Accelerated degradation of glycogen phosphorylase in denervated and dystrophic mouse skeletal muscle

1985 ◽  
Vol 5 (7) ◽  
pp. 567-572 ◽  
Author(s):  
P. Elaine Butler ◽  
E. Jane Cookson ◽  
Robert J. Beynon
Keyword(s):  
Skeletal Muscle ◽  
Glycogen Phosphorylase ◽  
Pyridoxal Phosphate ◽  
Mouse Skeletal Muscle ◽  
Accelerated Degradation ◽  
Dystrophic Mouse ◽  
Pathological Conditions ◽  
Good Index

Pyridoxal phosphate, the cofactor of glycogen phosphorylase, fulfils the criteria needed of a turnover label for this enzyme. The decay of protein-bound label following administration of [3H]pyridoxine is a good index of the rate of degradation of the enzyme in vivo. This method has been applied to the study of catabolism of the enzyme in normal, denervated and dystrophic mouse skeletal muscle. In both of the pathological conditions the enzyme is degraded more rapidly than normal.

scholarly journals Immunological detection of degradation intermediates of skeletal-muscle glycogen phosphorylase in vitro and in vivo

1992 ◽  
Vol 288 (1) ◽  
pp. 291-296 ◽  
Author(s):  
E J Cookson ◽  
A V Flannery ◽  
J A Cidlowski ◽  
R J Beynon
Keyword(s):  
Skeletal Muscle ◽  
High Speed ◽  
Glycogen Phosphorylase ◽  
Pyridoxal Phosphate ◽  
Polyclonal Antibodies ◽  
Supernatant Fraction ◽  
Immunological Methods ◽  
Degradation Intermediates

Over 95% of the pyridoxal phosphate (PLP) in skeletal is bound to one protein, glycogen phosphorylase. This, and the fact that phosphorylase constitutes approx. 5% of the soluble protein in skeletal muscle, introduce the possibility that PLP might be used as a specific label to identify degradation intermediates of the enzyme. In this investigation, we have developed immunological methods, using a monoclonal antibody to PLP and polyclonal antibodies to phosphorylase, to detect degradation intermediates in vitro and in vivo. We have identified a family of degradation intermediates of glycogen phosphorylase in the high-speed-supernatant fraction of mouse skeletal muscle. These peptides react with both types of antibodies and are in the size and concentration range expected for degradation intermediates in a model in which the committed step is followed by rapid clearance of the products. Changes in amounts of degradation intermediates are examined in physiological or pathological conditions in which the rate of degradation of phosphorylase is altered.

Purification of glycogen phosphorylase from small quantities of mouse skeletal muscle

1984 ◽  
Vol 141 (2) ◽  
pp. 494-498 ◽  
Author(s):  
P.Elaine Butler ◽  
Dorothy Fairhurst ◽  
Robert J. Beynon
Keyword(s):  
Skeletal Muscle ◽  
Glycogen Phosphorylase ◽  
Mouse Skeletal Muscle

MRI imaging for in vivo free radicals and bioenergetics in mouse skeletal muscle

2018 ◽  
Vol 128 ◽  
pp. S123
Author(s):  
Bumsoo Ahn ◽  
Nataliya Smith ◽  
Debra Saunders ◽  
Holly Van Remmen ◽  
Rheal Towner
Keyword(s):  
Skeletal Muscle ◽  
Free Radicals ◽  
Mri Imaging ◽  
Mouse Skeletal Muscle

scholarly journals 3H Leucine Incorporation Into Myofibrils of Normal and Dystrophic Mouse Skeletal Muscle

1975 ◽  
Vol 2 (1) ◽  
pp. 1-4 ◽  
Author(s):  
G. Monckton ◽  
H. Marusyk
Keyword(s):  
Skeletal Muscle ◽  
Muscular Dystrophy ◽  
Leucine Incorporation ◽  
Mouse Skeletal Muscle ◽  
Dystrophic Mouse ◽  
Before And After ◽  
Em Autoradiography ◽  
Marked Drop

SUMMARY:The study of 3H leucine incorporation into skeletal muscle of mouse muscular dystrophy (129 ReJ/dy Bar Harbour strain) shows the uptake of isotope into myofibrils. The techniques employed were light and EM autoradiography before and after glycerination (Szent-Gyorgyi 1947). The results indicate a marked drop in uptake of the 3H-Leucine into myofibrils in the dystrophic animals, supporting the contention of Nihei et al (1971) that reduced myosin synthesis occurs in mouse muscular dystrophy.

scholarly journals Myofiber Damage Precedes Macrophage Infiltration after in Vivo Injury in Dysferlin-Deficient A/J Mouse Skeletal Muscle

2015 ◽  
Vol 185 (6) ◽  
pp. 1686-1698 ◽  
Author(s):  
Joseph A. Roche ◽  
Mohan E. Tulapurkar ◽  
Amber L. Mueller ◽  
Nico van Rooijen ◽  
Jeffrey D. Hasday ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Macrophage Infiltration ◽  
Mouse Skeletal Muscle

scholarly journals Subproteomics analysis of Ca2+-binding proteins demonstrates decreased calsequestrin expression in dystrophic mouse skeletal muscle

2004 ◽  
Vol 271 (19) ◽  
pp. 3943-3952 ◽  
Author(s):  
Philip Doran ◽  
Paul Dowling ◽  
James Lohan ◽  
Karen McDonnell ◽  
Stephan Poetsch ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Binding Proteins ◽  
Mouse Skeletal Muscle ◽  
Dystrophic Mouse

Studies of the dynamics of skeletal muscle regeneration: the mouse came back!

1998 ◽  
Vol 76 (1) ◽  
pp. 13-26 ◽  
Author(s):  
Judy E Anderson
Keyword(s):  
Gene Expression ◽  
Skeletal Muscle ◽  
Magnetic Resonance ◽  
Magnetic Resonance Spectroscopy ◽  
Muscle Fiber ◽  
Muscle Regeneration ◽  
Skeletal Muscle Regeneration ◽  
Resonance Spectroscopy ◽  
Dystrophic Mouse

Regeneration of skeletal muscle tissue includes sequential processes of muscle cell proliferation and commitment, cell fusion, muscle fiber differentiation, and communication between cells of various tissues of origin. Central to the process is the myosatellite cell, a quiescent precursor cell located between the mature muscle fiber and its sheath of external lamina. To form new fibers in a muscle damaged by disease or direct injury, satellite cells must be activated, proliferate, and subsequently fuse into an elongated multinucleated cell. Current investigations in the field concern modulation of the effectiveness of skeletal muscle regeneration, the regeneration-specific role of myogenic regulatory gene expression distinct from expression during development, the impact of growth and scatter factors and their respective receptors in amplifying precursor numbers, and promoting fusion and maturation of new fibers and the ultimate clinical therapeutic applications of such information to alleviate disease. One approach to muscle regeneration integrates observations of muscle gene expression, proliferation, myoblast fusion, and fiber growth in vivo with parallel studies of cell cycling behaviour, endocrine perturbation, and potential biochemical markers of steps in the disease-repair process detected by magnetic resonance spectroscopy techniques. Experiments on muscles from limb, diaphragm, and heart of the mdx dystrophic mouse, made to parallel clinical trials on human Duchenne muscular dystrophy, help to elucidate mechanisms underlying the positive treatment effects of the glucocorticoid drug deflazacort. This review illustrates an effective combination of in vivo and in vitro experiments to integrate the distinctive complexities of post-natal myogenesis in regeneration of skeletal muscle tissue.Key words: satellite cell, cell cycling, HGF/SF, c-met receptor, MyoD, myogenin, magnetic resonance spectroscopy, mdx dystrophic mouse, deflazacort.

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