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Science 4 September 1992:
Vol. 257. no. 5075, pp. 1407 - 1409
DOI: 10.1126/science.1529341
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Articles

Science, Vol 257, Issue 5075, 1407-1409
Copyright © 1992 by American Association for the Advancement of Science

articles

A 90-kilodalton endothelial cell molecule mediating lymphocyte binding in humans

M Salmi and S Jalkanen

National Public Health Institute, Turku University, Finland.

Interactions between leukocyte surface receptors and their ligands on vascular endothelial cells control lymphocyte traffic between the blood and various lymphoid organs, as well as extravasation of leukocytes into sites of inflammation. A heretofore undescribed 90-kilodalton human endothelial cell adhesion molecule (VAP-1) defined by a monoclonal antibody 1B2 is described. The expression pattern, molecular mass, functional properties, and an amino-terminal amino acid sequence define VAP-1 as an endothelial ligand for lymphocytes. VAP-1 helps to elucidate the complex heterotypic cell interactions that direct tissue-selective lymphocyte migration in man.


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Circulating Form of Human Vascular Adhesion Protein-1 (VAP-1): Increased Serum Levels in Inflammatory Liver Diseases.
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Cloning of Vascular Adhesion Protein 1 Reveals a Novel Multifunctional Adhesion Molecule.
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The Role of Two Distinct Endothelial Molecules, Vascular Adhesion Protein-1 and Peripheral Lymph Node Addressin, in the Binding of Lymphocyte Subsets to Human Lymph Nodes.
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Vascular Adhesion Protein-1 and ICAM-1 Support the Adhesion of Tumor-Infiltrating Lymphocytes to Tumor Endothelium in Human Hepatocellular Carcinoma.
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J. Immunol. 160, 3978-3988
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Vascular Adhesion Protein 1 (VAP-1) Mediates Lymphocyte Subtype-specific, Selectin-independent Recognition of Vascular Endothelium in Human Lymph Nodes.
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J. Exp. Med. 186, 589-600
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Heterogeneity of Endothelial Cells : Specific Markers.
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   Abstract »    Full Text »


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