The glycoprotein Ib-IX-V complex is a platelet counterreceptor for P- selectin

Gabriel M. Romo, Jing Fei Dong, Alicia J. Schade, Elizabeth E. Gardiner, Geoffrey S. Kansas, Chester Q. Li, Larry V. McIntire, Michael C. Berndt, José A. López*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

304 Scopus citations


We have identified platelet glycoprotein (GP) Ibα as a counterreceptor for P-selectin. GP Ibα is a component of the GP [b-IX-V complex, which mediates platelet adhesion to subendothelium at sites of injury. Cells expressing P-selectin adhered to immobilized GP Ibα, and GP Ibα-expressing cells adhered to and rolled on P-selectin and on histamine-stimulated endothelium in a P-selectin-dependent manner. In like manner, platelets rolled on activated endothelium, a phenomenon inhibited by antibodies to both P-selectin and GP Ibα. Unlike the P-selectin interaction with its leukocyte ligand, PSGL-1 (P-selectin glycoprotein ligand 1), the interaction with GP Ibα required neither calcium nor carbohydrate core-2 branching or α(1,3)- fucosylation. The interaction was inhibited by sulfated proteoglycans and by antibodies against GP Ibα, including one directed at a tyrosine-sulfated region of the polypeptide. Thus, the GP Ib-IX-V complex mediates platelet attachment to both subendothelium and activated endothelium.

Original languageEnglish (US)
Pages (from-to)803-813
Number of pages11
JournalJournal of Experimental Medicine
Issue number6
StatePublished - Sep 20 1999


  • Endothelium
  • PSGL-1
  • Platelet adhesion
  • Platelet glycoproteins
  • Selectins

ASJC Scopus subject areas

  • Immunology and Allergy
  • Immunology


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