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Ephrin-A1/EphA4-mediated adhesion of monocytes to endothelial cells.

Authors :
Jellinghaus S
Poitz DM
Ende G
Augstein A
Weinert S
Stütz B
Braun-Dullaeus RC
Pasquale EB
Strasser RH
Source :
Biochimica et biophysica acta [Biochim Biophys Acta] 2013 Oct; Vol. 1833 (10), pp. 2201-11. Date of Electronic Publication: 2013 May 23.
Publication Year :
2013

Abstract

The Eph receptors represent the largest family of receptor tyrosine kinases. Both Eph receptors and their ephrin ligands are cell-surface proteins, and they typically mediate cell-to-cell communication by interacting at sites of intercellular contact. The major aim of the present study was to investigate the involvement of EphA4-ephrin-A1 interaction in monocyte adhesion to endothelial cells, as this process is a crucial step during the initiation and progression of the atherosclerotic plaque. Immunohistochemical analysis of human atherosclerotic plaques revealed expression of EphA4 receptor and ephrin-A1 ligand in major cell types within the plaque. Short-time stimulation of endothelial cells with the soluble ligand ephrin-A1 leads to a fourfold increase in adhesion of human monocytes to endothelial cells. In addition, ephrin-A1 further increases monocyte adhesion to already inflamed endothelial cells. EphrinA1 mediates its effect on monocyte adhesion via the activated receptor EphA4. This ephrinA1/EphA4 induced process involves the activation of the Rho signaling pathway and does not require active transcription. Rho activation downstream of EphA4 leads to increased polymerization of actin filaments in endothelial cells. This process was shown to be crucial for the proadhesive effect of ephrin-A1. The results of the present study show that ephrin-A1-induced EphA4 forward signaling promotes monocyte adhesion to endothelial cells via activation of RhoA and subsequent stress-fiber formation by a non-transcriptional mechanism.<br /> (Copyright © 2013 Elsevier B.V. All rights reserved.)

Details

Language :
English
ISSN :
0006-3002
Volume :
1833
Issue :
10
Database :
MEDLINE
Journal :
Biochimica et biophysica acta
Publication Type :
Academic Journal
Accession number :
23707953
Full Text :
https://doi.org/10.1016/j.bbamcr.2013.05.017