Developmental regulation of cell-surface glycoproteins in clonal cultures of human skeletal muscle satellite cells

Pure populations of myogenic cells were obtained by cloning satellite cells from human skeletal muscle biopsies. Cell-surface glycoproteins at various stages of myogenesis were analysed by one- and two-dimensional gel electrophoresis. A total of 14 distinct proteins were detectable at the cell surface, on the basis of their susceptibility to desialation by exogenous neuraminidase or their iodination by exogenous lactoperoxidase. Reproducible changes in lectin binding or iodination of eight of these proteins occurred during myogenesis. Only two of the developmentally regulated proteins were components of the detergent-insoluble extracellular matrix fraction. Developmental regulation of these two proteins was unaffected by growth of cultures in 5-bromo-2′-deoxyuridine to inhibit myogenesis. In contrast, developmental regulation of the other cell-surface proteins was inhibited by growth in 5-bromo-2′-deoxyuridine, suggesting that changes in these proteins are tightly coupled to satellite cell differentiation. These studies represent the first systematic analysis of the surface proteins of pure, clonally derived, primary cultures of normal myogenic cells.Key words: satellite cells, myogenesis, myoblast, glycoproteins, cell surface.

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Cloning and characterization of a myoblast cell surface antigen defined by 24.1D5 monoclonal antibody

Development ◽

10.1242/dev.105.4.723 ◽

1989 ◽

Vol 105 (4) ◽

pp. 723-731 ◽

Cited By ~ 1

Author(s):

H.J. Gower ◽

S.E. Moore ◽

G. Dickson ◽

V.L. Elsom ◽

R. Nayak ◽

...

Keyword(s):

Skeletal Muscle ◽

Monoclonal Antibody ◽

Cell Surface ◽

Human Skeletal Muscle ◽

Muscle Development ◽

Early Stage ◽

Primary Cultures ◽

Skeletal Muscle Development ◽

Mouse Muscle ◽

Human Skeletal Muscle Cells

Monoclonal antibody 24.1D5 reacts specifically with an epitope expressed on the cell surface of mononucleate myoblasts in primary cultures of human skeletal muscle cells, but not with either multinucleate myotubes or fibroblasts. Polypeptides of 60 and 100 X 10(3) Mr were identified by immunoblotting with the McAb. Human muscle cDNAs encoding the 24.1D5 epitope were used to study further the structure and expression of 24.1D5 during skeletal muscle development. Two mRNA species of 3.0 and 2.5 kb were identified in primary cultures of human skeletal muscle and in mouse muscle cell lines. The levels of both transcripts decreased during myotube formation in vitro and were similarly decreased during myogenesis in the mouse embryo. 24.1D5 mRNAs were expressed by multipotential cells and myoblast derivatives of the mouse embryonic cell line C3H10T1/2, suggesting that 24.1D5 is expressed at an early stage during skeletal muscle development.

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Cell surface glycoproteins change during gastrulation in Pleurodeles waltlii

Journal of Cell Science ◽

10.1242/jcs.82.1.23 ◽

1986 ◽

Vol 82 (1) ◽

pp. 23-40

Author(s):

J.F. Riou ◽

T. Darribere ◽

J.C. Boucaut

Keyword(s):

Cell Surface ◽

Gel Electrophoresis ◽

Lectin Binding ◽

Galactose Oxidase ◽

Two Dimensional ◽

Isolated Cells ◽

Two Dimensional Gel Electrophoresis ◽

Sodium Metaperiodate ◽

Cell Surface Glycoproteins ◽

Surface Glycoproteins

Identification of the cell surface glycoproteins is an essential requirement for elucidating the mechanisms that mediate intercellular adhesion and cell migration in gastrulating amphibian embryos. In our experiments the glycoproteins present at the surface of isolated cells at blastula and gastrula stages were labelled with 3H-labelled sodium borohydride. The procedure included the oxidation of either galactosyl and, or, N-acetylgalactosaminyl residues with galactose oxidase or sialic acid with sodium metaperiodate. The tritiated components were analysed by two-dimensional gel electrophoresis. On the surface of isolated embryonic cells, 23 glycoproteins have been identified. The most important observation was the labelling of 15 new glycoproteins during gastrulation. At the late blastula stage, eight glycoproteins containing galactosyl or N-acetyl-galactosaminyl residues are labelled, while 23 are labelled at the late gastrula stage. In other experiments, glycoproteins labelled by [3H]fucose or [3H]mannose or precipitated by concanavalin A(ConA)-, or wheat-germ agglutinin (WGA)-Sepharose were studied by two-dimensional gel electrophoresis in order to provide supplementary data on the synthesis and lectin-binding properties of major cell surface glycoproteins. It appears that approximately 100 different glycoproteins are revealed by these methods. Among them, 13 have been identified as major cell surface glycoproteins, 12 being labelled by [3H]mannose, four by [3H]fucose, 10 bearing an affinity for ConA and five for WGA. These 13 glycoproteins are synthesized throughout gastrulation without qualitative variation.

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Selective reentry of recycling cell surface glycoproteins to the biosynthetic pathway in human hepatocarcinoma HepG2 cells.

The Journal of Cell Biology ◽

10.1083/jcb.130.3.537 ◽

1995 ◽

Vol 130 (3) ◽

pp. 537-551 ◽

Cited By ~ 40

Author(s):

B Volz ◽

G Orberger ◽

S Porwoll ◽

H P Hauri ◽

R Tauber

Keyword(s):

Cell Surface ◽

Hepg2 Cells ◽

Biosynthetic Pathway ◽

Secretory Pathway ◽

Surface Proteins ◽

Early Secretory Pathway ◽

Golgi Transport ◽

Cell Surface Glycoproteins ◽

Golgi Network ◽

Surface Glycoproteins

Return of cell surface glycoproteins to compartments of the secretory pathway has been examined in HepG2 cells comparing return to the trans-Golgi network (TGN), the trans/medial- and cis-Golgi. Transport to these sites was studied by example of the transferrin receptor (TfR) and the serine peptidase dipeptidylpeptidase IV (DPPIV) after labeling these proteins with the N-hydroxysulfosuccinimide ester of biotin on the cell surface. This experimental design allowed to distinguish between glycoproteins that return to these biosynthetic compartments from the cell surface and newly synthesized glycoproteins that pass these compartments during biosynthesis en route to the surface. Reentry to the TGN was measured in that surface glycoproteins were desialylated with neuraminidase and were monitored for resialylation during recycling. Return to the trans-Golgi was traced measuring the transfer of [3H]fucose residues to recycling surface proteins by fucosyltransferases. To study return to the cis-Golgi, surface proteins were metabolically labeled in the presence of the mannosidase I inhibitor deoxymannojirimycin (dMM). As a result surface proteins retained N-glycans of the oligomannosidic type. Return to the site of mannosidase I in the medial/cis-Golgi was measured monitoring conversion of these glycans to those of the complex type after washout of dMM. Our data demonstrate that DPPIV does return from the cell surface not only to the TGN, but also to the trans-Golgi thus linking the endocytic to the secretory pathway. In contrast, no reentry to sites of mannosidase I could be detected indicating that the early secretory pathway is not or is only at insignificant rates accessible to recycling DPPIV. In contrast to DPPIV, TfR was very efficiently sorted from endosomes to the cell surface and did not return to the TGN or to other biosynthetic compartments in detectable amounts, indicating that individual surface proteins are subject to different sorting mechanisms or sorting efficiencies during recycling.

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Effect of insulin on GLUT4 cell surface content and turnover rate in human skeletal muscle as measured by the exofacial bis-mannose photolabeling technique

Diabetes ◽

10.2337/diabetes.46.12.1965 ◽

1997 ◽

Vol 46 (12) ◽

pp. 1965-1969 ◽

Cited By ~ 5

Author(s):

S. Lund ◽

G. D. Holman ◽

J. R. Zierath ◽

J. Rincon ◽

L. A. Nolte ◽

...

Keyword(s):

Skeletal Muscle ◽

Cell Surface ◽

Human Skeletal Muscle ◽

Turnover Rate ◽

Surface Content

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The B4 lectin from Vicia villosa seeds interacts with N-acetylgalactosamine residues alpha-linked to serine or threonine residues in cell surface glycoproteins.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(18)32554-7 ◽

1983 ◽

Vol 258 (8) ◽

pp. 5172-5176 ◽

Cited By ~ 3

Author(s):

S E Tollefsen ◽

R Kornfeld

Keyword(s):

Cell Surface ◽

Vicia Villosa ◽

Cell Surface Glycoproteins ◽

Surface Glycoproteins

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Recognition of collagen by fibroblasts through cell surface glycoproteins reactive with Phaseolus vulgaris agglutinin

Journal of Cell Science ◽

10.1242/jcs.101.3.625 ◽

1992 ◽

Vol 101 (3) ◽

pp. 625-633

Author(s):

H. Asaga ◽

K. Yoshizato

Keyword(s):

Phaseolus Vulgaris ◽

Cell Surface ◽

Ricinus Communis ◽

Specific Binding ◽

Collagen Gel ◽

Collagen Fibrils ◽

Pokeweed Mitogen ◽

Collagen Gel Contraction ◽

Cell Surface Glycoproteins ◽

Surface Glycoproteins

The role of glycochains of cell surface glycoproteins in the cell to collagen interaction was examined by studying the effect of lectins on the fibroblast-mediated collagen gel contraction. Lectins of Phaseolus vulgaris agglutinin (PHA), concanavalin A (ConA), lentil seed agglutinin (LCA), pea agglutinin (PSA), Ricinus communis agglutinin-60 (RCA), and wheat germ agglutinin (WGA) dose-dependently inhibited gel contraction, while lectins of mushroom agglutinin (ABA), peanut agglutinin (PNA), pokeweed mitogen (PWM), and soybean agglutinin (SBA) did not. Of these lectins, PHA seemed to be worthy of further analysis, because PHA, but not other lectins, inhibited spreading of fibroblasts on collagen fibrils but not on plastic or gelatin, suggesting that cell-surface glycoproteins responsive to the lectin are involved in the specific binding of fibroblasts to native collagen fibrils. The inhibitory effect of PHA-E4, an isolectin of PHA, was more intense than that of PHA-L4, another isolectin of PHA. The collagen gel contraction was also inhibited by tunicamycin and monensin in a concentration-dependent and reversible manner. These results strongly suggest that PHA-E4-reactive glycoproteins of the fibroblast surface play an important role in cell to collagen binding during the gel contraction. Five membrane proteins including beta 1 subunits of the integrin family were obtained by affinity chromatography with PHA-E4.

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