Metabolic changes in the extracellular matrix during differentiation of myoblasts of the L6 line and of a Myo- non-fusing mutant.
In the present study we have characterized by biochemical and immunochemical methods the changes which take place in collagen, laminin and fibronectin biosynthesis during the differentiation of clonal skeletal myoblasts of the L6 line. Time-course experiments showed that the relative rate of synthesis of collagen increased significantly during the cell-cell contact step of myogenesis and decreased later on. The major collagens synthesized were types I and III, found mainly as soluble precursors in the culture medium. Types IV and V collagens were detected exclusively in the cell layer. The relative amounts of types I and III collagens remained unchanged during myogenesis, while types IV and V collagens increased as the cells of the L6 line fused. In a non-fusing alpha-amanitin-resistant mutant of the L6 line (Ama 102), the rate of collagen synthesis was largely depressed and its rate of degradation was increased as compared with the fusing wild type. The synthesis of laminin was very low in cells of the fusing wild type, but abundant and associated with the cell layer of the Myo- mutant. The appearance of a muscle-specific extracellular matrix is a complex process involving changes in the organization, the biosynthesis and remodelling of its macromolecules of the extracellular matrix.
D000818:Animals; D002454:Cell Differentiation; D002455:Cell Division; D002459:Cell Fusion; D002460:Cell Line; D003094:Collagen / Q000096:biosynthesis*; D005109:Extracellular Matrix / Q000378:metabolism*; D005353:Fibronectins / Q000096:biosynthesis*; D007700:Kinetics; D007797:Laminin / Q000096:biosynthesis*; D009132:Muscles / Q000166:cytology* / Q000378:metabolism; D009154:Mutation
D005353:Fibronectins; D007797:Laminin; D003094:Collagen