 90 days could be due to an increased RNA content. Such a phenomenon was explained as due to infiltration of dystrophic muscle by invading macrophages.It is concluded that the metabolism of RNA is not decreased in the dystrophic muscle in preliminary stages of the disease as compared to the control.

Phosphorylase activation in stimulated dystrophic mouse muscle

1962 ◽  
Vol 202 (5) ◽  
pp. 821-823 ◽  
Author(s):  
R. R. Rulon ◽  
D. D. Schottelius ◽  
B. A. Schottelius
Keyword(s):  
Electrical Stimulus ◽  
Significant Decline ◽  
Dystrophic Muscle ◽  
Littermate Control ◽  
Mouse Muscle ◽  
Quick Freezing ◽  
Anterior Tibial ◽  
Chemical Events ◽  
T Values ◽  
Dystrophic Mice

Phosphorylase a, t( a + b), and a: t x 100 values/g of wet muscle were determined on paired anterior tibial muscles from Bar Harbor strain 129 dystrophic and littermate control mice after tetanizing one member of the pair from 1/2–15 sec with an electrical stimulus. Rapid interruption of chemical events was accomplished by simultaneously quick-freezing resting and stimulated muscles at the last pulse from stimulator. Dystrophic muscle, with approximately one-quarter the phosphorylase t activity exhibited by control muscles, showed a significant decline in enzyme activity with age (60–115 days) which was not paralleled in the control muscle. Short bouts of stimulation (1/2–1 sec) produced greater a: t increases in dystrophic mice; intermediate stimulation (3–8 sec) produced similar a: t increases in both groups; and after 15 sec the control muscles showed greater increases in a: t values. Control muscles activate the enzyme in a progressive manner with lengthening stimulation periods; dystrophic muscles show a fluctuating activation.

Defect in regulation of membrane transport of monosaccharides in dystrophic muscle

1979 ◽  
Vol 57 (7) ◽  
pp. 695-701 ◽  
Author(s):  
J. Elbrink
Keyword(s):  
Plasma Membranes ◽  
Sugar Transport ◽  
Normal Muscle ◽  
Dystrophic Muscle ◽  
Variable Effect ◽  
Cardiomyopathic Hamsters ◽  
Uncoupling Of Oxidative Phosphorylation ◽  
Dystrophic Mice ◽  
Normal Controls ◽  
Glucose Analogue

The penetration of a nonmetabolized glucose analogue, 3-O-methyl-D-glucose, across the plasma membranes of tissues from dystrophic mice and cardiomyopathic (dystrophic) hamsters has been compared with that of normal controls. Under basal conditions the penetration of test sugar was similar in lens and diaphragm of normal and dystrophic 129/ReJ mice. Stimulation of sugar transport by 2,4-dinitrophenol did occur in normal but not in dystrophic diaphragm. A submaximal concentration of insulin had a more variable effect in dystrophic than in normal muscle while a supramaximal concentration of the hormone increased the uptake of the glucose analogue to an equal extent in the two tissues. In the BIO 14.6 strain of cardiomyopathic hamsters, uncoupling of oxidative phosphorylation did not increase sugar transport in extensor digitorum longus muscles, while the normal effect was observed in dystrophic soleus and in both these muscles of the random bred controls. The absence of an effect by a condition simulating anoxia suggests that in dystrophy, certain muscles are unable to accelerate the entry of glucose when this is required.

PHARMACOLOGICAL REACTIVITY OF DYSTROPHIC MUSCLE

1966 ◽  
Vol 44 (2) ◽  
pp. 353-366 ◽  
Author(s):  
A. Beaulnes ◽  
P. Bois ◽  
R. Carle
Keyword(s):  
Neuromuscular Blocking ◽  
Dystrophic Muscle ◽  
Stimulant Effect ◽  
Xanthine Derivatives ◽  
Dystrophic Mouse ◽  
Normal Littermate ◽  
Blocking Activity ◽  
Increased Sensitivity ◽  
Dystrophic Mice ◽  
Cytotoxic Substance

The effects of curarizing drugs, anticholinesterases, and musculotropic substances were studied on the phrenic nerve – diaphragm preparation of the hereditarily dystrophic mouse and of the rat treated with N,N-dimethyl-p-phenylenediamine (PPD), a cytotoxic substance producing dystrophic-like lesions. Both species showed an increased resistance to the neuromuscular blocking activity of d-tubocurarine. Gallamine was also less potent in the dystrophic mouse than in its normal littermate. Both species showed an increased sensitivity to the initial stimulant effect of succinylcholine; on the other hand, the depressant effect of succinylcholine was less intense in PPD-treated rats but unaltered in the dystrophic mouse. The response to neostigmine and physostigmine was decreased in the PPD-treated rat but enhanced in the dystrophic mouse. Musculotropic drugs (chlorpromazine, tetrodotoxin, xanthine derivatives, and veratrine) produced similar effects in normal and dystrophic mice. Two hypotheses are suggested to explain these changes in sensitivity in the dystrophic mouse diaphragm: (a) an increased production of an acetylcholine-like material, and (b) an increase in the number of acetylcholine-sensitive sites on the cell membrane. The changes in drug reactivity of the PPD-treated rat are considered to be due to a functional denervation caused by the cytotoxic properties of PPD.

CREATINE KINASE IN NORMAL AND DYSTROPHIC MOUSE MUSCLE

1962 ◽  
Vol 40 (4) ◽  
pp. 443-447 ◽  
Author(s):  
C. Nichol ◽  
P. L. McGeer ◽  
J. R. Miller
Keyword(s):  
Creatine Kinase ◽  
Muscular Dystrophy ◽  
Kinase Activity ◽  
Creatine Kinase Activity ◽  
Mouse Muscle ◽  
Dystrophic Mouse ◽  
Leg Muscle ◽  
The Difference ◽  
Dystrophic Mice

The hind leg muscle of normal mice and mice with hereditary muscular dystrophy was taken for individual analyses of the creatine-phosphorylating enzyme, creatine kinase. Creatine kinase activity was always found to be higher in the muscle of normal mice than in that of dystrophic mice, and the values in each group decreased with increasing age of the mice. The difference was greatest in mice of 2 weeks of age, and in the light of these findings some suggestions are made about the pathogenesis of muscular dystrophy.

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.

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