Developmental progression of myosin gene expression in cultured muscle cells.
Myosin heavy chains are encoded by distinct members of a multigene family at different stages of muscle development. Study of the underlying regulatory mechanisms has been hindered because transitions in myosin expression have not been readily attained in tissue culture. Here we show a transition from early (fetal) to late (perinatal/adult) myosins defined by two monoclonal antibodies, F1.652 and N3.36, in the myotubes of mouse C2C12 cells. On day 1 of differentiation, essentially all myosin was early myosin. By day 8, early myosin dropped to 25% of its day 1 value and was replaced by late myosin. The transition occurred without neural contact, connective tissue components, or complex substrates, suggesting that its regulation may be intrinsic to the muscle cell. Our results demonstrate that a developmental progression in myosin gene expression, which occurs rapidly, with high frequency, and under relatively simple conditions, is now amenable to molecular analysis in cultured muscle cells.
D000818:Animals; D000911:Antibodies, Monoclonal; D002454:Cell Differentiation / Q000187:drug effects; D002478:Cells, Cultured; D003561:Cytarabine / Q000494:pharmacology; D005455:Fluorescent Antibody Technique; D005786:Gene Expression Regulation / Q000187:drug effects; D007163:Immunosorbent Techniques; D007527:Isoenzymes / Q000235:genetics / Q000276:immunology; D051379:Mice; D009132:Muscles / Q000166:cytology / Q000502:physiology*; D009218:Myosins / Q000235:genetics* / Q000276:immunology
D000911:Antibodies, Monoclonal; D007527:Isoenzymes; D003561:Cytarabine; D009218:Myosins