TY - JOUR
T1 - Single-molecule analysis of cadherin-mediated cell-cell adhesion
AU - Panorchan, Porntula
AU - Thompson, Melissa S.
AU - Davis, Kelly J.
AU - Tseng, Yiider
AU - Konstantopoulos, Konstantinos
AU - Wirtz, Denis
PY - 2006/1/1
Y1 - 2006/1/1
N2 - Cadherins are ubiquitous cell surface molecules that are expressed in virtually all solid tissues and localize at sites of cell-cell contact. Cadherins form a large and diverse family of adhesion molecules, which play a crucial role in a multitude of cellular processes, including cell-cell adhesion, motility, and cell sorting in maturing organs and tissues, presumably because of their different binding capacity and specificity. Here, we develop a method that probes the biochemical and biophysical properties of the binding interactions between cadherins expressed on the surface of living cells, at the single-molecule level. Single-molecule force spectroscopy reveals that classical cadherins, N-cadherin and E-cadherin, form bonds that display adhesion specificity, and a pronounced difference in adhesion force and reactive compliance, but not in bond lifetime. Moreover, their potentials of interaction, derived from force-spectroscopy measurements, are qualitatively different when comparing the single-barrier energy potential for the dissociation of an N-cadherin-N-cadherin bond with the double-barrier energy potential for an E-cadherin-E-cadherin bond. Together these results suggest that N-cadherin and E-cadherin molecules form homophilic bonds between juxtaposed cells that have significantly different kinetic and micromechanical properties.
AB - Cadherins are ubiquitous cell surface molecules that are expressed in virtually all solid tissues and localize at sites of cell-cell contact. Cadherins form a large and diverse family of adhesion molecules, which play a crucial role in a multitude of cellular processes, including cell-cell adhesion, motility, and cell sorting in maturing organs and tissues, presumably because of their different binding capacity and specificity. Here, we develop a method that probes the biochemical and biophysical properties of the binding interactions between cadherins expressed on the surface of living cells, at the single-molecule level. Single-molecule force spectroscopy reveals that classical cadherins, N-cadherin and E-cadherin, form bonds that display adhesion specificity, and a pronounced difference in adhesion force and reactive compliance, but not in bond lifetime. Moreover, their potentials of interaction, derived from force-spectroscopy measurements, are qualitatively different when comparing the single-barrier energy potential for the dissociation of an N-cadherin-N-cadherin bond with the double-barrier energy potential for an E-cadherin-E-cadherin bond. Together these results suggest that N-cadherin and E-cadherin molecules form homophilic bonds between juxtaposed cells that have significantly different kinetic and micromechanical properties.
KW - Biophysics
KW - Cadherins
KW - Cell adhesion
KW - Single-molecule force spectroscopy
UR - http://www.scopus.com/inward/record.url?scp=31644449928&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=31644449928&partnerID=8YFLogxK
U2 - 10.1242/jcs.02719
DO - 10.1242/jcs.02719
M3 - Article
C2 - 16371651
AN - SCOPUS:31644449928
SN - 0021-9533
VL - 119
SP - 66
EP - 74
JO - Journal of cell science
JF - Journal of cell science
IS - 1
ER -