Published in Volume
101, Issue 11 (June 1, 1998)
J Clin Invest. 1998;101(11):2550–2558.
doi:10.1172/JCI1204.
Copyright ©
1998, The American Society for
Clinical Investigation.
Research Article
Amended: Correction (July 1998)
Basal cell adhesion molecule/lutheran protein. The receptor critical for sickle cell adhesion to laminin.
M Udani, Q Zen, M Cottman, N Leonard, S Jefferson, C Daymont, G Truskey and M J Telen
Division of Hematology, Department of Medicine, Duke University Medical Center, Duke University, Durham, North Carolina 27710, USA.
Published June 1, 1998
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.
