Premium
Cytochrome C Oxidase—deficient myogenic cell lines in mitochondrial myopathy
Author(s) -
Shimoizumi Hideo,
Momoi Mariko Yoshida,
Ohta Shigeo,
Kagawam Yasuo,
Momoi Takashi,
Yanagisawa Masayoshi
Publication year - 1989
Publication title -
annals of neurology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 4.764
H-Index - 296
eISSN - 1531-8249
pISSN - 0364-5134
DOI - 10.1002/ana.410250614
Subject(s) - cytochrome c oxidase , mitochondrial myopathy , mitochondrial dna , biology , microbiology and biotechnology , mitochondrion , oxidase test , myopathy , electron transport complex iv , cytochrome c , cytochrome , biochemistry , cytochrome b , protein subunit , cell culture , enzyme , gene , genetics
In a patient with mitochondrial myopathy, the defect of cytochromeϵ oxidase activity was restricted to some muscle fibers. To isolate cell lines with or without oxidase activity from a single muscle sample, primary cultured cells were transformed by replication origin–defective simian virus 40, and then cloned. The clones were examined by cytochemical staining for cytochrome ϵ oxidase activity. Eight myogenic clones were completely devoid of activity, while the other myogenic and nonmyogenic clones were not. Deficiency of cytochrome ϵ oxidase was stable in culture for at least a year after serial passaging. The amount of mitochondrial DNA in cytochrome ϵ oxidase—deficient cells was the same as in control cells, and no deletion in the mitochondrial DNA was detected. Protein synthesis in mitochondria of the subunits of cytochrome ϵ oxidase and subunit 6 of the ATP synthase complex was markedly decreased, whereas synthesis of the other subunits encoded by mitochondrial DNA was normal. These cloned cell lines provide an excellent system for clarifying the cause of mitochondrial myopathy and for investigating nuclear‐mitochondrial genetic interaction.