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Fast dissociation kinetics between individual E-cadherin fragments revealed by flow chamber analysis

By Emilie Perret, Anne-Marie Benoliel, Pierre Nassoy, Anne Pierres, Véronique Delmas, Jean-Paul Thiery, Pierre Bongrand and Hélène Feracci

Abstract

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

Topics: Article
Publisher: Oxford University Press
Year: 2002
DOI identifier: 10.1093/emboj/21.11.2537
OAI identifier: oai:pubmedcentral.nih.gov:126034
Provided by: PubMed Central
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