The Lutheran glycoprotein: a multifunctional adhesion receptor.

Published

Journal Article (Review)

The Lutheran blood group system, which comprises one of the largest families of human red blood cell (RBC) antigens, resides on two immunoglobulin superfamily (IgSF) proteins: Lutheran and basal cell adhesion molecule (B-CAM). These two glycoproteins arise via alternative splicing of mRNA from a single gene and differ in structure only in the lengths of their cytoplasmic tails. Both are expressed on RBCs as well as a variety of other cell types, and they are overexpressed on sickle RBCs (SS RBC). B-CAM/Lu is the critical receptor for SS RBC adhesion to the extracellular matrix protein laminin, an interaction thought to contribute to the pathogenesis of sickle cell-related vasoocclusive events. Recent work has also shown that B-CAM/Lu on RBCs can undergo activation as a result of adrenergic signaling pathways. The high affinity of B-CAM/Lu for laminin is also thought to contribute to various developmental processes, including organogenesis, vascular development, erythropoiesis, and smooth muscle development and organization. Interestingly, the B-CAM spliceoform seems to be overexpressed by a variety of different malignant tumors and may be involved, along with other adhesion receptor proteins, in malignant transformation and tumor metastasis. Studies of B-CAM/Lu have thus expanded from defining antigen-specific polymorphisms to investigations of processes involved in sickle cell disease, human development, and cancer biology.

Full Text

Duke Authors

Cited Authors

  • Eyler, CE; Telen, MJ

Published Date

  • April 2006

Published In

Volume / Issue

  • 46 / 4

Start / End Page

  • 668 - 677

PubMed ID

  • 16584446

Pubmed Central ID

  • 16584446

International Standard Serial Number (ISSN)

  • 0041-1132

Digital Object Identifier (DOI)

  • 10.1111/j.1537-2995.2006.00779.x

Language

  • eng

Conference Location

  • United States