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• W1991362893 abstract "VEGF can be secreted in multiple isoforms with variable affinity for extracellular proteins and different abilities to induce vascular morphogenesis, but the molecular mechanisms behind these effects remain unclear. Here, we show molecular distinctions between signaling initiated from soluble versus matrix-bound VEGF, which mediates a sustained level of VEGFR2 internalization and clustering. Exposure of endothelial cells to matrix-bound VEGF elicits prolonged activation of VEGFR2 with differential phosphorylation of Y1214, and extended activation kinetics of p38. These events require association of VEGFR2 with β1 integrins. Matrix-bound VEGF also promotes reciprocal responses on β1 integrin by inducing its association with focal adhesions; a response that is absent upon exposure to soluble VEGF. Inactivation of β1 integrin blocks the prolonged phosphorylation of Y1214 and consequent activation of p38. Combined, these results indicate that when in the context of extracellular matrix, activation of VEGFR2 is distinct from that of soluble VEGF in terms of recruitment of receptor partners, phosphorylation kinetics, and activation of downstream effectors." @default.
• W1991362893 created "2016-06-24" @default.
• W1991362893 creator A5009494138 @default.
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• W1991362893 date "2010-02-22" @default.
• W1991362893 modified "2023-10-12" @default.
• W1991362893 title "Anchorage of VEGF to the extracellular matrix conveys differential signaling responses to endothelial cells" @default.
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• W1991362893 doi "https://doi.org/10.1083/jcb.200906044" @default.
• W1991362893 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2828913" @default.
• W1991362893 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/20176926" @default.
• W1991362893 hasPublicationYear "2010" @default.
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