Tie-2-dependent activation of RhoA and Rac1 participates in endothelial cell motility triggered by angiopoietin-1

Ilaria Cascone, Enrica Audero, Enrico Giraudo, Lucia Napione, Fabrizio Maniero, Mark R. Philips, John G. Collard, Guido Serini, Federico Bussolino

Research output: Contribution to journalArticlepeer-review

Abstract

Angiopoietin-1 is implicated in the maturation and remodeling of the vascular network during embryo development and in adult life. Through its tyrosine kinase receptor Tie-2 it stimulates endothelial cells to migrate and change shape. Here we show that angiopoietin-1 elicits chemokinesis of endothelial cells by a phosphoinositide 3-OH kinase/son of seven-less-dependent modulation of Rac1 and RhoA. The resulting temporal events are associated with cytoskeletal rearrangements and occur in discrete zones of the cell. Endothelial cells carrying dominant-negative mutants of RhoA and Rac1 or treated with LY294002, an inhibitor of phosphoinositide 3-OH kinase, dramatically decrease their chemokinetic velocity. Taken together, these results further expand our understanding of angiopoietin-1-mediated endothelial cell motility during vascular network assembly and angiogenesis.

Original languageEnglish
Pages (from-to)2482-2490
Number of pages9
JournalBlood
Volume102
Issue number7
DOIs
Publication statusPublished - Oct 1 2003

ASJC Scopus subject areas

  • Hematology

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