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 Citations (Scopus)

Abstract

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
Volume87
Issue number4
StatePublished - 2002

Fingerprint

Tunica Media
von Willebrand Factor
Collagen
Blood Platelets
Adventitia
Fibrillar Collagens
Arteries
Immunoelectron Microscopy
Indirect Fluorescent Antibody Technique
Fluorescence Microscopy
Electron Microscopy
Enzyme-Linked Immunosorbent Assay

Keywords

  • Adhesion
  • Collagen
  • Media
  • Platelet
  • Willebrand

ASJC Scopus subject areas

  • Hematology

Cite this

Reduced high shear platelet adhesion to the vascular media : Defective von Willebrand Factor binding to the interstitial collagen. / Komorowicz, Erzsebet; McBane, Robert D.; Charlesworth, Jon; Fass, David N.

In: Thrombosis and Haemostasis, Vol. 87, No. 4, 2002, p. 763-770.

Research output: Contribution to journalArticle

Komorowicz, Erzsebet ; McBane, Robert D. ; Charlesworth, Jon ; Fass, David N. / Reduced high shear platelet adhesion to the vascular media : Defective von Willebrand Factor binding to the interstitial collagen. In: Thrombosis and Haemostasis. 2002 ; Vol. 87, No. 4. pp. 763-770.
@article{987fff76e2314b50b24dd8f78cbe1535,
title = "Reduced high shear platelet adhesion to the vascular media: Defective von Willebrand Factor binding to the interstitial collagen",
abstract = "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.",
keywords = "Adhesion, Collagen, Media, Platelet, Willebrand",
author = "Erzsebet Komorowicz and McBane, {Robert D.} and Jon Charlesworth and Fass, {David N.}",
year = "2002",
language = "English (US)",
volume = "87",
pages = "763--770",
journal = "Thrombosis and Haemostasis",
issn = "0340-6245",
publisher = "Schattauer GmbH",
number = "4",

}

TY - JOUR

T1 - Reduced high shear platelet adhesion to the vascular media

T2 - Defective von Willebrand Factor binding to the interstitial collagen

AU - Komorowicz, Erzsebet

AU - McBane, Robert D.

AU - Charlesworth, Jon

AU - Fass, David N.

PY - 2002

Y1 - 2002

N2 - 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.

AB - 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.

KW - Adhesion

KW - Collagen

KW - Media

KW - Platelet

KW - Willebrand

UR - http://www.scopus.com/inward/record.url?scp=0036214730&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0036214730&partnerID=8YFLogxK

M3 - Article

VL - 87

SP - 763

EP - 770

JO - Thrombosis and Haemostasis

JF - Thrombosis and Haemostasis

SN - 0340-6245

IS - 4

ER -