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

TitleBasal cell adhesion molecule/lutheran protein. The receptor critical for sickle cell adhesion to laminin.
Publication TypeJournal Article
Year of Publication1998
AuthorsUdani, M, Zen, Q, Cottman, M, Leonard, N, Jefferson, S, Daymont, C, Truskey, G, and Telen, MJ
JournalJournal of Clinical Investigation
Volume101
Issue11
Start Page2550
Pagination2550 - 2558
Date Published06/1998
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.

DOI10.1172/JCI1204
Short TitleJournal of Clinical Investigation