Endogenous muscle lectin inhibits myoblast adhesion to laminin.
Endogenous muscle lectin inhibits myoblast adhesion to laminin.
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DOI：
10.1083/jcb.115.5.1437
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发表时间：
1991-12
期刊：
影响因子：
--
通讯作者：
Barondes SH
中科院分区：
文献类型：
--
作者：
Cooper DN;Massa SM;Barondes SH
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.
