Uncoupling of muscle-specific protein expression in myocyte x myoblast heterokaryons.
The inducibility of several rat skeletal muscle proteins was examined in heterokaryons formed by fusing differentiated chick myocytes to undifferentiated rat myoblasts. Chicken and rat proteins were distinguished using species-specific antibodies or by their different migrations in polyacrylamide or agarose gels. Both rat skeletal myosin light chain 1 and rat alpha-tropomyosin were induced in the heterokaryons. In contrast, neither rat acetylcholine receptors nor creatine kinase could be detected. These results suggest that chick myocytes may contain quantities of regulatory factors that are sufficient for the activation of some but not all of these rat muscle-specific proteins within the cellular context of the heterokaryon.
Wright
W E
WE
University of Texas Southwestern Medical Center, Dallas 75235.
Lin
V K
VK
D000818:Animals; D002460:Cell Line; D002467:Cell Nucleus / Q000648:ultrastructure; D002642:Chick Embryo; D003402:Creatine Kinase / Q000378:metabolism; D015870:Gene Expression; D006822:Hybrid Cells / Q000166:cytology / Q000378:metabolism / Q000648:ultrastructure*; D009124:Muscle Proteins / Q000235:genetics* / Q000276:immunology / Q000378:metabolism; D009132:Muscles / Q000166:cytology / Q000196:embryology / Q000648:ultrastructure; D051381:Rats; D011950:Receptors, Cholinergic / Q000378:metabolism; D013045:Species Specificity; D014335:Tropomyosin / Q000378:metabolism
D009124:Muscle Proteins; D011950:Receptors, Cholinergic; D014335:Tropomyosin; D003402:Creatine Kinase