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...

Descripción completa

Guardado en:

Detalles Bibliográficos
Autores principales:	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
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2019
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/4e1c0f8ebf6f4c9e8a2422a46f5ec318
Etiquetas:	Agregar Etiqueta Sin Etiquetas, Sea el primero en etiquetar este registro!

id	oai:doaj.org-article:4e1c0f8ebf6f4c9e8a2422a46f5ec318
record_format	dspace
spelling	oai:doaj.org-article:4e1c0f8ebf6f4c9e8a2422a46f5ec3182021-12-02T17:01:32ZN-terminal syndecan-2 domain selectively enhances 6-O heparan sulfate chains sulfation and promotes VEGFA165-dependent neovascularization10.1038/s41467-019-09605-z2041-1723https://doaj.org/article/4e1c0f8ebf6f4c9e8a2422a46f5ec3182019-04-01T00:00:00Zhttps://doi.org/10.1038/s41467-019-09605-zhttps://doaj.org/toc/2041-1723Proteoglycans 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.Federico CortiYingdi WangJohn M. RhodesDeepak AtriStephanie Archer-HartmannJiasheng ZhangZhen W. ZhuangDongying ChenTianyun WangZhirui WangParastoo AzadiMichael SimonsNature PortfolioarticleScienceQENNature Communications, Vol 10, Iss 1, Pp 1-14 (2019)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q 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 N-terminal syndecan-2 domain selectively enhances 6-O heparan sulfate chains sulfation and promotes VEGFA165-dependent neovascularization
description	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.
format	article
author	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
author_facet	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
author_sort	Federico Corti
title	N-terminal syndecan-2 domain selectively enhances 6-O heparan sulfate chains sulfation and promotes VEGFA165-dependent neovascularization
title_short	N-terminal syndecan-2 domain selectively enhances 6-O heparan sulfate chains sulfation and promotes VEGFA165-dependent neovascularization
title_full	N-terminal syndecan-2 domain selectively enhances 6-O heparan sulfate chains sulfation and promotes VEGFA165-dependent neovascularization
title_fullStr	N-terminal syndecan-2 domain selectively enhances 6-O heparan sulfate chains sulfation and promotes VEGFA165-dependent neovascularization
title_full_unstemmed	N-terminal syndecan-2 domain selectively enhances 6-O heparan sulfate chains sulfation and promotes VEGFA165-dependent neovascularization
title_sort	n-terminal syndecan-2 domain selectively enhances 6-o heparan sulfate chains sulfation and promotes vegfa165-dependent neovascularization
publisher	Nature Portfolio
publishDate	2019
url	https://doaj.org/article/4e1c0f8ebf6f4c9e8a2422a46f5ec318
work_keys_str_mv	AT federicocorti nterminalsyndecan2domainselectivelyenhances6oheparansulfatechainssulfationandpromotesvegfa165dependentneovascularization AT yingdiwang nterminalsyndecan2domainselectivelyenhances6oheparansulfatechainssulfationandpromotesvegfa165dependentneovascularization AT johnmrhodes nterminalsyndecan2domainselectivelyenhances6oheparansulfatechainssulfationandpromotesvegfa165dependentneovascularization AT deepakatri nterminalsyndecan2domainselectivelyenhances6oheparansulfatechainssulfationandpromotesvegfa165dependentneovascularization AT stephaniearcherhartmann nterminalsyndecan2domainselectivelyenhances6oheparansulfatechainssulfationandpromotesvegfa165dependentneovascularization AT jiashengzhang nterminalsyndecan2domainselectivelyenhances6oheparansulfatechainssulfationandpromotesvegfa165dependentneovascularization AT zhenwzhuang nterminalsyndecan2domainselectivelyenhances6oheparansulfatechainssulfationandpromotesvegfa165dependentneovascularization AT dongyingchen nterminalsyndecan2domainselectivelyenhances6oheparansulfatechainssulfationandpromotesvegfa165dependentneovascularization AT tianyunwang nterminalsyndecan2domainselectivelyenhances6oheparansulfatechainssulfationandpromotesvegfa165dependentneovascularization AT zhiruiwang nterminalsyndecan2domainselectivelyenhances6oheparansulfatechainssulfationandpromotesvegfa165dependentneovascularization AT parastooazadi nterminalsyndecan2domainselectivelyenhances6oheparansulfatechainssulfationandpromotesvegfa165dependentneovascularization AT michaelsimons nterminalsyndecan2domainselectivelyenhances6oheparansulfatechainssulfationandpromotesvegfa165dependentneovascularization
_version_	1718382080795082752

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

Ejemplares similares