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Conference Paper: Molecular dissection of the interplay between SIRT1, LKB1 and HERC2: linkage implication in endothelial senescence and vascular remodeling

TitleMolecular dissection of the interplay between SIRT1, LKB1 and HERC2: linkage implication in endothelial senescence and vascular remodeling
Authors
Bai, BMan, WCLiang, YDeng, HLi, JWang, YVanhoutte, PM
Issue Date2014
PublisherS Karger AG. The Journal's web site is located at http://www.karger.com/JVR
Citation
The 11th International Symposium on Resistance Arteries (ISRA 2014), Banff, AB., Canada, 7-11 September 2014. In Journal of Vascular Research, 2014, v. 51 suppl. 2, p. 132, abstract ISRA156 How to Cite?
DOI: http://dx.doi.org/10.1159/000369652
AbstractEndothelial senescence is one of the earliest events during vascular aging and contributes to vascular remodeling. Sirtuin-1 (SIRT1) elicits its anti-senescent functions in part by mediating proteasome-mediated degradation of LKB1, a pro-senescent protein kinase [1], [2]. The present study was designed to investigate the molecular mechanisms underlying SIRT1-regulated LKB1 degradation by focusing on an E3 ligase, HERC2 (HECT domain and RLD 2 protein). In primary porcine aortic endothelial cells (PAECs), LKB1 degradation was significantly blocked by MG132. Western blotting revealed that LKB1 was ubiquitinated and degraded in nucleus. HERC2 was identified as the E3 ligase of LKB1. Knockdown of HERC2 enhanced the protein accumulation of LKB1 in nucleus and promoted ...
DescriptionSymposium Theme: From Molecular Machinery to Clinical Challenges
Poster Session 3: Late Breaking Abstracts & Vendor Exhibits: no. PS3-4: abstract ISRA156
Persistent Identifierhttp://hdl.handle.net/10722/210382
ISSN
1018-1172
2023 Impact Factor: 1.8
2023 SCImago Journal Rankings: 0.486

 

DC FieldValueLanguage
dc.contributor.authorBai, B-
dc.contributor.authorMan, WC-
dc.contributor.authorLiang, Y-
dc.contributor.authorDeng, H-
dc.contributor.authorLi, J-
dc.contributor.authorWang, Y-
dc.contributor.authorVanhoutte, PM-
dc.date.accessioned2015-06-12T08:08:26Z-
dc.date.available2015-06-12T08:08:26Z-
dc.date.issued2014-
dc.identifier.citationThe 11th International Symposium on Resistance Arteries (ISRA 2014), Banff, AB., Canada, 7-11 September 2014. In Journal of Vascular Research, 2014, v. 51 suppl. 2, p. 132, abstract ISRA156-
dc.identifier.issn1018-1172-
dc.identifier.urihttp://hdl.handle.net/10722/210382-
dc.descriptionSymposium Theme: From Molecular Machinery to Clinical Challenges-
dc.descriptionPoster Session 3: Late Breaking Abstracts & Vendor Exhibits: no. PS3-4: abstract ISRA156-
dc.description.abstractEndothelial senescence is one of the earliest events during vascular aging and contributes to vascular remodeling. Sirtuin-1 (SIRT1) elicits its anti-senescent functions in part by mediating proteasome-mediated degradation of LKB1, a pro-senescent protein kinase [1], [2]. The present study was designed to investigate the molecular mechanisms underlying SIRT1-regulated LKB1 degradation by focusing on an E3 ligase, HERC2 (HECT domain and RLD 2 protein). In primary porcine aortic endothelial cells (PAECs), LKB1 degradation was significantly blocked by MG132. Western blotting revealed that LKB1 was ubiquitinated and degraded in nucleus. HERC2 was identified as the E3 ligase of LKB1. Knockdown of HERC2 enhanced the protein accumulation of LKB1 in nucleus and promoted ...-
dc.languageeng-
dc.publisherS Karger AG. The Journal's web site is located at http://www.karger.com/JVR-
dc.relation.ispartofJournal of Vascular Research-
dc.rightsJournal of Vascular Research. Copyright © S Karger AG.-
dc.titleMolecular dissection of the interplay between SIRT1, LKB1 and HERC2: linkage implication in endothelial senescence and vascular remodeling-
dc.typeConference_Paper-
dc.identifier.emailBai, B: baibohku@hku.hk-
dc.identifier.emailDeng, H: hbdeng1@hku.hk-
dc.identifier.emailWang, Y: yuwanghk@hku.hk-
dc.identifier.emailVanhoutte, PM: vanhoutt@hku.hk-
dc.identifier.authorityWang, Y=rp00239-
dc.identifier.authorityVanhoutte, PM=rp00238-
dc.description.naturepostprint-
dc.identifier.doi10.1159/000369652-
dc.identifier.scopuseid_2-s2.0-84925581525-
dc.identifier.hkuros243589-
dc.identifier.hkuros250012-
dc.identifier.volume51-
dc.identifier.issuesuppl. 2-
dc.identifier.spage132, abstract ISRA156-
dc.identifier.epage132, abstract ISRA156-
dc.publisher.placeSwitzerland-
dc.identifier.issnl1018-1172-

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