Iron supports myogenic cell differentiation to the same degree as does iron-bound transferrin.
T. Hasegawa, K. Saito, I. Kimura, and E. Ozawa (1981, Proc. Jopan Acad. B 57, 206-210) have shown that Fe ion can promote myogenic cell growth as Fe-bound transferrin. In the present work, the effects of these substances in supporting myogenic cell differentiation were examined. The hallmarks of differentiation adopted were appearance of structural and regulatory proteins, myofibrils, sarcoplasmic reticulum, and Ca-activated activities of myosin B and phosphorylase kinase; isoform transition of creatine kinase; and acquisition of cell membrane excitability and contractility following electrical stimulation of myotubes. The degree of differentiation of myotubes cultured in the presence of Fe ion was almost the same as that of myotubes cultured in the presence of Fe-bound transferrin. These facts suggest that transferrin protein molecules do not play a primary role in differentiation. Further, it has also been shown that myotubes acquire excitation-contraction and metabolism coupling qualitatively similar to that of adult muscle fiber.
D000200:Action Potentials; D000818:Animals; D002118:Calcium / Q000494:pharmacology; D002454:Cell Differentiation / Q000187:drug effects; D002462:Cell Membrane / Q000502:physiology; D002478:Cells, Cultured; D002642:Chick Embryo; D003402:Creatine Kinase / Q000378:metabolism; D007501:Iron / Q000378:metabolism / Q000494:pharmacology*; D009119:Muscle Contraction; D009132:Muscles / Q000166:cytology / Q000196:embryology* / Q000502:physiology; D009210:Myofibrils / Q000648:ultrastructure; D009218:Myosins / Q000378:metabolism; D010764:Phosphorylase Kinase / Q000378:metabolism; D012519:Sarcoplasmic Reticulum; D014168:Transferrin / Q000378:metabolism / Q000494:pharmacology*
D014168:Transferrin; D007501:Iron; D010764:Phosphorylase Kinase; D003402:Creatine Kinase; D009218:Myosins; D002118:Calcium