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Coordinate reciprocal trends in glycolytic and mitochondrial transcript accumulations during the in vitro differentiation of human myoblasts
Author(s) -
Webster Keith A.,
Gunning Peter,
Hardeman Edna,
Wallace Douglas C.,
Kedes Larry
Publication year - 1990
Publication title -
journal of cellular physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.529
H-Index - 174
eISSN - 1097-4652
pISSN - 0021-9541
DOI - 10.1002/jcp.1041420316
Subject(s) - myogenesis , biology , glycolysis , cytochrome c oxidase , biochemistry , microbiology and biotechnology , phosphoglycerate kinase , citrate synthase , pyruvate dehydrogenase kinase , pyruvate dehydrogenase complex , myocyte , mitochondrion , enzyme
Changes in the mRNA levels during mammalian myogenesis were compared for seven polypeptides of mitochondrial respiration (the mitochondrial DNA‐encoded cytochrome oxidase subunit III, ATP synthase subunit 6, NADH dehydrogenase subunits 1 and 2, and 16S ribosomal RNA; the nuclear encoded ATP synthase β subunit and the adenine nucleotide translocase) and three polypeptides of glycolysis (glyceraldehyde‐3‐phosphate dehydrogenase, pyruvate kinase, and triose‐phosphate isomerase). Progressive changes during the conversion from myoblasts to myotubes were monitored under both atmospheric oxygen (nor‐moxic) and hypoxic environments. Northern analyses revealed coordinate, biphasic, and reciprocal expression of the respiratory and glycolytic mRNAs during myogenesis. In normoxic cells the mitochondrial respiratory enzymes were highest in myoblasts, declined 3‐ to 5‐fold during commitment and exit from the cell cycle, and increased progressively as the myotubes matured. By contrast, the glycolytic enzyme mRNAs rose 3‐ to 6‐fold on commitment and then progressively declined. When partially differentiated myotubes were switched to hypoxic conditions, the glycolytic enzyme mRNAs increased and the respiratory mRNAs declined. Hence, the developmental regulation of muscle bioenergetic metabolism appears to be regulated at the pretranslational level and is modulated by oxygen tension.