
IndraLab
Statements
reach
"Given that weak binding of VEGF-A 165 appears to occur at concentrations of VEGF-A 165 required for biological effects in endothelial cells such as migration or angiogenesis, such as were used in this study, the biological relevance of VEGF-A 165 binding to NRP2 in cells is unclear."
reach
"Furthermore, NRP2 is co-expressed with NRP1 in endothelial and other cell types, NRP2 and NRP1 may associate to form heterodimers 14, and NRP2 also binds to VEGF-A in trimeric complexes with VEGF receptor 2 21, 22, suggesting that NRPs have the potential to interact in a cooperative fashion in the endothelium."
sparser
"To our surprise, in our study, we found that NRP-2 (an isoform of NRP-1)-related ligand-receptor interactions, specifically the NRP-2-SEMA3C and NRP-2-VEGFA interactions between CAFs/endothelial cells/DCs/macrophages/tumor cells and other cells, were relatively stronger in responders than in nonresponders."
sparser
"Given that weak binding of VEGF-A 165 appears to occur at concentrations of VEGF-A 165 required for biological effects in endothelial cells such as migration or angiogenesis, such as were used in this study, the biological relevance of VEGF-A 165 binding to NRP2 in cells is unclear."
sparser
"Initial studies showed that VEGF-A binding to VEGFR-2/NRP1 or NRP2 receptor complexes promoted endothelial cell proliferation, migration, and tube formation in vitro as well as angiogenesis in vivo. xref , xref , xref , xref In endothelial cells, NRPs enhance the binding of VEGF-A 165 to its receptor and increase ERK1/2 MAPK activation. xref The VEGF-A/NRP1/proline-rich TK2 (PYK2/PTK2B)/p130Cas (BCAR1) axis is also required for endothelial cell chemotaxis. xref NRP2 promotes lymphangiogenesis through a mechanism involving VEGF-C and VEGFR-3. xref Blocking the VEGF-C binding site with an NRP2-blocking antibody inhibits tumor lymphangiogenesis and metastatic spread to local lymph nodes and distant sites. xref In addition to its effects on angiogenesis, VEGF-A 165 promotes tumor cell survival through an NRP- and PI3K/AKT-dependent mechanism. xref – xref VEGF-A 165 also promotes physical interaction between NRP1 and c-MET, facilitates c-MET, Src kinase, and STAT3 activation, and leads to the upregulation of the pro-survival factor, MLC-1. xref VEGF-C binding to NRP2 prevents oxidative stress and promotes cancer cell survival and autophagy. xref , xref While the mechanism is unknown, the VEGF-C/NRP2 axis inhibits mammalian target of rapamycin complex (mTORC)-1 activity, relieving its suppression of autophagy and thus contributing to tumor cell survival under stress."