Sulphation requirement for GlyCAM-1, an endothelial ligand for L-selectin

Nature. 1993 Feb 11;361(6412):555-7. doi: 10.1038/361555a0.

Abstract

L-selectin participates in the initial attachment of leukocytes to the vascular endothelium. On lymphocytes, it mediates binding to high endothelial venules of lymph nodes. As a selectin it functions as a calcium-dependent lectin recognizing carbohydrate-bearing ligands on endothelial cells. Two lymph node ligands for L-selectin have been identified as sulphated glycoproteins of M(r) approximately 50K and approximately 90K, called Sgp50 and Sgp90 (ref. 10). The recently cloned Sgp50 (ref. 12), now designated GlyCAM-1, is a high endothelial venule-associated, mucin-like glycoprotein containing predominantly O-linked carbohydrate chains. Sialylation of GlyCAM-1 is necessary for its ligand activity and a role for fucosylation is suspected. We have used chlorate as a metabolic inhibitor of sulphation, and report here that GlyCAM-1 has an additional requirement for sulphate.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Animals
  • Cell Adhesion
  • Cell Adhesion Molecules
  • Endothelium / metabolism
  • L-Selectin
  • Lymph Nodes / chemistry
  • Membrane Glycoproteins
  • Mice
  • Mucins / metabolism*
  • Organ Culture Techniques
  • Sulfates / metabolism*
  • Threonine / metabolism

Substances

  • Cell Adhesion Molecules
  • Membrane Glycoproteins
  • Mucins
  • Sulfates
  • L-Selectin
  • sulfated glycoprotein p50
  • Threonine