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Merck

Neuroligin 1 induces blood vessel maturation by cooperating with the α6 integrin.

The Journal of biological chemistry (2014-05-27)
Anna Valeria Samarelli, Elena Riccitelli, Laura Bizzozero, Tatiana Nunes Silveira, Giorgio Seano, Margherita Pergolizzi, Grazia Vitagliano, Ilaria Cascone, Gilles Carpentier, Alessia Bottos, Luca Primo, Federico Bussolino, Marco Arese
RESUMEN

The synaptic protein Neuroligin 1 (NLGN1), a cell adhesion molecule, is critical for the formation and consolidation of synaptic connectivity and is involved in vascular development. The mechanism through which NLGN1 acts, especially in vascular cells, is unknown. Here, we aimed at deepening our knowledge on the cellular activities and molecular pathways exploited by endothelial NLGN1 both in vitro and in vivo. We analyzed the phenotypic consequences of NLGN1 expression modulation in endothelial cells through in vitro angiogenesis assays and the mouse postnatal retinal angiogenesis model. We demonstrate that NLGN1, whereas not affecting endothelial cell proliferation or migration, modulates cell adhesion to the vessel stabilizing protein laminin through cooperation with the α6 integrin, a specific laminin receptor. Finally, we show that in vivo, NLGN1 and α6 integrin preferentially colocalize in the mature retinal vessels, whereas NLGN1 deletion causes an aberrant VE-cadherin, laminin and α6 integrin distribution in vessels, along with significant structural defects in the vascular tree.

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Sigma-Aldrich
Anticuerpo anti-laminina, Chemicon®, from rabbit
Sigma-Aldrich
Anticuerpo anti-integrina α3, clon P1B5, sin azida, clone P1B5, Chemicon®, from mouse