Development of an in vitro technique for examining catch bond behavior of integrin receptors
Stanley, Brandon T.
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Previous research has shown catch bonds to be critical as bond lifetime regulators between integrin receptors and ligands. These adhesive mechanisms prolong the bond lifetimes of specific molecules with an increasing applied force. Characterizing catch bond behavior may be helpful in explaining how the body regulates the activity of white blood cells. These cells must flow freely, but attach to injury sites within blood vessels. To analyze catch bond behavior in groups of receptors, we plan to develop a technique to examine the catch-bond behavior of groups of α5β1 integrin molecules. A chimeric α5β1 integrin-Fc molecule, which presents the integrin binding domain at one end of the molecule and the human Fc portion of an antibody at the other end, will be used as the bead-bound receptor while fibronectin and various mutations of the molecule will be used as the surface-bound ligand. This experimental platform will allow the analysis of catch-bond behavior in a well-defined cell-free model system.