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Ultrastructural distribution of the M form of creatine phosphokinase in human muscle by immunogold labeling
Author(s) -
Dankert John R.,
Papadi George P.,
Shields Robert P.
Publication year - 1992
Publication title -
microscopy research and technique
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.536
H-Index - 118
eISSN - 1097-0029
pISSN - 1059-910X
DOI - 10.1002/jemt.1070200308
Subject(s) - sarcomere , creatine kinase , immunogold labelling , creatine , biology , ultrastructure , isozyme , biochemistry , cytoplasm , microbiology and biotechnology , myocyte , enzyme , anatomy
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.