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Receptor-cytoskeletal unbinding in detachment of P-selectin from PSGL-1 on leukocytes

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3 Author(s)
Evans, E. ; Dept. of Biomed. Eng. & Phys., Boston Univ., MA, USA ; Heinrich, V. ; Leung, A.

Using a biomembrane force probe decorated with P-selectin, discrete bonds were formed to PSGL-1 receptors on PMN surfaces and detached at speeds from ∼1 - 100 μm/sec. High resolution tracking of the distance between probe tip and PMN revealed an initial elastic deformation that was either terminated by abrupt detachment or interrupted by yield and fluid-like extrusion of a macroscale tether plus subsequent detachment. Selecting tests that exhibited first yield then a single detachment step, we were able to quantify cohesive strengths between single PSGL-1 receptors and the PMN cytoskeleton. Prior to yield, the constant force rate was set by elastic stiffness (∼0.25 pN/nm) of the cytostructure and the pulling speed. Collected at rates over a span from 265 pN/sec to 38000 pN/sec, distributions of yield forces were found to agree precisely with probability densities for rupture of a single bond defined by a spontaneous dissociation rate of ∼0.5/sec and an energy barrier projected at ∼0.25 nm along the direction of force. By comparison, single P-selectin bonds to PSGL-1 covalently attached to microspheres were slightly stronger at all loading rates as characterized by a spontaneous dissociation rate of ∼0.15/sec and an energy barrier projected at ∼0.22 nm. Weaker anchoring to the cytoskeleton implies frequent tether formation that can reduce the hydrodynamic load applied to selectin bonds and prolog PMN attachments to vessel walls under conditions of flow.

Published in:

Engineering in Medicine and Biology, 2002. 24th Annual Conference and the Annual Fall Meeting of the Biomedical Engineering Society EMBS/BMES Conference, 2002. Proceedings of the Second Joint  (Volume:1 )

Date of Conference:

2002

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