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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| Published in | The Journal of cell biology Vol. 115; no. 5; pp. 1437 - 1448 |
|---|---|
| Main Authors | , , |
| Format | Journal Article |
| Language | English |
| Published |
United States
Rockefeller University Press
01.12.1991
The Rockefeller University Press |
| Subjects | |
| Online Access | Get full text |
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| Abstract | 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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| AbstractList | 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. 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. |
| Author | Massa, Stephen M. Barondes, Samuel H. Douglas N. W. Cooper |
| Author_xml | – sequence: 1 fullname: Douglas N. W. Cooper – sequence: 2 givenname: Stephen M. surname: Massa fullname: Massa, Stephen M. – sequence: 3 givenname: Samuel H. surname: Barondes fullname: Barondes, Samuel H. |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/1955484$$D View this record in MEDLINE/PubMed |
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| Snippet | 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... |
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| SubjectTerms | 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 |
| Title | Endogenous Muscle Lectin Inhibits Myoblast Adhesion to Laminin |
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