Rhodocetin-αβ-induced neuropilin-1-cMet association triggers restructuring of matrix contacts in endothelial cells
Objective— - - The snake venom component rhodocetin-αβ (RCαβ) stimulates endothelial cell motility in an α2β1 integrin-independent manner. We aimed to elucidate its cellular and molecular mechanisms. - - Methods and Results— - - We identified neuropilin-1 (Nrp1) as a novel target of RCαβ by prote...
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| Hauptverfasser: | , , , , , |
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| Dokumenttyp: | Article (Journal) |
| Sprache: | Englisch |
| Veröffentlicht: |
3 Jan 2013
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| In: |
Arteriosclerosis, thrombosis, and vascular biology
Year: 2013, Jahrgang: 33, Heft: 3, Pages: 544-554 |
| ISSN: | 1524-4636 |
| DOI: | 10.1161/ATVBAHA.112.00006 |
| Online-Zugang: | Verlag, kostenfrei, Volltext: https://doi.org/10.1161/ATVBAHA.112.00006 Verlag, kostenfrei, Volltext: https://www.ahajournals.org/doi/10.1161/ATVBAHA.112.00006 
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| Verfasserangaben: | Stephan Niland, Bartosz Ditkowski, Désirée Parrandier, Lise Roth, Hellmut Augustin, and Johannes A. Eble |
MARC
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| 245 | 1 | 0 | |a Rhodocetin-αβ-induced neuropilin-1-cMet association triggers restructuring of matrix contacts in endothelial cells |c Stephan Niland, Bartosz Ditkowski, Désirée Parrandier, Lise Roth, Hellmut Augustin, and Johannes A. Eble |
| 246 | 3 | 3 | |a Rhodocetin-alpha-beta-induced neuropilin-1-cMet association triggers restructuring of matrix contacts in endothelial cells |
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| 520 | |a Objective— - - The snake venom component rhodocetin-αβ (RCαβ) stimulates endothelial cell motility in an α2β1 integrin-independent manner. We aimed to elucidate its cellular and molecular mechanisms. - - Methods and Results— - - We identified neuropilin-1 (Nrp1) as a novel target of RCαβ by protein-chemical methods. RCαβ and vascular endothelial growth factor (VEGF)-A avidly bind to Nrp1. Instead of acting as VEGF receptor 2 coreceptor, Nrp1 associates upon RCαβ treatment with cMet. Furthermore, cell-based ELISAs and kinase inhibitor studies showed that RCαβ induces phosphorylation of tyrosines 1234/1235 and thus activation of cMet. Consequently, paxillin is phosphorylated at Y31, which is redistributed from streak-like focal adhesions to spot-like focal contacts at the cell perimeter, along with α2β1 integrin, thereby regulating cell-matrix interactions. Cortactin is abundant in the cell perimeter, where it is involved in the branching of the cortical actin network of lamellipodia, whereas tensile force-bearing actin stress fibers radiating from focal adhesions disappear together with zyxin, a focal adhesion marker, on RCαβ treatment. - - Conclusion— - - Our data demonstrate that (1) Nrp1 is a novel target for venom components, such as RCαβ; (2) Nrp1 coupled to cMet regulates the type of cell-matrix interactions in a manner involving paxillin phosphorylation; and (3) altered cell-matrix interactions determine endothelial cell migration and cellular force management. | ||
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| 700 | 1 | |a Parrandier, Désirée |e VerfasserIn |4 aut | |
| 700 | 1 | |a Roth, Lise |e VerfasserIn |0 (DE-588)1151130745 |0 (DE-627)1011362716 |0 (DE-576)497492156 |4 aut | |
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