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Life Sci."],"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>\n                    Moesin (Msn) is a member of the ERM (Ezrin, Radixin, and Moesin) protein family implicated in cell-cell recognition, cell adhesion, and migration. In this work, we identified Msn as an \u03b1\n                    <jats:sub>\u03bd<\/jats:sub>\n                    \u03b2\n                    <jats:sub>3<\/jats:sub>\n                    integrin-interacting molecule in human endothelial cells, with a role in endothelial cell signaling and angiogenesis. Msn and its active phosphorylated form are highly expressed in endothelial cells in vitro and in vivo. Pleiotrophin and vascular endothelial growth factor A\n                    <jats:sub>165<\/jats:sub>\n                    (VEGFA\n                    <jats:sub>165<\/jats:sub>\n                    ), increase Msn phosphorylation and decrease the interaction of Msn with \u03b1\n                    <jats:sub>\u03bd<\/jats:sub>\n                    \u03b2\n                    <jats:sub>3<\/jats:sub>\n                    integrin. Downregulation of Msn expression in endothelial cells using siRNA reduced VEGF receptor 2 (VEGFR2) expression and activation. It also decreased permeability, collective cell migration, and tube formation in vitro, concomitant with reduced angiogenesis and blood-brain barrier permeability in\n                    <jats:italic>Msn<\/jats:italic>\n                    knockout mice. Concurrently, it decreased \u03b2\n                    <jats:sub>3<\/jats:sub>\n                    integrin expression, increased the c-Src- and phosphoinositide 3-kinase (PI3K)-dependent cell-surface localization of nucleolin, and activated ERK1\/2 kinases and cMet. Pharmacological inhibitors of c-Src, PI3K, cell-surface nucleolin, ERK1\/2, and cMet, but not of VEGFR2 or \u03b1\n                    <jats:sub>v<\/jats:sub>\n                    \u03b2\n                    <jats:sub>3<\/jats:sub>\n                    integrin, abolished siMsn-induced individual-cell motility. Taken together, these findings identify a novel binding partner of the \u03b1\n                    <jats:sub>v<\/jats:sub>\n                    \u03b2\n                    <jats:sub>3<\/jats:sub>\n                    integrin that regulates the activation of cMet and VEGFR2 in endothelial cells, clarifying the mechanisms underlying the activation of multiple angiogenic pathways and highlighting potential new targets for improving anti-angiogenic therapies.\n                  <\/jats:p>","DOI":"10.1007\/s00018-026-06352-5","type":"journal-article","created":{"date-parts":[[2026,7,15]],"date-time":"2026-07-15T19:14:28Z","timestamp":1784142868000},"update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["Moesin is an \u03b1\u03bd\u03b23 integrin-interacting protein that affects endothelial cell activation and angiogenesis through balancing c-Met and VEGFR2 activation"],"prefix":"10.1007","volume":"83","author":[{"given":"Michaela-Karina","family":"Enake","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Wanjing","family":"Lai","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sotiria","family":"Tsirmoula","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"\u039aonstantinos","family":"Papadimatos","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Marina","family":"\u039aoutsioumpa","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Lamprini","family":"Skondra","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Spyros","family":"Skandalis","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Constantinos M.","family":"Mikelis","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Lingling","family":"Shi","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-6429-4325","authenticated-orcid":false,"given":"Evangelia","family":"Papadimitriou","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2026,7,15]]},"reference":[{"key":"6352_CR1","doi-asserted-by":"publisher","first-page":"1157","DOI":"10.1016\/0092-8674(94)90007-8","volume":"79","author":"PC Brooks","year":"1994","unstructured":"Brooks PC, Montgomery AM, Rosenfeld M, Reisfeld RA, Hu T, Klier G, Cheresh DA (1994) Integrin alpha v beta 3 antagonists promote tumor regression by inducing apoptosis of angiogenic blood vessels. 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