Fast dissociation kinetics between individual E-cadherin fragments revealed by flow chamber analysis.
E-cadherin is the predominant adhesion molecule of epithelia. The interaction between extracellular segments of E-cadherin in the membrane of opposing cells is homophilic and calcium dependent. Whereas it is widely accepted that the specificity of the adhesive interaction is localized to the N-terminal domain, the kinetics of the recognition process are unknown. We report the first quantitative data describing the dissociation kinetics of individual E-cadherin interactions. Aggregation assays indicate that the two outermost domains of E-cadherin (E/EC1-2) retain biological activity when chemically immobilized on glass beads. Cadherin fragment trans-interaction was analysed using a flow chamber technique. Transient tethers had first-order kinetics, suggesting a unimolecular interaction. The unstressed lifetime of individual E-cadherin interactions was as brief as 2 s. A fast off rate and the low tensile strength of the E-cadherin bond may be necessary to support the high selectivity and plasticity of epithelial cell interactions.
Perret
Emilie
E
Laboratoire de Morphogenèse Cellulaire et Différenciation Tumorale, UMR 144, CNRS/Institut Curie, 26 rue d'Ulm, F-75248 Paris Cedex 05, France.
Benoliel
Anne-Marie
AM
Nassoy
Pierre
P
Pierres
Anne
A
Delmas
Véronique
V
Thiery
Jean-Paul
JP
Bongrand
Pierre
P
Feracci
Hélène
H
D000818:Animals; D001665:Binding Sites; D015820:Cadherins / Q000737:chemistry* / Q000378:metabolism; D002448:Cell Adhesion; D004847:Epithelial Cells / Q000378:metabolism; D007700:Kinetics; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D051381:Rats; D011994:Recombinant Proteins / Q000737:chemistry; D013379:Substrate Specificity; D013997:Time Factors; D014407:Tumor Cells, Cultured
D015820:Cadherins; D011994:Recombinant Proteins