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Differential surface activation of the A1 domain of von Willebrand factor
The clotting protein von Willebrand factor (VWF) binds to platelet receptor glycoprotein Ibα (GPIbα) when VWF is activated by chemicals, high shear stress, or immobilization onto surfaces. Activation of VWF by surface immobilization is an important problem in the failure of cardiovascular implants,...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Vacuum Society
2016
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4788635/ https://www.ncbi.nlm.nih.gov/pubmed/26968213 http://dx.doi.org/10.1116/1.4943618 |
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author | Tronic, Elaine H. Yakovenko, Olga Weidner, Tobias Baio, Joe E. Penkala, Rebecca Castner, David G. Thomas, Wendy E. |
author_facet | Tronic, Elaine H. Yakovenko, Olga Weidner, Tobias Baio, Joe E. Penkala, Rebecca Castner, David G. Thomas, Wendy E. |
author_sort | Tronic, Elaine H. |
collection | PubMed |
description | The clotting protein von Willebrand factor (VWF) binds to platelet receptor glycoprotein Ibα (GPIbα) when VWF is activated by chemicals, high shear stress, or immobilization onto surfaces. Activation of VWF by surface immobilization is an important problem in the failure of cardiovascular implants, but is poorly understood. Here, the authors investigate whether some or all surfaces can activate VWF at least in part by affecting the orientation or conformation of the immobilized GPIbα-binding A1 domain of VWF. Platelets binding to A1 adsorbed onto polystyrene surfaces translocated rapidly at moderate and high flow, but detached at low flow, while platelets binding to A1 adsorbed onto glass or tissue-culture treated polystyrene surfaces translocated slowly, and detached only at high flow. Both x-ray photoelectron spectroscopy and conformation independent antibodies reported comparable A1 amounts on all surfaces. Time-of-flight secondary ion mass spectrometry (ToF-SIMS) and near-edge x-ray absorption fine structure spectra suggested differences in orientation on the three surfaces, but none that could explain the biological data. Instead, ToF-SIMS data and binding of conformation-dependent antibodies were consistent with the stabilization of an alternative more activated conformation of A1 by tissue culture polystyrene and especially glass. These studies demonstrate that different material surfaces differentially affect the conformation of adsorbed A1 domain and its biological activity. This is important when interpreting or designing in vitro experiments with surface-adsorbed A1 domain, and is also of likely relevance for blood-contacting biomaterials. |
format | Online Article Text |
id | pubmed-4788635 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | American Vacuum Society |
record_format | MEDLINE/PubMed |
spelling | pubmed-47886352016-03-24 Differential surface activation of the A1 domain of von Willebrand factor Tronic, Elaine H. Yakovenko, Olga Weidner, Tobias Baio, Joe E. Penkala, Rebecca Castner, David G. Thomas, Wendy E. Biointerphases In Focus: Blood-Biomaterial Interactions The clotting protein von Willebrand factor (VWF) binds to platelet receptor glycoprotein Ibα (GPIbα) when VWF is activated by chemicals, high shear stress, or immobilization onto surfaces. Activation of VWF by surface immobilization is an important problem in the failure of cardiovascular implants, but is poorly understood. Here, the authors investigate whether some or all surfaces can activate VWF at least in part by affecting the orientation or conformation of the immobilized GPIbα-binding A1 domain of VWF. Platelets binding to A1 adsorbed onto polystyrene surfaces translocated rapidly at moderate and high flow, but detached at low flow, while platelets binding to A1 adsorbed onto glass or tissue-culture treated polystyrene surfaces translocated slowly, and detached only at high flow. Both x-ray photoelectron spectroscopy and conformation independent antibodies reported comparable A1 amounts on all surfaces. Time-of-flight secondary ion mass spectrometry (ToF-SIMS) and near-edge x-ray absorption fine structure spectra suggested differences in orientation on the three surfaces, but none that could explain the biological data. Instead, ToF-SIMS data and binding of conformation-dependent antibodies were consistent with the stabilization of an alternative more activated conformation of A1 by tissue culture polystyrene and especially glass. These studies demonstrate that different material surfaces differentially affect the conformation of adsorbed A1 domain and its biological activity. This is important when interpreting or designing in vitro experiments with surface-adsorbed A1 domain, and is also of likely relevance for blood-contacting biomaterials. American Vacuum Society 2016-03-11 /pmc/articles/PMC4788635/ /pubmed/26968213 http://dx.doi.org/10.1116/1.4943618 Text en © 2016 Author(s). 1934-8630/2016/11(2)/029803/9 All article content, except where otherwise noted, is licensed under a Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | In Focus: Blood-Biomaterial Interactions Tronic, Elaine H. Yakovenko, Olga Weidner, Tobias Baio, Joe E. Penkala, Rebecca Castner, David G. Thomas, Wendy E. Differential surface activation of the A1 domain of von Willebrand factor |
title | Differential surface activation of the A1 domain of von Willebrand
factor |
title_full | Differential surface activation of the A1 domain of von Willebrand
factor |
title_fullStr | Differential surface activation of the A1 domain of von Willebrand
factor |
title_full_unstemmed | Differential surface activation of the A1 domain of von Willebrand
factor |
title_short | Differential surface activation of the A1 domain of von Willebrand
factor |
title_sort | differential surface activation of the a1 domain of von willebrand
factor |
topic | In Focus: Blood-Biomaterial Interactions |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4788635/ https://www.ncbi.nlm.nih.gov/pubmed/26968213 http://dx.doi.org/10.1116/1.4943618 |
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