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Platelets drive fibronectin fibrillogenesis using integrin αIIbβ3
Platelets interact with multiple adhesion proteins during thrombogenesis, yet little is known about their ability to assemble fibronectin matrix. In vitro three-dimensional superresolution microscopy complemented by biophysical and biochemical methods revealed fundamental insights into how platelet...
Autores principales: | , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Association for the Advancement of Science
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8916723/ https://www.ncbi.nlm.nih.gov/pubmed/35275711 http://dx.doi.org/10.1126/sciadv.abj8331 |
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author | Lickert, Sebastian Kenny, Martin Selcuk, Kateryna Mehl, Johanna L. Bender, Markus Früh, Susanna M. Burkhardt, Melanie A. Studt, Jan-Dirk Nieswandt, Bernhard Schoen, Ingmar Vogel, Viola |
author_facet | Lickert, Sebastian Kenny, Martin Selcuk, Kateryna Mehl, Johanna L. Bender, Markus Früh, Susanna M. Burkhardt, Melanie A. Studt, Jan-Dirk Nieswandt, Bernhard Schoen, Ingmar Vogel, Viola |
author_sort | Lickert, Sebastian |
collection | PubMed |
description | Platelets interact with multiple adhesion proteins during thrombogenesis, yet little is known about their ability to assemble fibronectin matrix. In vitro three-dimensional superresolution microscopy complemented by biophysical and biochemical methods revealed fundamental insights into how platelet contractility drives fibronectin fibrillogenesis. Platelets adhering to thrombus proteins (fibronectin and fibrin) versus basement membrane components (laminin and collagen IV) pull fibronectin fibrils along their apical membrane versus underneath their basal membrane, respectively. In contrast to other cell types, platelets assemble fibronectin nanofibrils using αIIbβ3 rather than α5β1 integrins. Apical fibrillogenesis correlated with a stronger activation of integrin-linked kinase, higher platelet traction forces, and a larger tension in fibrillar-like adhesions compared to basal fibrillogenesis. Our findings have potential implications for how mechanical thrombus integrity might be maintained during remodeling and vascular repair. |
format | Online Article Text |
id | pubmed-8916723 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | American Association for the Advancement of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-89167232022-03-21 Platelets drive fibronectin fibrillogenesis using integrin αIIbβ3 Lickert, Sebastian Kenny, Martin Selcuk, Kateryna Mehl, Johanna L. Bender, Markus Früh, Susanna M. Burkhardt, Melanie A. Studt, Jan-Dirk Nieswandt, Bernhard Schoen, Ingmar Vogel, Viola Sci Adv Biomedicine and Life Sciences Platelets interact with multiple adhesion proteins during thrombogenesis, yet little is known about their ability to assemble fibronectin matrix. In vitro three-dimensional superresolution microscopy complemented by biophysical and biochemical methods revealed fundamental insights into how platelet contractility drives fibronectin fibrillogenesis. Platelets adhering to thrombus proteins (fibronectin and fibrin) versus basement membrane components (laminin and collagen IV) pull fibronectin fibrils along their apical membrane versus underneath their basal membrane, respectively. In contrast to other cell types, platelets assemble fibronectin nanofibrils using αIIbβ3 rather than α5β1 integrins. Apical fibrillogenesis correlated with a stronger activation of integrin-linked kinase, higher platelet traction forces, and a larger tension in fibrillar-like adhesions compared to basal fibrillogenesis. Our findings have potential implications for how mechanical thrombus integrity might be maintained during remodeling and vascular repair. American Association for the Advancement of Science 2022-03-11 /pmc/articles/PMC8916723/ /pubmed/35275711 http://dx.doi.org/10.1126/sciadv.abj8331 Text en Copyright © 2022 The Authors, some rights reserved; exclusive licensee American Association for the Advancement of Science. No claim to original U.S. Government Works. Distributed under a Creative Commons Attribution NonCommercial License 4.0 (CC BY-NC). https://creativecommons.org/licenses/by-nc/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution-NonCommercial license (https://creativecommons.org/licenses/by-nc/4.0/) , which permits use, distribution, and reproduction in any medium, so long as the resultant use is not for commercial advantage and provided the original work is properly cited. |
spellingShingle | Biomedicine and Life Sciences Lickert, Sebastian Kenny, Martin Selcuk, Kateryna Mehl, Johanna L. Bender, Markus Früh, Susanna M. Burkhardt, Melanie A. Studt, Jan-Dirk Nieswandt, Bernhard Schoen, Ingmar Vogel, Viola Platelets drive fibronectin fibrillogenesis using integrin αIIbβ3 |
title | Platelets drive fibronectin fibrillogenesis using integrin αIIbβ3 |
title_full | Platelets drive fibronectin fibrillogenesis using integrin αIIbβ3 |
title_fullStr | Platelets drive fibronectin fibrillogenesis using integrin αIIbβ3 |
title_full_unstemmed | Platelets drive fibronectin fibrillogenesis using integrin αIIbβ3 |
title_short | Platelets drive fibronectin fibrillogenesis using integrin αIIbβ3 |
title_sort | platelets drive fibronectin fibrillogenesis using integrin αiibβ3 |
topic | Biomedicine and Life Sciences |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8916723/ https://www.ncbi.nlm.nih.gov/pubmed/35275711 http://dx.doi.org/10.1126/sciadv.abj8331 |
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