Blood flow patterns switch VEGFR2 activity through differential S-nitrosylation and S-oxidation

Summary: Vascular endothelial growth factor receptor-2 (VEGFR2) plays a key role in maintaining vascular endothelial homeostasis. Here, we show that blood flows determine activation and inactivation of VEGFR2 through selective cysteine modifications. VEGFR2 activation is regulated by reversible oxid...
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Autor*in:	Dong Hoon Kang [verfasserIn] Yerin Kim [verfasserIn] Seongchun Min [verfasserIn] Su Youn Lee [verfasserIn] Ka Young Chung [verfasserIn] In-Jeoung Baek [verfasserIn] Kihwan Kwon [verfasserIn] Hanjoong Jo [verfasserIn] Sang Won Kang [verfasserIn]

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2023

Schlagwörter:	CP: Cell biology

Übergeordnetes Werk:	In: Cell Reports - Elsevier, 2015, 42(2023), 11, Seite 113361-
Übergeordnetes Werk:	volume:42 ; year:2023 ; number:11 ; pages:113361-

Links:	Link aufrufen Link aufrufen Link aufrufen Journal toc

DOI / URN:	10.1016/j.celrep.2023.113361

Katalog-ID:	DOAJ099606380

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520			\|a Summary: Vascular endothelial growth factor receptor-2 (VEGFR2) plays a key role in maintaining vascular endothelial homeostasis. Here, we show that blood flows determine activation and inactivation of VEGFR2 through selective cysteine modifications. VEGFR2 activation is regulated by reversible oxidation at Cys1206 residue. H2O2-mediated VEGFR2 oxidation is induced by oscillatory flow in vascular endothelial cells through the induction of NADPH oxidase-4 expression. In contrast, laminar flow induces the expression of endothelial nitric oxide synthase and results in the S-nitrosylation of VEGFR2 at Cys1206, which counteracts the oxidative inactivation. The shear stress model study reveals that disturbed blood flow operated by partial ligation in the carotid arteries induces endothelial damage and intimal hyperplasia in control mice but not in knock-in mice harboring the oxidation-resistant mutant (C1206S) of VEGFR2. Thus, our findings reveal that flow-dependent redox regulation of the VEGFR2 kinase is critical for the structural and functional integrity of the arterial endothelium.
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publishDate	2023
allfields	10.1016/j.celrep.2023.113361 doi (DE-627)DOAJ099606380 (DE-599)DOAJ9b602d14b06f45a29435838d47121b5e DE-627 ger DE-627 rakwb eng QH301-705.5 Dong Hoon Kang verfasserin aut Blood flow patterns switch VEGFR2 activity through differential S-nitrosylation and S-oxidation 2023 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Summary: Vascular endothelial growth factor receptor-2 (VEGFR2) plays a key role in maintaining vascular endothelial homeostasis. Here, we show that blood flows determine activation and inactivation of VEGFR2 through selective cysteine modifications. VEGFR2 activation is regulated by reversible oxidation at Cys1206 residue. H2O2-mediated VEGFR2 oxidation is induced by oscillatory flow in vascular endothelial cells through the induction of NADPH oxidase-4 expression. In contrast, laminar flow induces the expression of endothelial nitric oxide synthase and results in the S-nitrosylation of VEGFR2 at Cys1206, which counteracts the oxidative inactivation. The shear stress model study reveals that disturbed blood flow operated by partial ligation in the carotid arteries induces endothelial damage and intimal hyperplasia in control mice but not in knock-in mice harboring the oxidation-resistant mutant (C1206S) of VEGFR2. Thus, our findings reveal that flow-dependent redox regulation of the VEGFR2 kinase is critical for the structural and functional integrity of the arterial endothelium. CP: Cell biology Biology (General) Yerin Kim verfasserin aut Seongchun Min verfasserin aut Su Youn Lee verfasserin aut Ka Young Chung verfasserin aut In-Jeoung Baek verfasserin aut Kihwan Kwon verfasserin aut Hanjoong Jo verfasserin aut Sang Won Kang verfasserin aut In Cell Reports Elsevier, 2015 42(2023), 11, Seite 113361- (DE-627)684964562 (DE-600)2649101-1 22111247 nnns volume:42 year:2023 number:11 pages:113361- https://doi.org/10.1016/j.celrep.2023.113361 kostenfrei https://doaj.org/article/9b602d14b06f45a29435838d47121b5e kostenfrei http://www.sciencedirect.com/science/article/pii/S2211124723013736 kostenfrei https://doaj.org/toc/2211-1247 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2110 GBV_ILN_2112 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2470 GBV_ILN_2507 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4393 GBV_ILN_4700 AR 42 2023 11 113361-
spelling	10.1016/j.celrep.2023.113361 doi (DE-627)DOAJ099606380 (DE-599)DOAJ9b602d14b06f45a29435838d47121b5e DE-627 ger DE-627 rakwb eng QH301-705.5 Dong Hoon Kang verfasserin aut Blood flow patterns switch VEGFR2 activity through differential S-nitrosylation and S-oxidation 2023 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Summary: Vascular endothelial growth factor receptor-2 (VEGFR2) plays a key role in maintaining vascular endothelial homeostasis. Here, we show that blood flows determine activation and inactivation of VEGFR2 through selective cysteine modifications. VEGFR2 activation is regulated by reversible oxidation at Cys1206 residue. H2O2-mediated VEGFR2 oxidation is induced by oscillatory flow in vascular endothelial cells through the induction of NADPH oxidase-4 expression. In contrast, laminar flow induces the expression of endothelial nitric oxide synthase and results in the S-nitrosylation of VEGFR2 at Cys1206, which counteracts the oxidative inactivation. The shear stress model study reveals that disturbed blood flow operated by partial ligation in the carotid arteries induces endothelial damage and intimal hyperplasia in control mice but not in knock-in mice harboring the oxidation-resistant mutant (C1206S) of VEGFR2. Thus, our findings reveal that flow-dependent redox regulation of the VEGFR2 kinase is critical for the structural and functional integrity of the arterial endothelium. CP: Cell biology Biology (General) Yerin Kim verfasserin aut Seongchun Min verfasserin aut Su Youn Lee verfasserin aut Ka Young Chung verfasserin aut In-Jeoung Baek verfasserin aut Kihwan Kwon verfasserin aut Hanjoong Jo verfasserin aut Sang Won Kang verfasserin aut In Cell Reports Elsevier, 2015 42(2023), 11, Seite 113361- (DE-627)684964562 (DE-600)2649101-1 22111247 nnns volume:42 year:2023 number:11 pages:113361- https://doi.org/10.1016/j.celrep.2023.113361 kostenfrei https://doaj.org/article/9b602d14b06f45a29435838d47121b5e kostenfrei http://www.sciencedirect.com/science/article/pii/S2211124723013736 kostenfrei https://doaj.org/toc/2211-1247 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2110 GBV_ILN_2112 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2470 GBV_ILN_2507 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4393 GBV_ILN_4700 AR 42 2023 11 113361-
allfields_unstemmed	10.1016/j.celrep.2023.113361 doi (DE-627)DOAJ099606380 (DE-599)DOAJ9b602d14b06f45a29435838d47121b5e DE-627 ger DE-627 rakwb eng QH301-705.5 Dong Hoon Kang verfasserin aut Blood flow patterns switch VEGFR2 activity through differential S-nitrosylation and S-oxidation 2023 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Summary: Vascular endothelial growth factor receptor-2 (VEGFR2) plays a key role in maintaining vascular endothelial homeostasis. Here, we show that blood flows determine activation and inactivation of VEGFR2 through selective cysteine modifications. VEGFR2 activation is regulated by reversible oxidation at Cys1206 residue. H2O2-mediated VEGFR2 oxidation is induced by oscillatory flow in vascular endothelial cells through the induction of NADPH oxidase-4 expression. In contrast, laminar flow induces the expression of endothelial nitric oxide synthase and results in the S-nitrosylation of VEGFR2 at Cys1206, which counteracts the oxidative inactivation. The shear stress model study reveals that disturbed blood flow operated by partial ligation in the carotid arteries induces endothelial damage and intimal hyperplasia in control mice but not in knock-in mice harboring the oxidation-resistant mutant (C1206S) of VEGFR2. Thus, our findings reveal that flow-dependent redox regulation of the VEGFR2 kinase is critical for the structural and functional integrity of the arterial endothelium. CP: Cell biology Biology (General) Yerin Kim verfasserin aut Seongchun Min verfasserin aut Su Youn Lee verfasserin aut Ka Young Chung verfasserin aut In-Jeoung Baek verfasserin aut Kihwan Kwon verfasserin aut Hanjoong Jo verfasserin aut Sang Won Kang verfasserin aut In Cell Reports Elsevier, 2015 42(2023), 11, Seite 113361- (DE-627)684964562 (DE-600)2649101-1 22111247 nnns volume:42 year:2023 number:11 pages:113361- https://doi.org/10.1016/j.celrep.2023.113361 kostenfrei https://doaj.org/article/9b602d14b06f45a29435838d47121b5e kostenfrei http://www.sciencedirect.com/science/article/pii/S2211124723013736 kostenfrei https://doaj.org/toc/2211-1247 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2110 GBV_ILN_2112 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2470 GBV_ILN_2507 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4393 GBV_ILN_4700 AR 42 2023 11 113361-
allfieldsGer	10.1016/j.celrep.2023.113361 doi (DE-627)DOAJ099606380 (DE-599)DOAJ9b602d14b06f45a29435838d47121b5e DE-627 ger DE-627 rakwb eng QH301-705.5 Dong Hoon Kang verfasserin aut Blood flow patterns switch VEGFR2 activity through differential S-nitrosylation and S-oxidation 2023 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Summary: Vascular endothelial growth factor receptor-2 (VEGFR2) plays a key role in maintaining vascular endothelial homeostasis. Here, we show that blood flows determine activation and inactivation of VEGFR2 through selective cysteine modifications. VEGFR2 activation is regulated by reversible oxidation at Cys1206 residue. H2O2-mediated VEGFR2 oxidation is induced by oscillatory flow in vascular endothelial cells through the induction of NADPH oxidase-4 expression. In contrast, laminar flow induces the expression of endothelial nitric oxide synthase and results in the S-nitrosylation of VEGFR2 at Cys1206, which counteracts the oxidative inactivation. The shear stress model study reveals that disturbed blood flow operated by partial ligation in the carotid arteries induces endothelial damage and intimal hyperplasia in control mice but not in knock-in mice harboring the oxidation-resistant mutant (C1206S) of VEGFR2. Thus, our findings reveal that flow-dependent redox regulation of the VEGFR2 kinase is critical for the structural and functional integrity of the arterial endothelium. CP: Cell biology Biology (General) Yerin Kim verfasserin aut Seongchun Min verfasserin aut Su Youn Lee verfasserin aut Ka Young Chung verfasserin aut In-Jeoung Baek verfasserin aut Kihwan Kwon verfasserin aut Hanjoong Jo verfasserin aut Sang Won Kang verfasserin aut In Cell Reports Elsevier, 2015 42(2023), 11, Seite 113361- (DE-627)684964562 (DE-600)2649101-1 22111247 nnns volume:42 year:2023 number:11 pages:113361- https://doi.org/10.1016/j.celrep.2023.113361 kostenfrei https://doaj.org/article/9b602d14b06f45a29435838d47121b5e kostenfrei http://www.sciencedirect.com/science/article/pii/S2211124723013736 kostenfrei https://doaj.org/toc/2211-1247 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2110 GBV_ILN_2112 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2470 GBV_ILN_2507 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4393 GBV_ILN_4700 AR 42 2023 11 113361-
allfieldsSound	10.1016/j.celrep.2023.113361 doi (DE-627)DOAJ099606380 (DE-599)DOAJ9b602d14b06f45a29435838d47121b5e DE-627 ger DE-627 rakwb eng QH301-705.5 Dong Hoon Kang verfasserin aut Blood flow patterns switch VEGFR2 activity through differential S-nitrosylation and S-oxidation 2023 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Summary: Vascular endothelial growth factor receptor-2 (VEGFR2) plays a key role in maintaining vascular endothelial homeostasis. Here, we show that blood flows determine activation and inactivation of VEGFR2 through selective cysteine modifications. VEGFR2 activation is regulated by reversible oxidation at Cys1206 residue. H2O2-mediated VEGFR2 oxidation is induced by oscillatory flow in vascular endothelial cells through the induction of NADPH oxidase-4 expression. In contrast, laminar flow induces the expression of endothelial nitric oxide synthase and results in the S-nitrosylation of VEGFR2 at Cys1206, which counteracts the oxidative inactivation. The shear stress model study reveals that disturbed blood flow operated by partial ligation in the carotid arteries induces endothelial damage and intimal hyperplasia in control mice but not in knock-in mice harboring the oxidation-resistant mutant (C1206S) of VEGFR2. Thus, our findings reveal that flow-dependent redox regulation of the VEGFR2 kinase is critical for the structural and functional integrity of the arterial endothelium. CP: Cell biology Biology (General) Yerin Kim verfasserin aut Seongchun Min verfasserin aut Su Youn Lee verfasserin aut Ka Young Chung verfasserin aut In-Jeoung Baek verfasserin aut Kihwan Kwon verfasserin aut Hanjoong Jo verfasserin aut Sang Won Kang verfasserin aut In Cell Reports Elsevier, 2015 42(2023), 11, Seite 113361- (DE-627)684964562 (DE-600)2649101-1 22111247 nnns volume:42 year:2023 number:11 pages:113361- https://doi.org/10.1016/j.celrep.2023.113361 kostenfrei https://doaj.org/article/9b602d14b06f45a29435838d47121b5e kostenfrei http://www.sciencedirect.com/science/article/pii/S2211124723013736 kostenfrei https://doaj.org/toc/2211-1247 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2110 GBV_ILN_2112 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2470 GBV_ILN_2507 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4393 GBV_ILN_4700 AR 42 2023 11 113361-
language	English
source	In Cell Reports 42(2023), 11, Seite 113361- volume:42 year:2023 number:11 pages:113361-
sourceStr	In Cell Reports 42(2023), 11, Seite 113361- volume:42 year:2023 number:11 pages:113361-
format_phy_str_mv	Article
institution	findex.gbv.de
topic_facet	CP: Cell biology Biology (General)
isfreeaccess_bool	true
container_title	Cell Reports
authorswithroles_txt_mv	Dong Hoon Kang @@aut@@ Yerin Kim @@aut@@ Seongchun Min @@aut@@ Su Youn Lee @@aut@@ Ka Young Chung @@aut@@ In-Jeoung Baek @@aut@@ Kihwan Kwon @@aut@@ Hanjoong Jo @@aut@@ Sang Won Kang @@aut@@
publishDateDaySort_date	2023-01-01T00:00:00Z
hierarchy_top_id	684964562
id	DOAJ099606380
language_de	englisch
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callnumber-first	Q - Science
author	Dong Hoon Kang
spellingShingle	Dong Hoon Kang misc QH301-705.5 misc CP: Cell biology misc Biology (General) Blood flow patterns switch VEGFR2 activity through differential S-nitrosylation and S-oxidation
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topic_title	QH301-705.5 Blood flow patterns switch VEGFR2 activity through differential S-nitrosylation and S-oxidation CP: Cell biology
topic	misc QH301-705.5 misc CP: Cell biology misc Biology (General)
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title	Blood flow patterns switch VEGFR2 activity through differential S-nitrosylation and S-oxidation
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title_full	Blood flow patterns switch VEGFR2 activity through differential S-nitrosylation and S-oxidation
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author_browse	Dong Hoon Kang Yerin Kim Seongchun Min Su Youn Lee Ka Young Chung In-Jeoung Baek Kihwan Kwon Hanjoong Jo Sang Won Kang
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author-letter	Dong Hoon Kang
doi_str_mv	10.1016/j.celrep.2023.113361
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title_sort	blood flow patterns switch vegfr2 activity through differential s-nitrosylation and s-oxidation
callnumber	QH301-705.5
title_auth	Blood flow patterns switch VEGFR2 activity through differential S-nitrosylation and S-oxidation
abstract	Summary: Vascular endothelial growth factor receptor-2 (VEGFR2) plays a key role in maintaining vascular endothelial homeostasis. Here, we show that blood flows determine activation and inactivation of VEGFR2 through selective cysteine modifications. VEGFR2 activation is regulated by reversible oxidation at Cys1206 residue. H2O2-mediated VEGFR2 oxidation is induced by oscillatory flow in vascular endothelial cells through the induction of NADPH oxidase-4 expression. In contrast, laminar flow induces the expression of endothelial nitric oxide synthase and results in the S-nitrosylation of VEGFR2 at Cys1206, which counteracts the oxidative inactivation. The shear stress model study reveals that disturbed blood flow operated by partial ligation in the carotid arteries induces endothelial damage and intimal hyperplasia in control mice but not in knock-in mice harboring the oxidation-resistant mutant (C1206S) of VEGFR2. Thus, our findings reveal that flow-dependent redox regulation of the VEGFR2 kinase is critical for the structural and functional integrity of the arterial endothelium.
abstractGer	Summary: Vascular endothelial growth factor receptor-2 (VEGFR2) plays a key role in maintaining vascular endothelial homeostasis. Here, we show that blood flows determine activation and inactivation of VEGFR2 through selective cysteine modifications. VEGFR2 activation is regulated by reversible oxidation at Cys1206 residue. H2O2-mediated VEGFR2 oxidation is induced by oscillatory flow in vascular endothelial cells through the induction of NADPH oxidase-4 expression. In contrast, laminar flow induces the expression of endothelial nitric oxide synthase and results in the S-nitrosylation of VEGFR2 at Cys1206, which counteracts the oxidative inactivation. The shear stress model study reveals that disturbed blood flow operated by partial ligation in the carotid arteries induces endothelial damage and intimal hyperplasia in control mice but not in knock-in mice harboring the oxidation-resistant mutant (C1206S) of VEGFR2. Thus, our findings reveal that flow-dependent redox regulation of the VEGFR2 kinase is critical for the structural and functional integrity of the arterial endothelium.
abstract_unstemmed	Summary: Vascular endothelial growth factor receptor-2 (VEGFR2) plays a key role in maintaining vascular endothelial homeostasis. Here, we show that blood flows determine activation and inactivation of VEGFR2 through selective cysteine modifications. VEGFR2 activation is regulated by reversible oxidation at Cys1206 residue. H2O2-mediated VEGFR2 oxidation is induced by oscillatory flow in vascular endothelial cells through the induction of NADPH oxidase-4 expression. In contrast, laminar flow induces the expression of endothelial nitric oxide synthase and results in the S-nitrosylation of VEGFR2 at Cys1206, which counteracts the oxidative inactivation. The shear stress model study reveals that disturbed blood flow operated by partial ligation in the carotid arteries induces endothelial damage and intimal hyperplasia in control mice but not in knock-in mice harboring the oxidation-resistant mutant (C1206S) of VEGFR2. Thus, our findings reveal that flow-dependent redox regulation of the VEGFR2 kinase is critical for the structural and functional integrity of the arterial endothelium.
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title_short	Blood flow patterns switch VEGFR2 activity through differential S-nitrosylation and S-oxidation
url	https://doi.org/10.1016/j.celrep.2023.113361 https://doaj.org/article/9b602d14b06f45a29435838d47121b5e http://www.sciencedirect.com/science/article/pii/S2211124723013736 https://doaj.org/toc/2211-1247
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author2	Yerin Kim Seongchun Min Su Youn Lee Ka Young Chung In-Jeoung Baek Kihwan Kwon Hanjoong Jo Sang Won Kang
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up_date	2024-07-03T23:34:03.743Z
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Blood flow patterns switch VEGFR2 activity through differential S-nitrosylation and S-oxidation

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