IndraLab

Statements


3 | 5 4

reach
"It seems, therefore, that binding of VEGFA to VEGFR2 and PTPRZ1 activates VEGFR2 and c-Met, respectively, to activate endothelial cells."

reach
"Since VEGFA binds to PTPRZ1 in a VEGFR2-independent manner [10, 11], our data also warrant further investigation of the potential targeting of PTPRZ1 as an alternative therapeutic approach in anti-VEGFA/VEGFR2-resistant angiogenesis."

sparser
"The heparin-binding domain of VEGFA is also not involved [ xref , xref ], and the VEGFA domain that interacts with PTPRZ1 is still to be identified."

sparser
"Based on the above and our previous data showing that VEGFA binds to and requires PTPRZ1 to stimulate human endothelial cell migration [ xref ], we tested whether VEGFA 165 activates c-Met."

sparser
"Since VEGFA binds to PTPRZ1 in a VEGFR2-independent manner [ xref , xref ], our data also warrant further investigation of the potential targeting of PTPRZ1 as an alternative therapeutic approach in anti-VEGFA/VEGFR2-resistant angiogenesis."

sparser
"Another ligand of PTPRZ is FGF-2, and furthermore, VEGF-A can directly interact with PTPRZ, competing with PTN for PTPRZ binding [ xref , xref , xref ]."

reach
"In HUVEC, binding of PTN or VEGFA to PTPRZ1 leads to phosphorylation of β integrin on Tyr773 upstream of PI3K activation, cell surface nucleolin localization, and enhanced cell migration [30,33,37]."

reach
"It has been shown that upon binding of PTN or VEGFA to PTPRZ1 in HUVEC, c-Src kinase is dephosphorylated in its carboxyterminal Tyr527, and this dephosphorylation is the first step for the activation of c-Src and its downstream signaling [30,37,51]."

reach
"Based on the above and our previous data showing that VEGFA binds to and requires PTPRZ1 to stimulate human endothelial cell migration [10], we tested whether VEGFA activates c-Met."