Endogenous Muscle Lectin Inhibits Myoblast Adhesion to Laminin

L-14, a dimeric lactose-binding lectin with subunits of 14 kD, is expressed in a wide range of vertebrate tissues. Several functions have been postulated for this lectin, but definitive evidence for a specific biological role has been elusive. In muscle, L-14 is secreted during differentiation and a...

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Bibliographic Details
Published inThe Journal of cell biology Vol. 115; no. 5; pp. 1437 - 1448
Main Authors Douglas N. W. Cooper, Massa, Stephen M., Barondes, Samuel H.
Format Journal Article
LanguageEnglish
Published United States Rockefeller University Press 01.12.1991
The Rockefeller University Press
Subjects
Animals
Cell Adhesion
Cell Differentiation
Cell lines
Cells
Cells, Cultured
Glycoconjugates
Glycoproteins - metabolism
Immunohistochemistry
laminin
Laminin - metabolism
Lectins
Lectins - physiology
Ligands
Mice
Muscle fibers
Muscles
Muscles - cytology
Muscles - metabolism
Myoblasts
Recombinant Proteins - physiology
Secretion
Transfection
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Summary:L-14, a dimeric lactose-binding lectin with subunits of 14 kD, is expressed in a wide range of vertebrate tissues. Several functions have been postulated for this lectin, but definitive evidence for a specific biological role has been elusive. In muscle, L-14 is secreted during differentiation and accumulates with laminin in basement membrane surrounding each myofiber. Here we present evidence that laminin is a major glycoprotein ligand for L-14 in differentiating mouse C2C12 muscle cells and that binding of secreted L-14 to polylactosamine oligosaccharides of substrate laminin induces loss of cell-substratum adhesion. These results suggest that one function of L-14 is to regulate myoblast detachment from laminin during differentiation and fusion into tubular myofibers.
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ISSN:0021-9525
1540-8140
DOI:10.1083/jcb.115.5.1437