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Platelet adhesion to decorin but not collagen I correlates with the integrin ?2 dimorphism E534K, the basis of the human platelet alloantigen (HPA)-5 system

  • Author(s): Kunicki, Thomas J.
  • Williams, Shirley A.
  • Diaz, Daniel
  • Farndale, Richard W.
  • Nugent, Diane J.
  • et al.
Creative Commons Attribution 4.0 International Public License
Abstract

A single nucleotide polymorphism in the integrin α2 gene ITGA2 (rs1801106; G1600A) creates the non-conservative amino acid substitution E534K, the basis of the human platelet alloantigen system HPA-5. Yet HPA-5 alleles do not influence binding of α2β1 to its primary ligand collagen I, and the effect of HPA-5 on platelet function has not been determined. We used a direct platelet adhesion assay to evaluate whether differential inheritance of HPA-5 alleles influences platelet adhesion to collagen I or an alternative ligand, decorin. Platelets from donors bearing one or more minor allele HPA-5b showed attenuated adhesion to purified decorin but not collagen I. Adhesion to decorin was significantly inhibited by human alloantibodies specific for HPA-5a but not by the collagen I sequence GFOGER or α2-specific inhibitory monoclonal antibodies. The minor allele 534K attenuates platelet adhesion to decorin but not collagen I, providing the first evidence of a functional effect of HPA-5 alleles.

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