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  The spatial molecular pattern of integrin recognition sites and their immobilization to colloidal nanobeads determine α2β1 integrin-dependent platelet activation

Martins Lima, A., Wegner, S., Martins Cavaco, A. C., Estevao-Costa, M. I., Sanz-Soler, R., Niland, S., et al. (2018). The spatial molecular pattern of integrin recognition sites and their immobilization to colloidal nanobeads determine α2β1 integrin-dependent platelet activation. Biomaterials, 167, 107-120. doi:10.1016/j.biomaterials.2018.03.028.

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Item Permalink: http://hdl.handle.net/21.11116/0000-0000-EE99-8 Version Permalink: http://hdl.handle.net/21.11116/0000-0001-DB56-8
Genre: Journal Article

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Biomaterials_167_2018_107.pdf (Any fulltext), 4MB
 
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 Creators:
Martins Lima, Augusto, Author
Wegner, Seraphine, Author              
Martins Cavaco, Ana C., Author
Estevao-Costa, Maria Inacia, Author
Sanz-Soler, Raquel, Author
Niland, Stephan, Author
Nosov, Georgii, Author
Klingauf, Jürgen, Author
Spatz, Joachim P.1, 2, Author              
Eble, Johannes, Author
Affiliations:
1Cellular Biophysics, Max Planck Institute for Medical Research, Max Planck Society, ou_2364731              
2Biophysical Chemistry, Institute of Physical Chemistry, University of Heidelberg, 69120 Heidelberg, Germany, ou_persistent22              

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Free keywords: Platelet signaling; Platelet activation; Integrin α2β1 cluster; Nanopatterning; Biofunctionalized nanobeads and nano-sized membrane protein clusters
 Abstract: Collagen, a strong platelet activator, is recognized by integrin α2β1 and GPVI. It induces aggregation, if added to suspended platelets, or platelet adhesion if immobilized to a surface. The recombinant non-prolylhydroxylated mini-collagen FC3 triple helix containing one α2β1 integrin binding site is a tool to specifically study how α2β1 integrin activates platelet. Whereas soluble FC3 monomers antagonistically block collagen-induced platelet activation, immobilization of several FC3 molecules to an interface or to colloidal nanobeads determines the agonistic action of FC3. Nanopatterning of FC3 reveals that intermolecular distances below 64 nm between α2β1 integrin binding sites trigger signaling through dot-like clusters of α2β1 integrin, which are visible in high resolution microscopy with dSTORM. Upon signaling, these integrin clusters increase in numbers per platelet, but retain their individual size. Immobilization of several FC3 to 100 nm-sized nanobeads identifies α2β1 integrin-triggered signaling in platelets to occur at a twentyfold slower rate than collagen, which activates platelet in a fast integrative signaling via different platelet receptors. As compared to collagen stimulation, FC3-nanobead-triggered signaling cause a significant stronger activation of the protein kinase BTK, a weak and dispensable activation of PDK1, as well as a distinct phosphorylation pattern of PDB/Akt.

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Language(s): eng - English
 Dates: 2018-03-022017-10-222018-03-142018-03-162018-06-01
 Publication Status: Published in print
 Pages: 4
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Degree: -

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Title: Biomaterials
Source Genre: Journal
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Publ. Info: Guildford, England : Elsevier
Pages: - Volume / Issue: 167 Sequence Number: - Start / End Page: 107 - 120 Identifier: ISSN: 0142-9612
CoNE: https://pure.mpg.de/cone/journals/resource/954925472369