Altered synthesis of myosin light chains is associated with contractility in cultures of differentiating chick embryo breast muscle.
Cultured chick embryo skeletal muscle cells normally synthesize only the embryonic isoform of mysoin. We have found that aneural muscle cultures that become or are provoked into an extremely contractile state will begin to synthesize a pattern of myosin light chains typical of maturing muscle. Immunoblots with neonatal and adult specific monoclonal antibodies did not reveal a corresponding isozyme transition in myosin heavy chain. These results demonstrate a correlation between contractility and the regulation of myosin light chain maturation, and also suggest that the transitions of heavy and light chain synthesis during development do not appear to be under close coordinate regulation.
D000818:Animals; D002454:Cell Differentiation; D002642:Chick Embryo; D004591:Electrophoresis, Polyacrylamide Gel; D005470:Fluorometry; D007163:Immunosorbent Techniques; D009119:Muscle Contraction; D009132:Muscles / Q000166:cytology / Q000196:embryology*; D009218:Myosins / Q000096:biosynthesis*; D009924:Organ Culture Techniques
D009218:Myosins