Elongated Membrane Tethers, Individually Anchored by High Affinity α4β1/VCAM-1 Complexes, Are the Quantal Units of Monocyte Arrests

Calvin Chu, Emrah Celik, Felix Rico, Vincent T. Moy

Research output: Contribution to journalArticlepeer-review

17 Scopus citations

Abstract

The α4β1 integrin facilitates both monocyte rolling and adhesion to the vascular endothelium and is physiologically activated by monocyte chemoattractant protein (MCP-1). The current study investigated the initial events in the adhesion of THP-1 cells to immobilized Vascular Cell Adhesion Molecule 1 (VCAM-1). Using AFM force measurements, cell adhesion was shown to be mediated by two populations of α4β1/VCAM-1 complexes. A low affinity form of α4β1 was anchored to the elastic elements of the cytoskeleton, while a higher affinity conformer was coupled to the viscous elements of the cell membrane. Within 100 ms of contact, THP-1 cells, stimulated by co-immobilized MCP-1, exhibited a tremendous increase in adhesion to VCAM-1. Enhanced cell adhesion was accompanied by a local decoupling of the cell membrane from the cytoskeleton and the formation of long membrane tethers. The tethers were individually anchored by multiple α4β1/VCAM-1 complexes that prolonged the extension of the viscous tethers. In vivo, the formation of these membrane tethers may provide the quantal structural units for the arrest of rolling monocytes within the blood vessels.

Original languageEnglish (US)
Article numbere64187
JournalPloS one
Volume8
Issue number5
DOIs
StatePublished - May 17 2013

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)
  • Agricultural and Biological Sciences(all)
  • General

Fingerprint Dive into the research topics of 'Elongated Membrane Tethers, Individually Anchored by High Affinity α<sub>4</sub>β<sub>1</sub>/VCAM-1 Complexes, Are the Quantal Units of Monocyte Arrests'. Together they form a unique fingerprint.

Cite this