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Homophilic and heterophilic cadherin bond rupture forces in homo- or hetero-cellular systems measured by AFM-based single-cell force spectroscopy.
| Content Provider | Europe PMC |
|---|---|
| Author | Viji Babu, Prem Kumar Mirastschijski, Ursula Belge, Ganzanfer Radmacher, Manfred |
| Abstract | Cadherins enable intercellular adherens junctions to withstand tensile forces in tissues, e.g. generated by intracellular actomyosin contraction. In-vitro single molecule force spectroscopy experiments can reveal cadherin–cadherin extracellular region binding dynamics such as bond formation and strength. However, characterization of cadherin-presenting cell homophilic and heterophilic binding in the proteins’ native conformational and functional states in living cells has rarely been done. Here, we used atomic force microscopy (AFM) based single-cell force spectroscopy (SCFS) to measure rupture forces of homophilic and heterophilic bond formation of N- (neural), OB- (osteoblast) and E- (epithelial) cadherins in living fibroblast and epithelial cells in homo- and hetero-cellular arrangements, i.e., between cells and cadherins of the same and different types. In addition, we used indirect immunofluorescence labelling to study and correlate the expression of these cadherins in intercellular adherens junctions. We showed that N/N and E/E-cadherin homophilic binding events are stronger than N/OB heterophilic binding events. Disassembly of intracellular actin filaments affects the cadherin bond rupture forces suggesting a contribution of actin filaments in cadherin extracellular binding. Inactivation of myosin did not affect the cadherin rupture force in both homo- and hetero-cellular arrangements, but particularly strengthened the N/OB heterophilic bond and reinforced the other cadherins’ homophilic bonds.Supplementary InformationThe online version contains supplementary material available at 10.1007/s00249-021-01536-2. |
| Related Links | https://europepmc.org/backend/ptpmcrender.fcgi?accid=PMC8190030&blobtype=pdf |
| ISSN | 01757571 |
| Journal | European Biophysics Journal [Eur Biophys J] |
| Volume Number | 50 |
| DOI | 10.1007/s00249-021-01536-2 |
| PubMed Central reference number | PMC8190030 |
| Issue Number | 3-4 |
| PubMed reference number | 33880610 |
| e-ISSN | 14321017 |
| Language | English |
| Publisher | Springer International Publishing |
| Publisher Date | 2021-04-20 |
| Publisher Place | Gewerbestrasse 11, Cham, Ch 6330, Switzerland |
| Access Restriction | Open |
| Rights License | Open AccessThis article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/. © The Author(s) 2021 |
| Subject Keyword | Cadherins Actomyosin contraction Atomic force microscopy Single-cell force spectroscopy Fibroblast Epithelial cell |
| Content Type | Text |
| Resource Type | Article |
| Subject | Medicine Biophysics |
