Myofibrillar creatine kinase in Duchenne and avian muscular dystrophy

Feit, Howard; Fuseler, John W.; Cook, Jay D.

doi:10.1016/0006-2944(83)90070-4

Cited by 5 publications

(1 citation statement)

References 16 publications

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“…The intracellular distribution of the M-CPK has not been studied as extensively in muscle from humans as in other species. M-CPK has been visualized, however, along the M-line of human muscle using fluorescence microscopy (Feit et al, 1983). In this present work, fixed human muscle and immuno-gold staining techniques were used to provide electron microscopic evidence of the uniquely high concentration of M-CPK at the M-line.…”

Section: Resultsmentioning

confidence: 95%

Ultrastructural distribution of the M form of creatine phosphokinase in human muscle by immunogold labeling

Dankert

Papadi

Shields

1992

Microscopy Res & Technique

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Creatine phosphokinase regenerates ATP from ADP using creatine phosphate. Isoenzymes of creatine phosphokinase are bound to certain cellular structures or are compartmentalized in areas of the cell, and this has been used as a basis for defining the role of these isoenzymes in energy metabolism. The M isoenzyme of creatine phosphokinase has been morphologically associated with the M-line of striated muscle in many species. In this present study the ultrastructural distribution and the relative concentration of the M form of creatine phosphokinase in human muscle tissue was determined using immunogold and electron microscopy. The M-line of the sarcomere, comprising only 3-4% of the sarcomere area, was found to contain over 20% of the total M isoenzyme signal of the entire sarcomere. This technique represents a quantitative, ultrastructural method to study the subcellular distribution of this isoenzyme. These data suggest that localized concentrations of M-CPK may be important for normal energy metabolism, and may also serve as a foundation for a better understanding of the relationship between abnormal creatine metabolism and the pathogenesis of neuromuscular disease.

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Section: Resultsmentioning

confidence: 95%

Ultrastructural distribution of the M form of creatine phosphokinase in human muscle by immunogold labeling

Dankert

Papadi

Shields

1992

Microscopy Res & Technique

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³¹P‐NMR studies of normal and dystrophic chicken muscle

1984

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Phosphorus-31 nuclear magnetic resonance (31P-NMR) analysis was performed on normal (line 412) and dystrophic (line 413) superficial pectoralis muscles excised from chickens between 15 and 116 days after hatching. An apparent alteration in dystrophic muscle energy metabolism was abolished by pretreatment with curare and was attributed to muscle hyperexcitability. Time-dependent 31P-NMR studies demonstrated no apparent difference in the overall tissue adenosine triphosphatase (ATPase) activity of dystrophic as compared to normal muscle. After 55 days of age, a resonance signal attributed to serine ethanolamine phosphodiester (SEPDE) was observed only in dystrophic muscle. Adding the paramagnetic cation Mn2+ to the buffer surrounding the muscle resulted in an approximate 80% decrement in the dystrophic SEPDE signal without apparent alteration of the other phosphatic signals in either the normal or dystrophic muscle. This would argue against any generalized membrane defect in dystrophic chicken muscle and suggest that SEPDE is in a compartment accessible to Mn2+.

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In situ study of myofibrils, mitochondria and bound creatine kinases in experimental cardiomyopathies

Veksler

Ventura‐Clapier

1994

Cellular Bioenergetics: Role of Coupled Creatine Kinases

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Human cardiomyopathy has been extensively studied in the last decade, and knowledge of the functional and structural alterations of the heart has grown. However, understanding of the pathogenesis has come mostly from experimental studies. A number of work have been designed to elucidate if alterations of the contractile apparatus of cardiac cells contribute to the impairment of heart mechanics in cardiomyopathies. As well, an important question is to be solved: whether energy supply of the contraction-relaxation cycle is sufficient in the myopathic heart. Use of cardiac fibers skinned by different techniques allows to evaluate functional ability of myofibrils, mitochondria and bound creatine kinase which plays an important role in cardiomyocyte energy metabolism. The data presented in this chapter show that experimental cardiomyopathies of various types have some common features. These are an increase in calcium sensitivity of myofibrils and a depression of functional activity of mitochondrial creatine kinase. Possible mechanisms and physiological significance of these changes are discussed. (Mol Cell Biochem 133/134: 287-298, 1994)

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Myofibrillar creatine kinase in Duchenne and avian muscular dystrophy

Cited by 5 publications

References 16 publications

Ultrastructural distribution of the M form of creatine phosphokinase in human muscle by immunogold labeling

Ultrastructural distribution of the M form of creatine phosphokinase in human muscle by immunogold labeling

³¹P‐NMR studies of normal and dystrophic chicken muscle

In situ study of myofibrils, mitochondria and bound creatine kinases in experimental cardiomyopathies

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Myofibrillar creatine kinase in Duchenne and avian muscular dystrophy

Cited by 5 publications

References 16 publications

Ultrastructural distribution of the M form of creatine phosphokinase in human muscle by immunogold labeling

Ultrastructural distribution of the M form of creatine phosphokinase in human muscle by immunogold labeling

31P‐NMR studies of normal and dystrophic chicken muscle

In situ study of myofibrils, mitochondria and bound creatine kinases in experimental cardiomyopathies

Contact Info

Product

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About

³¹P‐NMR studies of normal and dystrophic chicken muscle