Specific changes in cellular glycoproteins and surface proteins during myogenesis in clonal muscle cells

Walsh, Frank S.; Phillips, Elsa

doi:10.1016/0012-1606(81)90286-4

Cited by 59 publications

(23 citation statements)

References 19 publications

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“…Compton and Konigsberg, however, found that arrest of myoblasts at Gl was not alone sufficient to activate their differentiative program (4). Changes of some proteins in the cell surface have been implicated in events before myoblast fusion (2, 3, 15,20,22). Moreover, there are reports of changes in the distributions of various antigens during fusion (9, ll, 21).…”

Section: Discussionmentioning

confidence: 99%

Differentiation of Quail Myoblasts Transformed with a Temperature Sensitive Mutant of Rous Sarcoma Virus. II. Relationship of Myoblast Fusion with Calcium and Temperature

Kim

Adachi

Saiuchi

et al. 1992

Cell Struct. Funct.

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ABSTRACT. The effects of calcium and temperature on fusion of quail embryonicmyoblasts were examined using cells transformed with a temperature-sensitive mutant of Rous sarcoma virus (ts-RSV). The transformed quail myoblasts (QM-RSV)fused to form myotubes at 41°C, the non-permissive temperature, but not at 35.5°C, the permissive temperature. On incubation at 41°C, a period of more than 10 hr was needed for the myoblasts to become fusion-competent, but calcium was not needed for development of fusion-competence.Once the cells had become competent, fusion proceeded even at 35.5°C. These results suggest that the src gene product expressed at 35.5°C may control the fusion of cells in the competent stage by inactivating a components) that is associated with fusion-competence. However, fusion of even myoblasts in the competent stage was blocked in calcium-deficient medium, suggesting that calcium is essential for the fusion, probably at a step immediately before membrane union. Unlike fusion, other biochemical processes of differentiation proceeded even in calcium-deficient medium, indicating a distinction of fusion from these other processes during myoblast differentiation.

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Section: Discussionmentioning

confidence: 99%

Differentiation of Quail Myoblasts Transformed with a Temperature Sensitive Mutant of Rous Sarcoma Virus. II. Relationship of Myoblast Fusion with Calcium and Temperature

Kim

Adachi

Saiuchi

et al. 1992

Cell Struct. Funct.

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“…It is doubtful, however, that the ob served pattern of lectin binding is due solely to the AChR. The differentiating muscle cell contains a number of glycoproteins [45] so that each lectin most likely binds to more than one surface glycoprotein. In addition, some lectins associated with AChR patches occurred elsewhere as well.…”

Section: Discussionmentioning

confidence: 99%

“…It would be of inter est, therefore, to determine whether the spe cialized patches on myotube surfaces differ in their carbohydrate composition from the general cell surface. Plant lectins have been used to identify and map the glycoconjugate composition of developing tissues [2,31,34,37,45]. Some studies have described the binding of lectins to myoblasts and myotubes [11,14,16,22].…”

Section: Introductionmentioning

confidence: 99%

“…In addition, to determine whether lectin binding sites colocalize with AChR-rich regions, cells were doublestained with F-labeled lectins and HRP-labeled a-bungarotoxin (HRP-a-BTX). Final ly, the distribution of fibronectin, a major cell surface glycoprotein which plays a role in cell adhesion and undergoes major changes dur ing myogenesis [7,14,20,35,45], was deter mined by an immunocytochemical proce dure.…”

Section: Introductionmentioning

confidence: 99%

“…Fi bronectin is an adhesive protein that binds cells to other cells or to the substrate [47]. During myogenesis, fibronectin undergoes changes in amount and distribution and may be involved in the fusion of myoblasts to form multinucleated myotubes [7,14,20,35,38,45], In the postmitotic myotube, fibronectin could function in establishment of the neuro muscular junction by promoting adhesion of the innervating nerve to the muscle surface.…”

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confidence: 99%

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Distribution of Cell Surface Saccharides and Fibronectin on Cultured Chick Myotubes: Relationship to Acetylcholine Receptor Clusters

Burrage

Lentz

1982

Dev Neurosci

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This study examines the distribution of glycoconjugates on the surface of cultured chick myotubes with a battery of lectins labeled with ferritin or horseradish peroxidase. In addition, the distribution of a specific glycoprotein, fibronectin, is investigated by immunocytochemistry. Particular attention is paid to the localization of these substances in specialized patches on the cell surface previously shown to contain a high density of acetylcholine receptors as demonstrated with horseradish peroxidase labeled α-bungarotoxin. The specialized patches are found to bind a greater amount of concanavalin A, ricin agglutinin I, and soy bean agglutinin and a lesser amount of wheat germ agglutinin than the general myotube surface. Limulus lectin is distributed over the entire cell surface while other lectins do not bind to any sites. The surface patches contain a high density of acetylcholine receptors as shown by double labeling with ferritin-labeled lectins and peroxidase labeled α-bungarotoxin. Fibronectin occurs in high concentration at the surface patches and is present over other regions of the cell surface as well. These results reveal differential patterns of distribution of glycoconjugates and fibronectin over the myotube surface. These regional differences may be related to the distribution of acetylcholine receptors or to recognition and attachment by the innervating nerve.

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Plasminogen activator: The major secreted neutral protease of cultured skeletal muscle cells

Festoff

Patterson

Romstedt

1982

Journal Cellular Physiology

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Clonal mouse skeletal muscle cells which differentiate in culture and form synapses with neuronal cells were found to secrete high levels of protease activity as measured with an 125I-fibrin assay. The secreted proteolytic activity was more than 90% dependent upon the presence of plasminogen in the medium, and had a pH optimum at 7 to 8. This activity was not inhibited by n-ethylmaleimide, pepstatin, EDTA, or EGTA. At millimolar concentrations, greater than 90% inhibition was obtained with either soybean trypsin inhibitor, epsilon aminocaproic acid, Trasylol, or leupeptin. Almost complete inhibition occurred with 1 mM diisopropylfluorophosphate suggesting the presence of a serine residue at the catalytic site. In contrast to the high levels of secreted activity, a lower steady-state level of cell-associated protease activity was detected in cell lysates. The high level of plasminogen activator secreted into the medium of cultured muscle cells suggests a role for such extracellular protease activity in myogenesis during development and remodeling following muscle injury. Such information may be useful in understanding the initial degeneration of neuromuscular contacts in experimental and pathologic denervation.

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Specific changes in cellular glycoproteins and surface proteins during myogenesis in clonal muscle cells

Cited by 59 publications

References 19 publications

Differentiation of Quail Myoblasts Transformed with a Temperature Sensitive Mutant of Rous Sarcoma Virus. II. Relationship of Myoblast Fusion with Calcium and Temperature

Differentiation of Quail Myoblasts Transformed with a Temperature Sensitive Mutant of Rous Sarcoma Virus. II. Relationship of Myoblast Fusion with Calcium and Temperature

Distribution of Cell Surface Saccharides and Fibronectin on Cultured Chick Myotubes: Relationship to Acetylcholine Receptor Clusters

Plasminogen activator: The major secreted neutral protease of cultured skeletal muscle cells

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