Alterations in surface proteins during myogenesis of a rat myoblast cell line

Pauw, Peter G.; David, John D.

doi:10.1016/0012-1606(79)90004-6

Cited by 51 publications

(7 citation statements)

References 22 publications

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“…However, the source phospholipid has been found to be phosphatidylcholine (Kent, 1979;Grove & Schimmel, 1982). The metabolism of this lipid is unchanged in Ca2+-activated neutral proteinases Lipids (i) Unique phospholipid asymmetry (ii) Changes in ganglioside pattern (iii) Inositol phospholipid breakdown Plasma membrane structure (i) Reorganization of cytoskeletal framework (ii) Particle-free domains at fusion sites (iii) Increase in membrane fluidity Gartner & Podleski (1975) Cates & Holland (1978) Yoshioka & Suroka (1983) Senechal et al (1982) Walsh et al (1984; Kaufman & Foster (1984) Kaufman & Foster (1984 Moss et al (1978) Pauw & David (1979) Couch & Strittmatter (1983) Kaur & Sanwal (1981) Sessions & Horwitz (1983) Whatley et al (1976) Wakelam & Pette (1982); Wakelam (1983) Fulton et al (1981) Kalderon & Gilula (1979) Weidekamm et al (1976; Prives & Shinitzky (1977); Herman & Fernandez (1978; Elson & Yguerabide (1979) normal myoblast fusion (Wakelam & Pette, 1982). Table 1 summarizes the various changes in myoblast membrane structure known to occur at fusion.…”

Section: Relationship Between Membrane Organization and Fusion Mechanmentioning

confidence: 96%

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The fusion of myoblasts

Wakelam¹

1985

Biochemical Journal

304

197

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Section: Relationship Between Membrane Organization and Fusion Mechanmentioning

confidence: 96%

“…Moss et al (1978) and Pauw & David (1979) utilized lactoperoxidase-catalysed iodination of surface proteins. Decreased amounts of high-Mr proteins and higher amounts of low-Mr proteins were found during fusion.…”

Section: Surface Biochemistry Of Myoblasts During Fusionmentioning

confidence: 99%

The fusion of myoblasts

Wakelam¹

1985

Biochemical Journal

304

197

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“…Attempts have been made to identify changes in cell-surface glycoproteins during myogenesis using lactoperoxidase-catalysed iodination of exposed tyrosine residues (Hynes et al, 1976;Moss et al, 1978;Pauw & David, 1979;Cates & Holland, 1978Walsh & Phillips, 1981). From these studies only one 125I-labelled protein has been clearly shown to correspond to a cell-surface glycoprotein, namely fibronectin.…”

mentioning

confidence: 99%

Developmental regulation of neuraminidase-sensitive lectin-binding glycoproteins during myogenesis of rat L6 myoblasts

Holland¹,

Pena²,

Guérin³

1984

Biochemical Journal

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Intact monolayers of L6 myoblasts were treated with neuraminidase, with the aim of selectively removing sialic acid residues of cell-surface glycoproteins. Neuraminidase treatment unmasked binding sites for Ricinus communis agglutinin I and peanut agglutinin, thus allowing the identification of the major binding proteins for these lectins. For Ricinus communis agglutinin I these neuraminidase-sensitive glycoproteins had apparent Mr values of 136000, 115000, 87000, 83000 and 49000. For peanut agglutinin the major neuraminidase-sensitive glycoproteins had apparent Mr values of 200000, 136000, 87000 and 83000. We found highly reproducible, developmentally regulated, changes in the lectin-binding capacity of certain of these glycoproteins as L6 myoblasts differentiated into myotubes. Coincident with myoblast fusion there was a co-ordinate decrease in Ricinus communis agglutinin I binding by glycoproteins of apparent Mr of 136000 and 49000. There was also a co-ordinate shift in mobility of the broad band of glycoprotein, centred at an apparent Mr of 115000 in myoblasts, to a new average apparent Mr of 107000 in mid-fusion cultures and myotube cultures. Peanut agglutinin binding by the major protein of apparent Mr 136000 also decreased at the mid-fusion stage of myogenesis, and was barely detectable in 7-day-old fused cultures. These developmentally regulated changes in neuraminidase-sensitive glycoproteins were all inhibited by growth of myoblasts in 6.4 microM-5-bromo-2'-deoxyuridine, indicating that they are associated with myoblast differentiation. In contrast, an increase in fibronectin was seen in mid-fusion cultures, which was not inhibited by growth of myoblasts in 5-bromo-2'-deoxyuridine. This initial increase in fibronectin is, therefore, unlikely to be directly related to myoblast fusion or differentiation.

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“…[ IJ-Lactoperoxidase-catalyzed iodination of cell surface proteins, (a) Monolayer -lodinations were performed on 100 mm plates by a modification of the procedure ofHynes (1973) as described byPauw and David (1979). Plates were rinsed 5 times with Pucks saline G (room ten^erature) and incubated in 4 ml of this buffer without phenol red 125 but including 200 yci carrier-free sodium [ I] iodide (New England Nuclear or Amersham, specific activity 100 mCi/ml.…”

mentioning

confidence: 99%

Isolation and characterization of cytochalasin D-resistant variants of a Chinese hamster ovary cell line

Grund

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Alterations in surface proteins during myogenesis of a rat myoblast cell line

Cited by 51 publications

References 22 publications

The fusion of myoblasts

The fusion of myoblasts

Developmental regulation of neuraminidase-sensitive lectin-binding glycoproteins during myogenesis of rat L6 myoblasts

Isolation and characterization of cytochalasin D-resistant variants of a Chinese hamster ovary cell line

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