Autoinhibitory module underlies species difference in shear activation of von Willebrand factor.

ABSTRACT:

Background

Von Willebrand factor (VWF) is a multimeric plasma protein that bridges the gap between vessel injury and platelet capture at high shear rates. Under high shear or tension, VWF can become activated upon the unfolding of its autoinhibitory module (AIM). AIM unfolding exposes the A1 domain, allowing for binding to platelet glycoprotein (GP)Ibα to initiate primary hemostasis. The characteristics of the AIM and its inhibitory properties within mouse VWF are unknown.

Objectives

To determine and characterize the autoinhibitory properties of mouse VWF.

Methods

Recombinant mouse VWF A1 fragments containing or lacking the flanking regions around the A1 domain were generated. We tested the ability of these fragments to bind to human or mouse GPIbα and platelets. We c

SUBMITTER: Arce NA 

PROVIDER: S-EPMC9588639 | biostudies-literature | 2022 Nov

REPOSITORIES: biostudies-literature