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  Tuning RGD motif and hyaluronan density to study integrin binding

Zapp, C., Baykal Minsky, B., & Böhm, H. (2018). Tuning RGD motif and hyaluronan density to study integrin binding. Frontiers in Physiology, 1022(9), 1-8. doi:10.3389/fphys.2018.01022.

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Item Permalink: http://hdl.handle.net/21.11116/0000-0002-1B5E-8 Version Permalink: http://hdl.handle.net/21.11116/0000-0002-79BA-5
Genre: Journal Article

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FrontPsychol_1022_2018_1.pdf (Any fulltext), 2MB
 
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 Creators:
Zapp, Cornelia1, 2, Author
Baykal Minsky, Burcu1, 2, Author              
Böhm, Heike1, 2, Author              
Affiliations:
1Biophysical Chemistry, Institute of Physical Chemistry, University of Heidelberg, 69120 Heidelberg, Germany, ou_persistent22              
2Cellular Biophysics, Max Planck Institute for Medical Research, Max Planck Society, ou_2364731              

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Free keywords: QCM-D; cell adhesion; hyaluronan; integrins; proteoliposomes
 Abstract: Well-controlled surfaces with immobilized substrates enable novel approaches to investigate specific aspects of biological processes related to cell adhesion or motility. A subset of integrins, cellular transmembrane glycoproteins, recognize the evolutionarily conserved tripeptide sequence RGD, and anchor cells to their surrounding proteins as well as mediate bidirectional signaling. In this study, the main question was how co-presentation of hyaluronan (HA), an essential component of the extracellular matrix (ECM), and the RGD motif affect integrin binding. We report a method to prepare self-assembled monolayers on gold surfaces, co-presenting the cell adhesive RGD motif and small HA molecules, to investigate integrin containing proteoliposome binding. This technique enables an independent adjustment of the RGD motif and HA density while maintaining a passivating background: Layer formation and subsequent interactions with αIIbβ3 integrins, which are reconstituted in liposomes, was monitored by label-free quartz crystal microbalance with dissipation monitoring (QCM-D). Exceeding a critical RGD motif density of 40% results in enhanced binding of proteoliposomes. Co-presentation studies with varying HA and constant RGD motif density demonstrate that marginal amounts of HA are sufficient to prevent integrin binding. These findings are of specific importance in relation to cancer cell microenvironments, which show highly enriched HA in the surrounding ECM to reduce adhesion properties.

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Language(s): eng - English
 Dates: 2018-02-222018-07-102018-08-072018-08-07
 Publication Status: Published in print
 Pages: 8
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
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Title: Frontiers in Physiology
  Other : Front. Physiol.
  Abbreviation : FPHYS
Source Genre: Journal
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Publ. Info: Lausanne : Frontiers Research Foundation
Pages: - Volume / Issue: 1022 (9) Sequence Number: - Start / End Page: 1 - 8 Identifier: ISSN: 1664-042X
CoNE: https://pure.mpg.de/cone/journals/resource/1664-042X