Homophilic and heterophilic cadherin bond rupture forces in homo- or hetero-cellular systems measured by AFM-based single-cell force spectroscopy
| Autor: | Manfred Radmacher, Ganzanfer Belge, Prem Kumar Viji Babu, Ursula Mirastschijski |
|---|---|
| Rok vydání: | 2020 |
| Předmět: |
0301 basic medicine
Biophysics Microscopy Atomic Force Adherens junction 03 medical and health sciences Atomic force microscopy 0302 clinical medicine Myosin Extracellular medicine Cell Adhesion Actomyosin contraction Fibroblast Actin Mechanical Phenomena Cadherin Chemistry Spectrum Analysis Force spectroscopy Single-cell force spectroscopy General Medicine Cadherins Epithelial cell 030104 developmental biology medicine.anatomical_structure 030220 oncology & carcinogenesis Original Article Intracellular Protein Binding |
| Zdroj: | European Biophysics Journal |
| ISSN: | 1432-1017 |
| Popis: | 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 Information The online version contains supplementary material available at 10.1007/s00249-021-01536-2. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Full text from SpringerLink