
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."
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."
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
"This finding aligns with previous studies showing significantly higher levels of PGR in glandular epithelium in EPs. xref Furthermore, angiogenesis signaling, particularly the VEGFA‐NRP2 interaction, demonstrated increased activity between mast cells and endothelial cells (Figure xref )."
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."