One- and two-dimensional gel electrophoretic analysis of proteins and phosphoproteins synthesised by clonal muscle cells during myogenesis.
Profiles of protein and phosphoprotein synthesis during the myogenic differentiation of clonal G8-1 skeletal muscle cells have been prepared using one and two-dimensional polyacrylamide gel electrophoretic methods. Analysis of these profiles shows the majority of proteins and phosphoproteins to be invariant. Those changes in protein and phosphoprotein synthesis seen, may be placed in three categories: (a) proteins increasing during myogenesis, (b) proteins decreasing during myogenesis and (c) stage specific proteins which appear exclusively in myoblasts or myotubes. Not all of the changes in protein and phosphoprotein synthesis during myogenesis could be correlated in one and two dimensional polyacrylamide gel electrophoresis, but the major changes can be summarised as follows. The most significant increases in protein synthesis were in components of molecular weight, 190 K (myosin), 56 K and 39.5 K (tropomyosin). ? actin (45 K) was shown to decrease in amount as were components of 58 K, 38 K and 30 K. Myoblast specific components were of 60 K, 50.5 K, 27.5 K and 23 K. Those proteins which first appeared during or after myoblast fusion were of 90 K, 66 K, 65.5 K, 59 K, 39.5 K, 25 K, 24 K, 23.5 K and 22 K. Phosphoproteins of 33 K, 43 K and 44 K were seen to increase strikingly during myogenesis. Myoblast specific phosphoproteins were of 120 K, 48 K and 45 K. Myotube specific phosphoproteins were of 180 K, 60 K, 47 K and 35 K.
Moore
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Muscular Dystrophy Research Laboratories, Institute of Neurology, The National Hospital, Queen Square, London WC1N 3BG, U.K.
Phillips
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Walsh
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