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

We have identified platelet glycoprotein (GP) Ibalpha as a counterreceptor for P-selectin. GP Ibalpha is a component of the GP Ib-IX-V complex, which mediates platelet adhesion to subendothelium at sites of injury. Cells expressing P-selectin adhered to immobilized GP Ibalpha, and GP Ibalpha-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 Ibalpha. Unlike the P-selectin interaction with its leukocyte ligand, PSGL-1 (P-selectin glycoprotein ligand 1), the interaction with GP Ibalpha required neither calcium nor carbohydrate core-2 branching or alpha(1,3)-fucosylation. The interaction was inhibited by sulfated proteoglycans and by antibodies against GP Ibalpha, 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.

Pubmed ID: 10499919


  • Romo GM
  • Dong JF
  • Schade AJ
  • Gardiner EE
  • Kansas GS
  • Li CQ
  • McIntire LV
  • Berndt MC
  • L√≥pez JA


The Journal of experimental medicine

Publication Data

September 20, 1999

Associated Grants

  • Agency: NHLBI NIH HHS, Id: HL18672
  • Agency: NHLBI NIH HHS, Id: HL54218

Mesh Terms

  • Animals
  • Blood Platelets
  • CHO Cells
  • Cricetinae
  • Endothelium, Vascular
  • Humans
  • Ligands
  • Membrane Glycoproteins
  • P-Selectin
  • Platelet Adhesiveness
  • Platelet Glycoprotein GPIb-IX Complex