Review: Lutheran/B-CAM: A Laminin Receptor on Red Blood Cells and in Various Tissues
- 1 January 2005
- journal article
- review article
- Published by Taylor & Francis in Connective Tissue Research
- Vol. 46 (4-5) , 193-199
- https://doi.org/10.1080/03008200500344074
Abstract
The Lutheran blood group glycoprotein (Lu), also known as basal cell adhesion molecule (B-CAM), is a transmembrane receptor with five immunoglobulin-like domains in its extracellular region; it is therefore classified as a member of the immunoglobulin (Ig) gene family. Lu/B-CAM is observed not only on red blood cells, but also on a subset of muscle and epithelial cells in various tissues. Recently, several groups have reported that Lu/B-CAM is a novel receptor for laminin α5. The laminin α5 chain is a component of the laminin-511 (α5β1γ1), -521 (α5β2γ1), and -523 (α5β2γ3) heterotrimers and is expressed throughout the mammalian body. We also have shown that Lu/B-CAM is co-localized with laminin α5 in various tissues. Although the biological role of Lu/B-CAM remains unclear, the specific binding of Lu/B-CAM to laminin α5 suggests that it plays an important role in developmental and physiological processes. It also is necessary to investigate further the interaction between Lu/B-CAM and laminin α5 in pathological processes, including sickle cell disease and cancer.Keywords
This publication has 64 references indexed in Scilit:
- Molecular Dissection of the α-Dystroglycan- and Integrin-binding Sites within the Globular Domain of Human Laminin-10Journal of Biological Chemistry, 2004
- Laminin α5 chain is required for intestinal smooth muscle developmentDevelopmental Biology, 2003
- Mesangial cells organize the glomerular capillaries by adhering to the G domain of laminin α5 in the glomerular basement membraneThe Journal of cell biology, 2003
- Identification of the Binding Site for the Lutheran Blood Group Glycoprotein on Laminin α5 through Expression of Chimeric Laminin Chains in VivoJournal of Biological Chemistry, 2002
- Localization of Lutheran, a novel laminin receptor, in normal, knockout, and transgenic mice suggests an interaction with laminin α5 in vivoDevelopmental Dynamics, 2001
- Characterization of the Laminin Binding Domains of the Lutheran Blood Group GlycoproteinJournal of Biological Chemistry, 2001
- Posttranslational Modifications and β/γ Chain Associations of Human Laminin α1 and Laminin α5 Chains: Purification of Laminin-3 from PlacentaExperimental Cell Research, 2000
- Isolation and Characterization of Laminin-10/11 Secreted by Human Lung Carcinoma CellsJournal of Biological Chemistry, 1998
- Neurolin, a cell surface glycoprotein on growing retinal axons in the goldfish visual system, is reexpressed during retinal axonal regenerationThe Journal of cell biology, 1992
- Report on group 8 (Lutheran) antibodiesRevue Française de Transfusion et Immuno-hématologie, 1988