Advertisement

Amendment history:

Research Article Free access | 10.1172/JCI1204

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.

Find articles by Udani, M. in: JCI | PubMed | Google Scholar

Division of Hematology, Department of Medicine, Duke University Medical Center, Duke University, Durham, North Carolina 27710, USA.

Find articles by Zen, Q. in: JCI | PubMed | Google Scholar

Division of Hematology, Department of Medicine, Duke University Medical Center, Duke University, Durham, North Carolina 27710, USA.

Find articles by Cottman, M. in: JCI | PubMed | Google Scholar

Division of Hematology, Department of Medicine, Duke University Medical Center, Duke University, Durham, North Carolina 27710, USA.

Find articles by Leonard, N. in: JCI | PubMed | Google Scholar

Division of Hematology, Department of Medicine, Duke University Medical Center, Duke University, Durham, North Carolina 27710, USA.

Find articles by Jefferson, S. in: JCI | PubMed | Google Scholar

Division of Hematology, Department of Medicine, Duke University Medical Center, Duke University, Durham, North Carolina 27710, USA.

Find articles by Daymont, C. in: JCI | PubMed | Google Scholar

Division of Hematology, Department of Medicine, Duke University Medical Center, Duke University, Durham, North Carolina 27710, USA.

Find articles by Truskey, G. in: JCI | PubMed | Google Scholar

Division of Hematology, Department of Medicine, Duke University Medical Center, Duke University, Durham, North Carolina 27710, USA.

Find articles by Telen, M. in: JCI | PubMed | Google Scholar

Published June 1, 1998 - More info

Published in Volume 101, Issue 11 on June 1, 1998
J Clin Invest. 1998;101(11):2550–2558. https://doi.org/10.1172/JCI1204.
© 1998 The American Society for Clinical Investigation
Published June 1, 1998 - Version history
View PDF
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.

Version history
  • Version 1 (June 1, 1998): No description
Advertisement
Advertisement