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

Article Details

Citation

Cascone I, Audero E, Giraudo E, Napione L, Maniero F, Philips MR, Collard JG, Serini G, Bussolino F

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

Blood. 2003 Oct 1;102(7):2482-90. Epub 2003 Jun 19.

PubMed ID
12816861 [ View in PubMed
]
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 sevenless-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.

DrugBank Data that Cites this Article

Polypeptides
NameUniProt ID
Angiopoietin-1 receptorQ02763Details