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Creatine kinase activity in normal and duchenne muscular dystrophy fibroblasts
Author(s) -
Davis Michael H.,
Cappel Roseann,
Vester John W.,
Samaha Frederick J.,
Gruenstein Eric
Publication year - 1982
Publication title -
muscle and nerve
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.025
H-Index - 145
eISSN - 1097-4598
pISSN - 0148-639X
DOI - 10.1002/mus.880050102
Subject(s) - isozyme , duchenne muscular dystrophy , creatine kinase , fibroblast , muscular dystrophy , endocrinology , medicine , biology , microbiology and biotechnology , chemistry , enzyme , cell culture , biochemistry , genetics
Abstract Cultured human skin fibroblasts from 9 patients with Duchenne muscular dystrophy (DMD) and 8 normal age‐ and sex‐matched controls were examined for creatine kinase (CK) activity. Both the normal and the DMD fibroblasts were found to have significant levels of CK activity (approximately 10 × 10 −3 IU per milligram of fibroblast protein). The control cells had slightly higher CK activity than the DMD lines, but this difference was not significant (0.2 < P < 0.1). The MM (muscle) isozyme, the BB (brain) isozyme, and the MB (hybrid) isozyme of CK were found to be present in fibroblasts. The isozymes were separated by electrophoresis and the relative amount of each was determined for both normal and DMD cells. In normal fibroblasts, approximately 48% of the total CK activity was of the MM type, 40% was of the BB type, and 12% was of the MB type with no significant differences apparent between normal and DMD groups. The presence in human fibroblasts of significant levels of CK activity with a characteristic isozyme profile is an important consideration for studies of this “marker” enzyme in the pseudohypertrophic muscle of DMD.