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Basal cell adhesion molecule/lutheran protein. The receptor critical for sickle cell adhesion to laminin.
M Udani, … , G Truskey, M J Telen
M Udani, … , G Truskey, M J Telen
Published June 1, 1998
Citation Information: J Clin Invest. 1998;101(11):2550-2558. https://doi.org/10.1172/JCI1204.
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Research Article

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

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Abstract

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.

Authors

M Udani, Q Zen, M Cottman, N Leonard, S Jefferson, C Daymont, G Truskey, M J Telen

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