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

Authors: Perret, E  Benoliel, AM  Nassoy, P  Pierres, A  Delmas, V  Thiery, JP  Bongrand, P  Feracci, H 
Citation: Perret E, etal., EMBO J 2002 Jun 3;21(11):2537-46.
Pubmed: (View Article at PubMed) PMID:12032067
DOI: Full-text: DOI:10.1093/emboj/21.11.2537

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.


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RGD Object Information
RGD ID: 632467
Created: 2003-08-29
Species: All species
Last Modified: 2006-04-25
Status: ACTIVE


RGD is funded by grant HL64541 from the National Heart, Lung, and Blood Institute on behalf of the NIH.