Accuri C6 Flow Cytometer System
Originally published online as doi:10.1189/jlb.0906553 on December 12, 2006

Published online before print December 12, 2006
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(Journal of Leukocyte Biology. 2007;81:686-695.)
© 2007 by Society for Leukocyte Biology

Transendothelial migration enhances integrin-dependent human neutrophil chemokinesis

Anjelica L. Gonzalez*, Wafa El-Bjeirami*, Jennifer L. West{dagger}, Larry V. McIntire{ddagger} and C. Wayne Smith*

* Section of Leukocyte Biology, Department of Pediatrics, Baylor College of Medicine, Houston, Texas, USA;
{dagger} Department of Bioengineering, Rice University, Houston, Texas, USA; and
{ddagger} Coulter Department of Biomedical Engineering, Georgia Institute of Technology/Emory University, Atlanta, Georgia, USA

1 Correspondence: Baylor College of Medicine, Leukocyte Biology, 1100 Bates, Suite 6014, Houston, TX 77030-2600, USA. E-mail: cwsmith{at}bcm.tmc.edu

Transendothelial migration of neutrophils induces phenotypic changes that influence the interactions of neutrophils with extravascular tissue components. To assess the influence of transmigration on neutrophil chemokinetic motility, we used polyethylene glycol hydrogels covalently modified with specific peptide sequences relevant to extracellular matrix proteins. We evaluated fMLP-stimulated human neutrophil motility on peptides Arg-Gly-Asp-Ser (RGDS) and TMKIIPFNRTLIGG (P2), alone and in combination. RGDS is a bioactive sequence found in a number of proteins, and P2 is a membrane-activated complex-1 (Mac-1) ligand located in the {gamma}-chain of the fibrinogen protein. We evaluated, via video microscopy, cell motility by measuring cell displacement from origin and total accumulated distance traveled and then calculated average velocity. Results indicate that although adhesion and shape change were supported by hydrogels containing RGD alone, motility was not. Mac-1-dependent motility was supported on hydrogels containing P2 alone. Motility was enhanced through combined presentation of RGD and P2, engaging Mac-1, {alpha}Vß3, and ß1 integrins. Naïve neutrophil motility on combined peptide substrates was dependent on Mac-1, and {alpha}4ß1 while {alpha}6ß1 contributed to speed and linear movement. Transmigrated neutrophil motility was dependent on {alpha}vß3 and {alpha}5ß1, and {alpha}4ß1, {alpha}6ß1, and Mac-1 contributed to speed and linear motion. Together, the data demonstrate that efficient neutrophil migration, dependent on multi-integrin interaction, is enhanced after transendothelial migration.

Key Words: transmigration • ß1 integrins • inflammation • extracellular matrix • motility • ß2 integrin




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