Requirement for sialic acid on neutrophils in a GMP-140 (PADGEM) mediated adhesive interaction with activated platelets

Biochem Biophys Res Commun. 1990 Nov 15;172(3):1349-56. doi: 10.1016/0006-291x(90)91598-m.

Abstract

Platelet GMP-140, along with ELAM-1 and gp90MEL, comprise the LEC-CAM family of cell-cell adhesion proteins. The three proteins demonstrate a highly related domain organization, which includes an extracellular calcium-type lectin motif. gp90MEL, a lymphocyte homing receptor, mediates lymphocyte attachment to high endothelial venules of lymph nodes through recognition of a sialylated ligand on the endothelial cells. The rosetting of neutrophils or promyelocytic HL60 cells by activated platelets is mediated by GMP-140 on the platelets. We show here that treatment of neutrophils or HL60 cells with 3 broad spectrum sialidases completely prevents rosetting. However, the Newcastle disease virus sialidase, an enzyme specific for alpha 2,3 and alpha 2,8 linkages of sialic acid does not affect rosetting of HL60 cells. These results indicate that the ligand for GMP-140 requires sialic acid and suggest that an alpha 2,6 linkage may be critical.

Publication types

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

MeSH terms

  • Blood Platelets / metabolism*
  • Carbohydrate Conformation
  • Carbohydrate Sequence
  • Cell Adhesion Molecules / metabolism
  • Cells, Cultured
  • Egtazic Acid / pharmacology
  • Endothelium / metabolism
  • Humans
  • Molecular Sequence Data
  • Neuraminidase / pharmacology
  • Neutrophils / metabolism*
  • P-Selectin
  • Platelet Activation
  • Platelet Membrane Glycoproteins / metabolism*
  • Sialic Acids / metabolism*

Substances

  • Cell Adhesion Molecules
  • P-Selectin
  • Platelet Membrane Glycoproteins
  • Sialic Acids
  • Egtazic Acid
  • Neuraminidase