{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,1,19]],"date-time":"2026-01-19T07:16:20Z","timestamp":1768806980219,"version":"3.49.0"},"reference-count":36,"publisher":"Ovid Technologies (Wolters Kluwer Health)","issue":"3","content-domain":{"domain":["www.ahajournals.org"],"crossmark-restriction":true},"short-container-title":["ATVB"],"published-print":{"date-parts":[[2013,3]]},"abstract":"<jats:sec>\n            <jats:title>Objective\u2014<\/jats:title>\n            <jats:p>The snake venom component rhodocetin-\u03b1\u03b2 (RC\u03b1\u03b2) stimulates endothelial cell motility in an \u03b12\u03b21 integrin\u2013independent manner. We aimed to elucidate its cellular and molecular mechanisms.<\/jats:p>\n          <\/jats:sec>\n          <jats:sec>\n            <jats:title>Methods and Results\u2014<\/jats:title>\n            <jats:p>We identified neuropilin-1 (Nrp1) as a novel target of RC\u03b1\u03b2 by protein-chemical methods. RC\u03b1\u03b2 and vascular endothelial growth factor (VEGF)-A avidly bind to Nrp1. Instead of acting as VEGF receptor 2 coreceptor, Nrp1 associates upon RC\u03b1\u03b2 treatment with cMet. Furthermore, cell-based ELISAs and kinase inhibitor studies showed that RC\u03b1\u03b2 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 \u03b12\u03b21 integrin, thereby regulating cell\u2013matrix 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\u2013bearing actin stress fibers radiating from focal adhesions disappear together with zyxin, a focal adhesion marker, on RC\u03b1\u03b2 treatment.<\/jats:p>\n          <\/jats:sec>\n          <jats:sec>\n            <jats:title>Conclusion\u2014<\/jats:title>\n            <jats:p>Our data demonstrate that (1) Nrp1 is a novel target for venom components, such as RC\u03b1\u03b2; (2) Nrp1 coupled to cMet regulates the type of cell\u2013matrix interactions in a manner involving paxillin phosphorylation; and (3) altered cell\u2013matrix interactions determine endothelial cell migration and cellular force management.<\/jats:p>\n          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