Two laminin receptors with N-acetylglucosamine-binding specificity.
Two glycoproteins, the first, CBP70 which has lectin properties, and the second, cbg72 which is a laminin-1 receptor, have been previously described. We investigated whether cbg72 could have lectin properties and whether CBP70 could have a laminin-receptor function. We observed that CBP70, like cbg72, is a laminin-binding protein. CBP70 interacts with laminin-1 in a carbohydrate-dependent fashion, but this interaction could also be a protein-protein interaction. In parallel, we showed that cbg72, as well as CBP70, is a lectin that recognizes glucose and N-acetylglucosamine in a calcium-dependent manner. Moreover, cross-immunoreactivity was observed between these two lectins using their respective antibodies. The resistance of the two lectins, cbg72 and CBP70, to Triton X-100 extraction, suggests that they potentially interact with cytoskeleton elements, since transmembrane proteins that interact with cytoskeleton elements are known to be resistant to such an extraction.
Botti
Joelle
J
Unité INSERM 504, Hôpital Paul-Brousse, Bâtiment INSERM, 16, avenue Paul-Vaillant-Couturier, 94807 Villejuif, France.
Musset
Murielle
M
Moutsita
Richard
R
Aubery
Michèle
M
Derappe
Christian
C
D000117:Acetylglucosamine / Q000737:chemistry / Q000378:metabolism*; D000818:Animals; D002460:Cell Line; D003429:Cross Reactions; D003599:Cytoskeleton / Q000737:chemistry / Q000378:metabolism; D006801:Humans; D015151:Immunoblotting; D007150:Immunohistochemistry; D007797:Laminin / Q000737:chemistry / Q000378:metabolism; D037102:Lectins / Q000032:analysis / Q000737:chemistry / Q000378:metabolism*; D008856:Microscopy, Fluorescence; D011485:Protein Binding; D017474:Receptors, Laminin / Q000737:chemistry / Q000378:metabolism*
D007797:Laminin; D037102:Lectins; D017474:Receptors, Laminin; C104787:carbohydrate-binding protein 70, human; D000117:Acetylglucosamine