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.

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.

Palmitic acid-1-14C oxidation by skeletal muscle mitochondria of dystrophic mice

1970 ◽  
Vol 48 (5) ◽  
pp. 566-572 ◽  
Author(s):  
C. H. Lin ◽  
A. J. Hudson ◽  
K. P. Strickland
Keyword(s):  
Skeletal Muscle ◽  
Palmitic Acid ◽  
Krebs Cycle ◽  
Supernatant Fraction ◽  
Dystrophic Muscle ◽  
Muscle Mitochondria ◽  
Normal Littermate ◽  
Skeletal Muscle Mitochondria ◽  
Dystrophic Mice ◽  
Muscle Homogenate

Cofactor requirements for the oxidation of palmitate-1-14C by 600 × g supernatant fraction of mouse skeletal muscle homogenate and by skeletal muscle mitochondria are described. Optimal oxidation of palmitate-1-14C by skeletal muscle mitochondria requires the presence of carnitine, ATP, CoA, and a Krebs cycle intermediate (e.g. succinate). Succinate, malate, alpha-ketoglutarate, and oxaloacetate are all equally effective in supporting the oxidation, but isocitrate is less effective. The oxidation of palmitate-1-14C by 600 × g supernatant fraction of muscle homogenate as well as by skeletal muscle mitochondria from dystrophic mice is significantly decreased compared with that of the normal littermate controls. The present results, together with the previous findings, suggest that the decrease in oxidation of palmitate-1-14C by the dystrophic muscle preparations is most likely due to a defect in one or more of the steps of the Krebs cycle.

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.

Non-depolarizing Neuromuscular Blocking Activity of Bisquaternary Amino Di- and Tripeptide Derivatives

2000 ◽  
Vol 43 (25) ◽  
pp. 4822-4833 ◽  
Author(s):  
Leo H. D. J. Booij ◽  
Leon A. G. M. van der Broek ◽  
Wilson Caulfield ◽  
Brigitte M. G. Dommerholt-Caris ◽  
John K. Clark ◽  
...  
Keyword(s):  
Neuromuscular Blocking ◽  
Blocking Activity

Influence of diet on transamidinase activity in dystrophic mice

1960 ◽  
Vol 199 (5) ◽  
pp. 927-930 ◽  
Author(s):  
D. L. Coleman ◽  
M. E. Ashworth
Keyword(s):  
Dystrophic Mouse ◽  
Dystrophic Mice

The activities of the enzymes involved in creatine synthesis were studied in normal and dystrophic mice maintained on two commercial mouse chows. Kidney transamidinase activity in the dystrophic mouse was found to vary from 150 to –50% of the normal depending on the diet fed while the activity of the enzyme in the control mice remained unaltered. Addition of protein or glycine to the diet normally causing the lower transamidinase values resulted in increased enzyme levels equal to those found in animals maintained on the diet normally producing the higher enzyme levels.

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