Abstract
Weassess the cross-reactivity of both cellular as well as recombinant E- and N-cadherins using functionalized bead arrays assembled on atomic-force-microscope cantilevers. This new approach builds upon and enhances the utility of a recently developed force probe that integrates a custom-built, horizontal atomic force microscope with micropipette manipulation. It enables us to test multiple biomolecular interactions of the same cell in a swift sequential or cyclic manner and thus to resolve subtle differences between individual interactions that otherwise would be obscured by cell-cell baseline variability. For each cell, we contrast heterophilic E:N-cadherin binding with the respectiv homophilic bonds and with a suitable control. Clarifying previous literature reports, we establish that specific bonds between E- and N-cadherins form readily, albeit less frequently than homophilic bonds of either cadherin. We support this assessment with a rough estimate of the ratio of on-rate constants of E/N-cadherin binding.
| Original language | English (US) |
|---|---|
| Journal | Biophysical Journal |
| Volume | 99 |
| Issue number | 12 |
| DOIs | |
| State | Published - Dec 15 2010 |
Fingerprint
ASJC Scopus subject areas
- Biophysics
Cite this
Single-cell adhesion tests against functionalized microspheres arrayed on AFM cantilevers confirm heterophilic E- and N-cadherin binding. / Ounkomol, Chawin; Yamada, Soichiro; Heinrich, Volkmar.
In: Biophysical Journal, Vol. 99, No. 12, 15.12.2010.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Single-cell adhesion tests against functionalized microspheres arrayed on AFM cantilevers confirm heterophilic E- and N-cadherin binding
AU - Ounkomol, Chawin
AU - Yamada, Soichiro
AU - Heinrich, Volkmar
PY - 2010/12/15
Y1 - 2010/12/15
N2 - Weassess the cross-reactivity of both cellular as well as recombinant E- and N-cadherins using functionalized bead arrays assembled on atomic-force-microscope cantilevers. This new approach builds upon and enhances the utility of a recently developed force probe that integrates a custom-built, horizontal atomic force microscope with micropipette manipulation. It enables us to test multiple biomolecular interactions of the same cell in a swift sequential or cyclic manner and thus to resolve subtle differences between individual interactions that otherwise would be obscured by cell-cell baseline variability. For each cell, we contrast heterophilic E:N-cadherin binding with the respectiv homophilic bonds and with a suitable control. Clarifying previous literature reports, we establish that specific bonds between E- and N-cadherins form readily, albeit less frequently than homophilic bonds of either cadherin. We support this assessment with a rough estimate of the ratio of on-rate constants of E/N-cadherin binding.
AB - Weassess the cross-reactivity of both cellular as well as recombinant E- and N-cadherins using functionalized bead arrays assembled on atomic-force-microscope cantilevers. This new approach builds upon and enhances the utility of a recently developed force probe that integrates a custom-built, horizontal atomic force microscope with micropipette manipulation. It enables us to test multiple biomolecular interactions of the same cell in a swift sequential or cyclic manner and thus to resolve subtle differences between individual interactions that otherwise would be obscured by cell-cell baseline variability. For each cell, we contrast heterophilic E:N-cadherin binding with the respectiv homophilic bonds and with a suitable control. Clarifying previous literature reports, we establish that specific bonds between E- and N-cadherins form readily, albeit less frequently than homophilic bonds of either cadherin. We support this assessment with a rough estimate of the ratio of on-rate constants of E/N-cadherin binding.
UR - http://www.scopus.com/inward/record.url?scp=78650205710&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=78650205710&partnerID=8YFLogxK
U2 - 10.1016/j.bpj.2010.11.013
DO - 10.1016/j.bpj.2010.11.013
M3 - Article
C2 - 21156120
AN - SCOPUS:78650205710
VL - 99
JO - Biophysical Journal
JF - Biophysical Journal
SN - 0006-3495
IS - 12
ER -