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. 1998 Jun 1;101(11):2550–2558. doi: 10.1172/JCI1204

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

M Udani 1, Q Zen 1, M Cottman 1, N Leonard 1, S Jefferson 1, C Daymont 1, G Truskey 1, M J Telen 1
PMCID: PMC508844  PMID: 9616226

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.

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Selected References

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