Biochem Biophys Res Commun 2003,
PMID: 12890486
Yoon, Mi-Jeong; Cho, Chung-Hyun; Lee, Chang Sup; Jang, Il-Ho; Ryu, Sung Ho; Koh, Gou Young
Angiopoietin-1 (Ang1) and its receptor, Tie2, play critical roles in blood vessel formation. Ang1 triggers a variety of signaling events in endothelial cells leading to vasculogenic and angiogenic processes. However, the underlying mechanism for Ang1/Tie2 signaling is not fully understood. Here, we show that Tie2 and phospholipase D (PLD) are localized in the caveolae, specialized subdomains of the endothelial cell plasma membrane enriched with signaling molecules. Interestingly, Ang1 increased PLD activities in a dose- and time-dependent manner. Ang1-induced MEK/ERK activation was abrogated when PLD was inhibited, suggesting that PLD mediates Ang1-induced MEK/ERK activation. Moreover, PLD inhibitor, 1-butanol, inhibited Ang1-induced endothelial cell migration. Our results indicate that: (1) caveolae may be the platform for Tie2/PLD association in endothelial cells; (2) PLD is a new mediator of Ang1/Tie2-induced signaling pathway, and it participates in MAPK activation and endothelial cell migration.
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Text Mining Data
MEK/ERK → Tie2: "
Localization of
Tie2 and phospholipase D in endothelial caveolae is
involved in angiopoietin-1 induced
MEK/ERK phosphorylation and migration in endothelial cells
"
MEK/ERK → phospholipase D: "
Localization of Tie2 and phospholipase D in endothelial caveolae is involved in angiopoietin-1 induced MEK/ERK phosphorylation and migration in endothelial cells
"
MEK/ERK → angiopoietin-1: "
Localization of Tie2 and phospholipase D in endothelial caveolae is involved in angiopoietin-1 induced MEK/ERK phosphorylation and migration in endothelial cells
"
PLD → Ang1: "
Interestingly, Ang1 increased PLD activities in a dose- and time dependent manner
"
MEK/ERK → PLD: "
Ang1 induced MEK/ERK activation was abrogated when PLD was inhibited, suggesting that PLD mediates Ang1 induced MEK/ERK activation
"
MEK/ERK → Ang1: "
Ang1 induced MEK/ERK activation was abrogated when PLD was inhibited, suggesting that PLD mediates Ang1 induced MEK/ERK activation
"
MAPK → Ang1/Tie2: "
Our results indicate that : ( 1 ) caveolae may be the platform for Tie2/PLD association in endothelial cells ; ( 2 ) PLD is a new mediator of Ang1/Tie2 induced signaling pathway, and it participates in MAPK activation and endothelial cell migration
"
MAPK → Ang1/Tie2: "
Our results indicate that : ( 1 ) caveolae may be the platform for Tie2/PLD association in endothelial cells ; ( 2 ) PLD is a new mediator of Ang1/Tie2 induced signaling pathway, and it participates in MAPK activation and endothelial cell migration
"
Manually curated Databases
-
NCI Pathway Database Angiopoietin receptor Tie2-mediated signaling:
None
→
None
(modification, collaborate)
Evidence: assay
-
NCI Pathway Database Angiopoietin receptor Tie2-mediated signaling:
None
→
PLD (PLD2)
(modification, collaborate)
Evidence: assay
-
NCI Pathway Database Angiopoietin receptor Tie2-mediated signaling:
None
→
None
(modification, collaborate)
Evidence: assay
-
NCI Pathway Database Angiopoietin receptor Tie2-mediated signaling:
None
→
None
(modification, collaborate)
Evidence: assay
-
NCI Pathway Database Angiopoietin receptor Tie2-mediated signaling:
PLD (PLD2)
→
None
(modification, activates)
Evidence: assay
-
NCI Pathway Database Angiopoietin receptor Tie2-mediated signaling:
Erk1-2 (MAPK3/MAPK1)
→
Erk1-2-active (MAPK3/MAPK1)
(modification, collaborate)
Evidence: mutant phenotype, assay
-
NCI Pathway Database Angiopoietin receptor Tie2-mediated signaling:
Erk1-2 (MAPK3/MAPK1)
→
PLD (PLD2)
(modification, collaborate)
Evidence: mutant phenotype, assay
-
NCI Pathway Database Angiopoietin receptor Tie2-mediated signaling:
Tie2/Ang1 complex (ANGPT1-TEK)
→
PLD (PLD2)
(modification, activates)
In total, 8 gene pairs are associated to this article in curated databases