Abstract
Angiopoietins 1–4 (Ang1–4) represent an important family of growth factors, whose activities are mediated through the tyrosine kinase receptors, Tie1 and Tie2. The best characterized are angiopoietin-1 (Ang1) and angiopoietin-2 (Ang2). Ang1 is a potent angiogenic growth factor signaling through Tie2, whereas Ang2 was initially identified as a vascular disruptive agent with antagonistic activity through the same receptor. Recent data demonstrates that Ang2 has context-dependent agonist activities. Ang2 plays important roles in physiological processes and the deregulation of its expression is characteristic of several diseases. In this review, we summarize the activity of Ang2 on blood and lymphatic endothelial cells, its significance in human physiology and disease, and provide a current view of the molecular signaling pathways regulated by Ang2 in endothelial cells.
Highlights
Angiopoietin-2 (Ang2) is a growth factor belonging to the angiopoietin/Tie signaling pathway, one of the main pathways involved in angiogenesis
Ang2 was identified through a cDNA library screening, shortly after the identification of angiopoietin-1 (Ang1) [1], a potent angiogenic factor, critical for in vivo angiogenesis, with distinct functions from vascular endothelial growth factor (VEGF) [2]
The aim of this review is to summarize the activity of Ang2 in blood and lymphatic endothelial cells, its different functions in the body under both physiological and pathological conditions, and the main molecular mechanisms identified to date
Summary
Angiopoietin-2 (Ang2) is a growth factor belonging to the angiopoietin/Tie (tyrosine kinase with Ig and EGF homology domains) signaling pathway, one of the main pathways involved in angiogenesis. (Ang1) [1], a potent angiogenic factor, critical for in vivo angiogenesis, with distinct functions from vascular endothelial growth factor (VEGF) [2]. Amino acid homology with Ang and lacks one of the nine cysteines found in mature Ang. Amino acid homology with Ang and lacks one of the nine cysteines found in mature Ang1 It has a secretion signal peptide, an NH2 -terminal coiled-coil domain, and a COOH-terminal fibrinogen-like domain. The aim of this review is to summarize the activity of Ang in blood and lymphatic endothelial cells, its different functions in the body under both physiological and pathological conditions, and the main molecular mechanisms identified to date
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