Creatine kinase, myokinase, and acetylcholinesterase activities in muscle-forming primary cultures of mouse teratocarcinoma cells.
Multipotential mouse teratocarcinoma cells in embryoid bodies were explanted on plastic or collagen substrates. Various modes of cell determination, including myogenesis, occurred. The predominant avenue of differentiation soon became myogenesis: many multinucleated myotubes formed and yielded an extensive network of skeletal muscle fibers. The process does not proceed to normal completion, as the fibers have a paucity of striations and are not contractile. Activities of several enzymes ordinarily associated with muscle differentiation were examined. Acetylcholinesterase activity increases, especially during myotube formation, as in normal myogenesis. However, creatine kinase activity rises during myotube formation and then drops abnormally, and myokinase activity fails to increase appreciably. The fetal isozymic form of creatine kinase is expressed in the cultures, although well differentiated solid tumors taken from mice show attainment of the adult muscle isozyme type if skeletal muscle is demonstrably present. The results are consistent with the interpretation that coordinately regulated changes in gene expressions controlling these functions may be required for later stages of myogenesis.
D000110:Acetylcholinesterase / Q000378:metabolism*; D000263:Adenylate Kinase / Q000378:metabolism*; D000818:Animals; D002091:Butyrylcholinesterase / Q000378:metabolism; D002454:Cell Differentiation; D002478:Cells, Cultured; D003402:Creatine Kinase / Q000378:metabolism*; D007527:Isoenzymes / Q000378:metabolism; D051379:Mice; D009132:Muscles / Q000196:embryology; D010770:Phosphotransferases / Q000378:metabolism*; D013724:Teratoma / Q000201:enzymology*
D007527:Isoenzymes; D010770:Phosphotransferases; D003402:Creatine Kinase; D000263:Adenylate Kinase; D000110:Acetylcholinesterase; D002091:Butyrylcholinesterase