Inflammation

, Volume 28, Issue 4, pp 177–188

Sialylation of ICAM-2 on Platelets Impairs Adhesion of Leukocytes via LFA-1 and DC-SIGN

  • Kim S. C. Weber
  • Ronen Alon
  • Lloyd B. Klickstein
Article

Abstract

Intercellular adhesion molecule (ICAM)-2 is highly expressed on platelets and endothelium and is a counter-receptor for the leukocyte integrin, lymphocyte function-associated antigen-1 (LFA-1) and for the dendritic cell-specific, ICAM-grabbing non-integrin (DC-SIGN) protein. In this study, we investigated structural and functional differences between ICAM-2 from platelets and that from endothelial cells. The isoelectric point (pI) of ICAM-2 from HUVEC was pH 3.5–4.3, whereas that of platelet ICAM-2 was more acidic at pH 3.0–3.7. This charge difference was abolished by treatment with N-glycanase or neuraminidase, thus it was due to cell-specific N-linked glycosylation. Purified, immobilized platelet ICAM-2 supported 50% less adhesion of LFA-1-bearing T cells than did purified HUVEC ICAM-2 and no adhesion was observed of monocyte-derived immature dendritic cells via DC-SIGN to platelet ICAM-2. Treatment of platelet ICAM-2 with neuraminidase abolished these functional differences. These findings demonstrated that physiologic sialylation of platelet ICAM-2 renders it less able than endothelial ICAM-2 to support adherence of leukocytes.

platelets dendritic cells cell adhesion ICAM integrin 

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Copyright information

© Springer Science+Business Media, Inc. 2004

Authors and Affiliations

  • Kim S. C. Weber
    • 1
  • Ronen Alon
    • 2
  • Lloyd B. Klickstein
    • 3
  1. 1.Department of Medicine, Division of Rheumatology, Immunology & AllergyHarvard Medical School and Brigham & Women's HospitalBoston
  2. 2.Department of ImmunologyWeizmann InstituteRehovotIsrael
  3. 3.Sialylation of ICAM-2 on Platelets Impairs Adhesion of Leukocytes Via LFA-1 and DC-SIGN;USA

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