Reduced high shear platelet adhesion to the vascular media: Defective von Willebrand Factor binding to the interstitial collagen

Erzsebet Komorowicz, Robert D. McBane, Jon Charlesworth, David N. Fass

Research output: Contribution to journalArticle

6 Scopus citations


Fibrillar collagen serves as a thrombogenic surface for platelet adhesion mediated by von Willebrand factor (vWf) at high shear. Although abundant throughout the arterial wall, vWf-dependent platelet deposition to artery cross-sections from perfused citrated blood is localized to the adventitia of the vessel wall. Here we describe a similarly skewed distribution of vWf-binding sites in artery cross-sections. Binding of vWf-coated fluorescent beads, as well as detection of plasma vWf bound to artery cross-section at 3350 s-1 shear rate with indirect particle-immunofluorescence or immunoelectron microscopy demonstrate vWf binding sites in the adventitia, but not in the media. A monoclonal anti-vWf antibody that interferes with vWf-binding to collagen in a microplate ELISA inhibits vWf-binding to both the adventitia and sections of collagen fibrils. Our data suggest that the media, despite its fibrillar collagen content, evidenced by electron microscopy, is defective for vWf-binding, which may explain its thromboresistant nature at high shear rates.

Original languageEnglish (US)
Pages (from-to)763-770
Number of pages8
JournalThrombosis and Haemostasis
Issue number4
StatePublished - Apr 23 2002



  • Adhesion
  • Collagen
  • Media
  • Platelet
  • Willebrand

ASJC Scopus subject areas

  • Hematology

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