Detection of bidirectional signaling during integrin activation and neutrophil adhesion

Stuart M. Altman, Neha Dixit, Scott I. Simon

Research output: Chapter in Book/Report/Conference proceedingChapter

3 Scopus citations

Abstract

Neutrophil arrest and migration on inflamed endothelium is dependent upon a conformational shift in CD11a/CD18 (LFA-1) from a low to high affinity and clustered state which determines the strength and lifetime of bond formation with intracellular adhesion molecule 1 (ICAM-1). Cytoskeletal adaptor proteins kindlin-3 and talin-1 anchor clustered LFA-1 to the cytoskeleton and support the transition from neutrophil rolling to arrest. We employ microfluidic flow channels and total internal reflection fluorescence microscopy to evaluate the spatiotemporal regulation of LFA-1 affinity and bond formation that facilitate the transition from neutrophil rolling to arrest. Methodology is presented to correlate the relationship between integrin conformation, bond formation with ICAM-1, and cytoskeletal engagement and adhesion strengthening necessary to achieve a migratory phenotype.

Original languageEnglish (US)
Title of host publicationMethods in Molecular Biology
PublisherHumana Press Inc.
Pages235-248
Number of pages14
Volume1124
ISBN (Print)9781627038447
DOIs
StatePublished - 2014

Publication series

NameMethods in Molecular Biology
Volume1124
ISSN (Print)10643745

Keywords

  • Adhesion strengthening
  • Cytoskeleton
  • G-protein coupled receptors
  • ICAM-1
  • Integrin
  • Intercellular adhesion molecule-1
  • Leukocyte function associated protein-1 (LFA-1)
  • Macrophage protein-1 (Mac-1)
  • Selectin

ASJC Scopus subject areas

  • Molecular Biology
  • Genetics

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  • Cite this

    Altman, S. M., Dixit, N., & Simon, S. I. (2014). Detection of bidirectional signaling during integrin activation and neutrophil adhesion. In Methods in Molecular Biology (Vol. 1124, pp. 235-248). (Methods in Molecular Biology; Vol. 1124). Humana Press Inc.. https://doi.org/10.1007/978-1-62703-845-4_15