scholarly journals Skeletal-muscle sarcolemma from normal and dystrophic mice. Isolation, characterization and lipid composition

1977 ◽  
Vol 168 (2) ◽  
pp. 229-237 ◽  
Author(s):  
T A de Kretser ◽  
B G Livett
Keyword(s):  
Skeletal Muscle ◽  
Muscular Dystrophy ◽  
Neutral Lipid ◽  
Lipid Composition ◽  
Free Cholesterol ◽  
Total Lipid Content ◽  
Dystrophic Muscle ◽  
Mouse Muscle ◽  
Membrane Function ◽  
Dystrophic Mice

1. Mouse skeletal-muscle sarcolemma was isolated, and the preparations obtained from normal mouse muscle and from muscle of mice with hereditary muscular dystrophy were characterized with respect to appearance under the optical and electron microscopes, distribution of marker enzymes, histochemical properties and biochemical composition. 2. The sarcolemmal membranes from normal and dystrophic muscle were subjected to detailed lipied analysis. Total lipid content was shown to increase in sarcolemma from dystrophic mice as a result of a large increase in neutral lipid and a smaller increase in total phospholipids. Further analysis of the neutral-lipid fraction showed that total acylglycerols increased 6-fold, non-esterified fatty acid 4-fold and cholesterol esters 2-fold, whereas the amount of free cholesterol remained unchanged in sarcolemma from dystrophic muscle. Significant increases were found in lysophosphatidylcholine, phosphatidylcholine and phosphatidylethanolamine in dystrophic-muscle sarcolemma; however, the relative composition of the phospholipid fraction remained essentially the same as in the normal case. 3. The overall result of alterations in lipid composition of the sarcolemma in mouse muscular dystrophy was an increase in neutral lipid compared with total phospholipid, and a 4-fold decrease in the relative amount of free cholesterol in the membrane. The possible impact of these changes on membrane function is discussed.

Biochemical Changes in Progressive Muscular Dystrophy. IX. Synthesis of Native Myosin, Actin, and Tropomyosin in the Skeletal Muscle of Mouse as a Function of Muscular Dystrophy

1972 ◽  
Vol 50 (4) ◽  
pp. 409-415 ◽  
Author(s):  
Uma Srivastava
Keyword(s):  
Skeletal Muscle ◽  
Muscular Dystrophy ◽  
Protein Purification ◽  
Gel Electrophoresis ◽  
Dystrophic Muscle ◽  
Mouse Muscle ◽  
Progressive Muscular Dystrophy ◽  
Dystrophic Mice

The synthesis of native myosin, actin, and tropomyosin in the skeletal muscle of normal and hereditary dystrophic mice was studied with the help of direct counting as well as acrylamide-gel electrophoresis and protein purification procedures.Labelling of the nascent protein indicated that heavier polysomes from the normal muscle were able to incorporate more radioactivity into the protein than the heavier polysomes from the dystrophic muscles. Contrary to this, lighter polysomes in the dystrophic muscle demonstrated higher incorporation as compared to the normal.Results of in vivo and in vitro incorporation as well as those of acrylamide-gel electrophoresis and protein purification procedures indicated that synthesis of myosin decreased in the dystrophic muscle. The synthesis of actin did not show a significant change either in normal or dystrophic muscle, whereas that of tropomyosin increased sharply in the dystrophic mouse muscle.

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.

Biochemical changes in progressive muscular dystrophy. XI. Cyclic nucleotides in the skeletal and cardiac muscle of normal and dystrophic mice

1981 ◽  
Vol 59 (4) ◽  
pp. 329-334 ◽  
Author(s):  
Uma Srivastava ◽  
Mikael Sebag ◽  
Manohar Thakur
Keyword(s):  
Skeletal Muscle ◽  
Muscular Dystrophy ◽  
Cardiac Muscle ◽  
Cyclic Nucleotides ◽  
Dystrophic Muscle ◽  
Camp Content ◽  
Progressive Muscular Dystrophy ◽  
Camp And Cgmp ◽  
Dystrophic Mice ◽  
Murine Dystrophy

cAMP and cGMP contents were determined in the skeletal and cardiac muscle of normal and dystrophic mice. cAMP content increased in the dystrophic muscle at every stage of the disease whereas cGMP content decreased in the preliminary stages and increased at the terminal stage of the disease. The content of both nucleotides per heart was not affected in murine dystrophy. Thus, levels of cyclic nucleotides appear to be selectively altered in dystrophic skeletal muscle.

Biochemical changes in progressive muscular dystrophy. XIV. Skeletal muscle myosin mRNA translatability in dystrophic mice

1987 ◽  
Vol 65 (9) ◽  
pp. 833-841 ◽  
Author(s):  
U. S. Srivastava ◽  
E. A. Sugden ◽  
P. K. Majumdar ◽  
M. L. Thakur ◽  
G. M. Bhatnagar
Keyword(s):  
Skeletal Muscle ◽  
Muscular Dystrophy ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Cdna Probe ◽  
Sodium Dodecyl ◽  
Mouse Muscle ◽  
Skeletal Muscle Myosin ◽  
Dystrophic Mouse ◽  
Dystrophic Mice

Variations in the content and translatability of the poly(A)+ RNA and mRNA molecules coding for myosin (M) were studied in the hind leg muscles of genetically dystrophic mice. The poly(A)+ RNA content of total skeletal muscle failed to increase normally during progression of the disease. M mRNA, isolated from dystrophic murine muscle poly(A)+ RNA, was mostly found to be associated with the 26S RNA species. The translation of M mRNA in an in vitro heterologous wheat germ system was lower at 8 and 16 weeks in the dystrophic group as compared with the controls. Analysis of the translation products via sodium dodecyl sulfate – polyacrylamide gel electrophoresis, autoradiography, and densitometric autoradiographic tracing demonstrated the gradual disappearance of a protein band corresponding to M, the major component of skeletal muscle. cDNA was synthesized, using M mRNA that was isolated and purified from normal and dystrophic mouse muscle as a template. Total radioactivity was measured in some cDNA fractions produced from normal and dystrophic mouse muscle, while other fractions were utilized for separation and sizing of cDNA by disc gel electrophoresis. The cDNA from normal muscle was hybridized with M mRNA from normal and 16-week-old dystrophic mouse muscles. The cDNA probe, hybridization experiments, and studies involving the content and synthesis of M mRNA suggest that murine muscular dystrophy elicited a shorter species of mRNA or shorter sequences of the same species of mRNA coding for M. Not all poly(A)+ mRNA sequences coding for M, found in control mice, were present in their dystrophic counterparts. In conclusion, it appears that murine muscular dystrophy produces a shorter species of pre-M mRNA via decreased polynucleotide elongation.

scholarly journals Drastic reduction of calsequestrin-like proteins and impaired calcium binding in dystrophic mdx muscle

2002 ◽  
Vol 92 (2) ◽  
pp. 435-445 ◽  
Author(s):  
Kevin Culligan ◽  
Niamh Banville ◽  
Paul Dowling ◽  
Kay Ohlendieck
Keyword(s):  
Skeletal Muscle ◽  
Sarcoplasmic Reticulum ◽  
Muscular Dystrophy ◽  
Calcium Binding ◽  
Functional Decline ◽  
Two Dimensional ◽  
Drastic Reduction ◽  
Dystrophic Muscle ◽  
One Dimensional ◽  
Blotting Technique

Although the reduction in dystrophin-associated glycoproteins is the primary pathophysiological consequence of the deficiency in dystrophin, little is known about the secondary abnormalities leading to x-linked muscular dystrophy. As abnormal Ca2+ handling may be involved in myonecrosis, we investigated the fate of key Ca2+ regulatory membrane proteins in dystrophic mdx skeletal muscle membranes. Whereas the expression of the ryanodine receptor, the dihydropyridine receptor, the Ca2+-ATPase, and calsequestrin was not affected, a drastic decline in calsequestrin-like proteins of 150–220 kDa was observed in dystrophic microsomes using one-dimensional immunoblotting, two-dimensional immunoblotting with isoelectric focusing, diagonal two-dimensional blotting technique, and immunoprecipitation. In analogy, overall Ca2+ binding was reduced in the sarcoplasmic reticulum of dystrophic muscle. The reduction in Ca2+ binding proteins might be directly involved in triggering impaired Ca2+ sequestration within the lumen of the sarcoplasmic reticulum. Thus disturbed sarcolemmal Ca2+ fluxes seem to influence overall Ca2+homeostasis, resulting in distinct changes in the expression profile of a subset of Ca2+ handling proteins, which might be an important factor in the progressive functional decline of dystrophic muscle fibers.

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.

Concentrations of K and Na in Skeletal Muscle of Mice With a Hereditary Myopathy (Dystrophia Muscularis)

1958 ◽  
Vol 193 (3) ◽  
pp. 530-533 ◽  
Author(s):  
Nome Baker ◽  
William H. Blahd ◽  
P. Hart
Keyword(s):  
Skeletal Muscle ◽  
Vitamin E ◽  
Muscular Dystrophy ◽  
Extracellular Space ◽  
Partial Replacement ◽  
Vitamin E Deficiency ◽  
Normal Value ◽  
Hereditary Myopathy ◽  
The Mean ◽  
Dystrophic Mice

Exchangeable body potassium (Ke), muscle potassium and muscle sodium concentrations have been measured in hereditarily dystrophic mice and in their normal littermates. Both Ke and K39/gm muscle were depressed in the dystrophics approximately 20% below the mean normal value; however, the concentration of Na23/gm muscle was higher by 50%, on the average, in the dystrophic tissue. The data suggest a partial replacement of intracellular by extracellular space in the dystrophic mice. Thus, this form of hereditary muscular dystrophy is qualitatively similar, with regard to K and Na concentrations, to human muscular dystrophy, vitamin E deficiency in rabbits, nutritional dystrophy in calves, and denervation in puppies.

Biochemical changes in progressive muscular dystrophy. XIII. Nucleic acids, proteins, and total nucleotides in the thymus and spleen of dystrophic mice

1985 ◽  
Vol 63 (5) ◽  
pp. 325-332 ◽  
Author(s):  
Uma Srivastava ◽  
Mikael Sebag ◽  
Manohar Thakur
Keyword(s):  
Skeletal Muscle ◽  
Amino Acid ◽  
Muscular Dystrophy ◽  
Free Amino Acid ◽  
Free Amino ◽  
Specific Activity ◽  
Cellular Growth ◽  
Free Amino Acid Pool ◽  
Acid Pool ◽  
Dystrophic Mice

Assessments were made of the thymus and spleen weights and the total nucleotide, nucleic acid, and protein content as well as the incorporation of [14C]leucine into protein and of [3H]orotate into RNA, in the thymus, spleen, liver, brain, kidney, lungs, heart, pancreas, and skeletal muscle of normal (+/+) and dystrophic (dy/dy) 129 ReJ mice aged 40, 60, or 90 days. The weights of the thymus and spleen were lower at all stages of dystrophy. Total nucleotide and RNA levels per thymus were reduced at 90 days, while total DNA content was decreased at 60 and 90 days. Protein concentrations per thymus were diminished at each stage of the disease. The specific activity of the free amino acid pool and total free nucleotide pool did not show any significant variations in the thymus at any phase of dystrophy. Incorporation of [14C]leucine into protein and of [3H]orotate into RNA was considerably lower in the thymus at each stage of the disease. Total nucleotide content per spleen was decreased at 40 days, with no change at 60 days and followed by an increase at 90 days in the dystrophic mice. DNA, RNA, and protein levels were all reduced in the spleen at each stage of the disease. The specific activity of the free amino acid pool and total free nucleotide pool, as well as the incorporation of [14C]leucine into protein and of [3H]orotate into RNA, showed similar changes in the spleen as noted in the thymus at each phase of dystrophy. These observations indicate that significant alterations in cellular growth occur not only in skeletal muscle and other nonlymphoid organs, but also in the lymphoid organs of dystrophic mice. Such changes in the cellular growth of lymphoid organs could be responsible for an impairment of immunologic responses reflecting thymic atrophy in murine muscular dystrophy.

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.

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