Basal cell adhesion molecule/lutheran protein. The receptor critical for sickle cell adhesion to laminin

Sickle red cells bind significant amounts of soluble laminin, whereas normal red cells do not. Solid phase assays demonstrate that B-CAM/LU binds laminin on intact sickle red cells and that red cell B-CAM/LU binds immobilized laminin, whereas another putative laminin binding protein, CD44, does not....

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Bibliographic Details
Published in:The Journal of clinical investigation 1998-06, Vol.101 (11), p.2550-2558
Main Authors: Udani, M, Zen, Q, Cottman, M, Leonard, N, Jefferson, S, Daymont, C, Truskey, G, Telen, M J
Format: Article
Language:English
Subjects:
Anemia, Sickle Cell - blood
Animals
Blotting, Western
Cell Adhesion Molecules - metabolism
Erythrocytes - metabolism
Humans
Laminin - metabolism
Lutheran Blood-Group System
Mice
Neoplasm Proteins - metabolism
Receptors, Laminin - metabolism
Recombinant Proteins - metabolism
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Summary:Sickle red cells bind significant amounts of soluble laminin, whereas normal red cells do not. Solid phase assays demonstrate that B-CAM/LU binds laminin on intact sickle red cells and that red cell B-CAM/LU binds immobilized laminin, whereas another putative laminin binding protein, CD44, does not. Ligand blots also identify B-CAM/LU as the only erythrocyte membrane protein(s) that binds laminin. Finally, transfection of murine erythroleukemia cells with human B-CAM cDNA induces binding of both soluble and immobilized laminin. Thus, B-CAM/LU appears to be the major laminin-binding protein of sickle red cells. Previously reported overexpression of B-CAM/LU by epithelial cancer cells suggests that this protein may also serve as a laminin receptor in malignant tumors.
ISSN:0021-9738
1558-8238
DOI:10.1172/JCI1204