N-terminal syndecan-2 domain selectively enhances 6-O heparan sulfate chains sulfation and promotes VEGFA165-dependent neovascularization

Proteoglycans are glycosylated proteins that play a number of structural and signalling functions. Here, Corti, Wang et al. show that the N-terminal sequence of proteoglycan Syndecan-2 selectively increases 6-O sulfation of its heparan sulfate chains, and that this promotes formation of a ternary Sd...

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Auteurs principaux: Federico Corti, Yingdi Wang, John M. Rhodes, Deepak Atri, Stephanie Archer-Hartmann, Jiasheng Zhang, Zhen W. Zhuang, Dongying Chen, Tianyun Wang, Zhirui Wang, Parastoo Azadi, Michael Simons
Format: article
Langue:EN
Publié: Nature Portfolio 2019
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Accès en ligne:https://doaj.org/article/4e1c0f8ebf6f4c9e8a2422a46f5ec318
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Résumé:Proteoglycans are glycosylated proteins that play a number of structural and signalling functions. Here, Corti, Wang et al. show that the N-terminal sequence of proteoglycan Syndecan-2 selectively increases 6-O sulfation of its heparan sulfate chains, and that this promotes formation of a ternary Sdc2/VEGFA/VEGFR2 complex leading to increased angiogenesis.