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J. Biol. Chem., Vol. 269, Issue 48, 30081-30084, 12, 1994
PA McCourt, B Ek, N Forsberg and S Gustafson
Our laboratory has previously characterized and purified the hyaluronan
receptor by hyaluronan affinity chromatography of rat liver endothelial
cells. We have now isolated the receptor from whole rat liver and have
obtained sufficient quantities for amino acid sequence analysis. Four
peptides of various lengths were obtained from affinity-purified receptor
and found to have identity with rat intercellular adhesion molecule-1. This
glycoprotein is normally expressed in low amounts on the endothelial cells,
but is up-regulated in inflamed and malignant tissues, and mediates
cell-cell adhesion as a ligand for lymphocyte function-associated antigen-1
and the macrophage-associated Mac-1. The affinity of intercellular adhesion
molecule-1 for hyaluronan is likely to have important implications for cell
adhesion in normal and in disease states such as inflammation,
atherosclerosis, and cancer.
Intercellular adhesion molecule-1 is a cell surface receptor for hyaluronan
Department of Medical and Physiological Chemistry, University of Uppsala, Sweden.
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