Sulfation-dependent recognition of high endothelial venules (HEV)-ligands by L-selectin and MECA 79, and adhesion-blocking monoclonal antibody.

Abstract

L-selectin is a lectin-like receptor that mediates the attachment of lymphocytes to high endothelial venules (HEV) of lymph nodes during the process of lymphocyte recirculation. Two sulfated, mucin-like glycoproteins known as Sgp50/GlyCAM-1 and Sgp90/CD34 have previously been identified as HEV-associated ligands for L-selectin. These proteins were originally detected with an L-selectin/Ig chimera called LEC-IgG. GlyCAM-1 and CD34 are also recognized by an antiperipheral node addressin (PNAd) mAb called MECA 79, which blocks L-selectin-dependent adhesion and selectively stains lymph node HEV. The present study compares the requirements for the binding of MECA 79 and LEC-IgG to HEV-ligands. Whereas desialylation of GlyCAM-1 and CD34 drastically reduced binding to LEC-IgG, this treatment enhanced the binding of GlyCAM-1 to MECA 79. In contrast, the binding of both MECA 79 and LEC-IgG to GlyCAM-1 and CD34 was greatly decreased when the sulfation of these ligands was reduced with chlorate, a metabolic inhibitor of sulfation. Because MECA 79 stains HEV-like vessels at various sites of inflammation, recognition by L-selectin of ligands outside of secondary lymphoid organs may depend on sulfation. In addition to their reactivity with GlyCAM-1 and CD34, both MECA 79 and LEC-IgG recognize an independent molecule of approximately 200 kD in a sulfate-dependent manner. Thus, this molecule, which we designate Sgp200, is an additional ligand for L-selectin.

• Authors: S Hemmerich, E C Butcher, S D Rosen
• Journal: The Journal of experimental medicine (J Exp Med) Vol. 180 Issue 6 Pg. 2219-26 (Dec 01 1994) ISSN: 0022-1007 [Print] United States
• PMID: 7525849 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't, Research Support, U.S. Gov't, P.H.S.)

Chemical References

• Antibodies
• Antibodies, Monoclonal
• Antigens, CD
• Antigens, CD34
• Cell Adhesion Molecules
• Mucins
• Peptides
• Recombinant Fusion Proteins
• Sulfates
• Sulfur Radioisotopes
• Tritium
• L-Selectin
• sulfated glycoprotein p50
• Galactose

Topics

• Amino Acid Sequence
• Animals
• Antibodies
• Antibodies, Monoclonal (pharmacology)
• Antigens, CD (immunology, physiology)
• Antigens, CD34
• Binding Sites
• Cell Adhesion (drug effects, immunology, physiology)
• Cell Adhesion Molecules (pharmacology)
• Cells, Cultured
• Endothelium, Vascular (physiology)
• Galactose (metabolism)
• L-Selectin
• Lymph Nodes (blood supply)
• Lymphocytes (physiology)
• Mice
• Mice, Inbred ICR
• Molecular Sequence Data
• Mucins (immunology, physiology)
• Peptides (chemical synthesis, immunology)
• Recombinant Fusion Proteins (pharmacology)
• Sulfates (metabolism)
• Sulfur Radioisotopes
• Tritium