Abstract
We studied the mechanical strength of the adhesion of living cells to model membranes. The latter contained a RGD lipopeptide which is a high affinity binding site for a cell adhesion molecule (integrin alpha(V)beta(3)). Cells adhered specifically to the vesicles. We used micropipette aspiration for breaking this adhesion with well defined forces. Systematic variation of the rate of force application revealed pronounced kinetic effects. The dependence of the detachment forces on the loading rate was well described by a power law (exponent approximately 0.4), in agreement with recent theoretical work.
Publication types
-
Research Support, Non-U.S. Gov't
MeSH terms
-
Binding Sites
-
Cell Adhesion / physiology*
-
Cells, Cultured
-
Collagen
-
Endothelium, Vascular / cytology
-
Endothelium, Vascular / metabolism
-
Humans
-
Kinetics
-
Lipoproteins / chemistry
-
Lipoproteins / metabolism
-
Membranes, Artificial*
-
Molecular Mimicry
-
Oligopeptides / chemistry
-
Oligopeptides / metabolism
-
Receptors, Vitronectin / chemistry
-
Receptors, Vitronectin / metabolism*
-
Spectrum Analysis / methods
-
Tensile Strength
-
Vitronectin / chemistry
-
Vitronectin / metabolism*
Substances
-
Lipoproteins
-
Membranes, Artificial
-
Oligopeptides
-
Receptors, Vitronectin
-
Vitronectin
-
arginyl-glycyl-aspartic acid
-
Collagen