Description: Margination and stretching of von Willebrand factor in the blood stream enable adhesion

This title appears in the Scientific Report : 2017

Margination and stretching of von Willebrand factor in the blood stream enable adhesion

The protein von Willebrand factor (VWF) is essential in primary hemostasis, as it mediates platelet adhesion to vessel walls. VWF retains its compact (globule-like) shape in equilibrium due to internal molecular associations, but is able to stretch when a high enough shear stress is applied. Even th...

Personal Name(s):	Rack, Kathrin
	Huck, Volker / Hoore, Masoud / Fedosov, Dmitry A. (Corresponding author) / Schneider, Stefan W. / Gompper, Gerhard
Contributing Institute:	Theorie der Weichen Materie und Biophysik; ICS-2 JARA - HPC; JARA-HPC
Published in:	Scientific reports, 7 (2017) 1, S. 14278
Imprint:	London Nature Publishing Group 2017
PubMed ID:	29079767
DOI:	10.1038/s41598-017-14346-4
Document Type:	Journal Article
Research Program:	Margination and Adhesion of Particles and Cells in Blood Flow Physical Basis of Diseases
Link:	OpenAccess OpenAccess
	Publikationsportal JuSER

Please use the identifier: http://hdl.handle.net/2128/15832 in citations.
Please use the identifier: http://dx.doi.org/10.1038/s41598-017-14346-4 in citations.

The protein von Willebrand factor (VWF) is essential in primary hemostasis, as it mediates platelet adhesion to vessel walls. VWF retains its compact (globule-like) shape in equilibrium due to internal molecular associations, but is able to stretch when a high enough shear stress is applied. Even though the shear-flow sensitivity of VWF conformation is well accepted, the behavior of VWF under realistic blood flow conditions remains poorly understood. We perform mesoscopic numerical simulations together with microfluidic experiments in order to characterize VWF behavior in blood flow for a wide range of flow-rate and hematocrit conditions. In particular, our results demonstrate that the compact shape of VWF is important for its migration (or margination) toward vessel walls and that VWF stretches primarily in a near-wall region in blood flow making its adhesion possible. Our results show that VWF is a highly optimized protein in terms of its size and internal associations which are necessary to achieve its vital function. A better understanding of the relevant mechanisms for VWF behavior in microcirculation provides a further step toward the elucidation of the role of mutations in various VWF-related diseases.