For Publishers
DiscoveryMetadataPeer reviewHostingPublishing
For Researchers
JoinPublishReviewCollect
Register
Blog
About
Search
Advanced search
My ScienceOpen
Search
For Publishers
For Researchers
Blog
About
11
views
33
references
 Top references
cited by
16
    
0 reviews
 Review
0
comments
 Comment
0
recommends
+1 Recommend
0 collections
    0
    shares
      774
      similar
       All similar
      • Record: found
      • Abstract: found
      • Article: found
      Is Open Access

      Caveolin 1-related autophagy initiated by aldosterone-induced oxidation promotes liver sinusoidal endothelial cells defenestration

      research-article
      Author(s): a , f , 1 , a , 1 , b , c , a , a , a , a , d , a , a , e , * , a , f , **
      Publication date (Electronic):
      Journal: Redox Biology
      Publisher: Elsevier
      Keywords: 3MA, 3-methyladenine, AMPK, AMP-activated protein kinase, ATP, adenosine triphosphate, ATP1B2, ATPase Na+/K+ transporting subunit beta 2, BDL, bile duct ligation, Cav1, Caveolin 1, CD31, platelet endothelial cell adhesion molecule-1, PECAM-1, cGMP, cyclic guanosine monophosphate, eNOS, endothelial nitric oxide synthase, LC3, microtubule-associated protein 1 light chain 3, LSEC, liver sinusoidal endothelial cell, MR, mineralocorticoid receptor, NAC, N-acetyl-L-cysteine, NO, nitric oxide, PKG, protein kinase G, ROS, reactive oxygen species, SEM, scanning electron microscopy, sGC, soluble guanylatecyclase, TEMPO, 2,2,6,6-tetramethylpiperidinooxy, mito-TEMPO, mitochondria 2,2,6,6-tetramethylpiperidinooxy, TEM, transmission electron microscopy, ULK1, unc-51 like autophagy activating kinase 1, VASP, vasodilator-stimulated phosphoprotein, vWF, von Willebrand Factor, Autophagy, Liver sinusoidal endothelial cell, Defenestration, Aldosterone, Caveolin 1, Oxidation

      Read this article at

      ScienceOpenPublisherPMC
      Bookmark
          There is no author summary for this article yet. Authors can add summaries to their articles on ScienceOpen to make them more accessible to a non-specialist audience.

          Abstract

          Aldosterone, with pro-oxidation and pro-autophagy capabilities, plays a key role in liver fibrosis. However, the mechanisms underlying aldosterone-promoted liver sinusoidal endothelial cells (LSECs) defenestration remain unknown. Caveolin 1 (Cav1) displays close links with autophagy and fenestration. Hence, we aim to investigate the role of Cav1-related autophagy in LSECs defenestration. We found the increase of aldosterone/MR (mineralocorticoid receptor) level, oxidation, autophagy, and defenestration in LSECs in the human fibrotic liver, BDL or hyperaldosteronism models; while antagonizing aldosterone or inhibiting autophagy relieved LSECs defenestration in BDL-induced fibrosis or hyperaldosteronism models. In vitro, fenestrae of primary LSECs gradually shrank, along with the down-regulation of the NO-dependent pathway and the augment of the AMPK-dependent autophagy; these effects were aggravated by rapamycin (an autophagy activator) or aldosterone treatment. Additionally, aldosterone increased oxidation mediated by Cav1, reduced ATP generation, and subsequently induced the AMPK-dependent autophagy, leading to the down-regulation of the NO-dependent pathway and LSECs defenestration. These effects were reversed by MR antagonist spironolactone, antioxidants or autophagy inhibitors. Besides, aldosterone enhanced the co-immunoprecipitation of Cav1 with p62 and ubiquitin, and induced Cav1 co-immunofluorescence staining with LC3, ubiquitin, and F-actin in the perinuclear area of LSECs. Furthermore, aldosterone treatment increased the membrane protein level of Cav1, whereas decrease the cytoplasmic protein level of Cav1, indicating that aldosterone induced Cav1-related selective autophagy and F-actin remodeling to promote defenestration. Consequently, Cav1-related selective autophagy initiated by aldosterone-induced oxidation promotes LSECs defenestration via activating the AMPK-ULK1 pathway and inhibiting the NO-dependent pathway.

          Related collections

          Most cited references33

          • Record: found
          • Abstract: found
          • Article: not found

          HDAC6 controls autophagosome maturation essential for ubiquitin-selective quality-control autophagy.

          Joo-Yong Lee, Hiroshi Koga, Yoshiharu Kawaguchi … (2010)
          Autophagy is primarily considered a non-selective degradation process induced by starvation. Nutrient-independent basal autophagy, in contrast, imposes intracellular QC by selective disposal of aberrant protein aggregates and damaged organelles, a process critical for suppressing neurodegenerative diseases. The molecular mechanism that distinguishes these two fundamental autophagic responses, however, remains mysterious. Here, we identify the ubiquitin-binding deacetylase, histone deacetylase-6 (HDAC6), as a central component of basal autophagy that targets protein aggregates and damaged mitochondria. Surprisingly, HDAC6 is not required for autophagy activation; rather, it controls the fusion of autophagosomes to lysosomes. HDAC6 promotes autophagy by recruiting a cortactin-dependent, actin-remodelling machinery, which in turn assembles an F-actin network that stimulates autophagosome-lysosome fusion and substrate degradation. Indeed, HDAC6 deficiency leads to autophagosome maturation failure, protein aggregate build-up, and neurodegeneration. Remarkably, HDAC6 and F-actin assembly are completely dispensable for starvation-induced autophagy, uncovering the fundamental difference of these autophagic modes. Our study identifies HDAC6 and the actin cytoskeleton as critical components that define QC autophagy and uncovers a novel regulation of autophagy at the level of autophagosome-lysosome fusion.
          Article 0 comments Cited 254 times – based on 0 reviews     Review now
            Bookmark
            • Record: found
            • Abstract: found
            • Article: not found

            Liver sinusoidal endothelial cells in hepatic fibrosis.

            Laurie DeLeve (2015)
            Capillarization, lack of liver sinusoidal endothelial cell (LSEC) fenestration, and formation of an organized basement membrane not only precedes fibrosis, but is also permissive for hepatic stellate cell activation and fibrosis. Thus, dysregulation of the LSEC phenotype is a critical step in the fibrotic process. Both a vascular endothelial growth factor (VEGF)-stimulated, nitric oxide (NO)-independent pathway and a VEGF-stimulated NO-dependent pathway are necessary to maintain the differentiated LSEC phenotype. The NO-dependent pathway is impaired in capillarization and activation of this pathway downstream from NO restores LSEC differentiation in vivo. Restoration of LSEC differentiation in vivo promotes HSC quiescence, enhances regression of fibrosis, and prevents progression of cirrhosis.
            Article 0 comments Cited 144 times – based on 0 reviews     Review now
              Bookmark
              • Record: found
              • Abstract: found
              • Article: not found

              A role for autophagy during hepatic stellate cell activation.

              Etienne Sokal, Lien F R Thoen, Eduardo Guimarães … (2011)
              Autophagy is a metabolic process that degrades and recycles intracellular organelles and proteins with many connections to human disease and physiology. We studied the role of autophagy during hepatic stellate cell (HSC) activation, a key event in liver fibrogenesis. Analysis of the autophagic flux during in vitro activation of primary mouse HSCs was performed using a DsRed-GFP-LC3B encoding plasmid. The effect of autophagy inhibition by bafilomycin A1 on the in vitro activation process of human and mouse HSCs was examined by measuring proliferation, presence of activation markers by RT-qPCR, immunofluorescence, and Western blotting. Analysis of lipid droplet and microtubule-associated protein light chain 3 beta (LC3B) colocalization in the presence of PDGF-BB was investigated by immunocytochemistry. A significant increased autophagic flux was observed during culture induced mouse HSC activation. Treatment of mouse HSCs and human HSCs with autophagy inhibitor bafilomycin A1 results in a significant decreased proliferation and expression of activation markers. In addition, lipid droplets and LC3B colocalization was increased after PDGF-BB treatment in quiescent HSCs. During HSC activation, autophagic flux is increased. The demonstration of partly inhibition of in vitro HSC activation after treatment with an autophagy inhibitor unveils a potential new therapeutic strategy for liver fibrosis. Copyright © 2011 European Association for the Study of the Liver. Published by Elsevier B.V. All rights reserved.
              Article 0 comments Cited 143 times – based on 0 reviews     Review now
                Bookmark
                All references

                Author and article information

                Contributors
                Ying Meng
                Xu Li
                Journal
                Journal ID (nlm-ta): Redox Biol
                Journal ID (iso-abbrev): Redox Biol
                Title: Redox Biology
                Publisher: Elsevier
                ISSN (Electronic): 2213-2317
                Publication date PMC-release: 13 July 2017
                Publication date Collection: October 2017
                Publication date (Electronic): 13 July 2017
                Volume: 13
                Pages: 508-521
                Affiliations
                [a ]Guangdong Provincial Key Laboratory of Gastroenterology, Department of Gastroenterology, Nanfang Hospital, Southern Medical University, Guangzhou, China
                [b ]Department of Hepatobiliary Surgery, Guizhou Provincial People's Hospital, No. 52 Zhongshan East Road Nanming District, Guiyang, Guizhou Province, China
                [c ]Southern Medical University, Guangzhou, China
                [d ]Department of Emergency and Critical Care Medicine, Guangdong General Hospital & Guangdong Academy of Medical Sciences, Guangzhou, China
                [e ]Department of Respiratory Diseases, Nanfang Hospital, Southern Medical University, Guangzhou, China
                [f ]State Key Laboratory of Organ Failure Research, Guangdong Provincial Key Laboratory of Viral Hepatitis Research, Department of Infectious Diseases, Nanfang Hospital, Southern Medical University, Guangzhou, China
                Author notes
                [* ]Correspondence to:Department of Respiratory Diseases, Nanfang Hospital, Southern Medical University, Guangzhou, China 510515. 519343749@ 123456qq.com
                [** ]Correspondence to:State Key Laboratory of Organ Failure Research, Guangdong Provincial Key Laboratory of Viral Hepatitis Research, Department of Infectious Diseases, Nanfang Hospital, Southern Medical University, Guangzhou, 510515, China. mylx99@ 123456163.com
                [1]

                These authors contributed equally to this work.

                Article
                Publisher ID: S2213-2317(17)30271-9
                DOI: 10.1016/j.redox.2017.07.011
                PMC ID: 5521033
                PubMed ID: 28734243
                SO-VID: 1cb0fd2a-1af6-41e4-8190-541349da8b46
                Copyright © © 2017 The Authors
                License:

                This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).

                History
                Date received : 14 April 2017
                Date revision received : 12 June 2017
                Date accepted : 12 July 2017
                Categories
                Subject: Research Paper

                Keywords: 3ma, 3-methyladenine,ampk, amp-activated protein kinase,atp, adenosine triphosphate,atp1b2, atpase na+/k+ transporting subunit beta 2,bdl, bile duct ligation,cav1, caveolin 1,cd31, platelet endothelial cell adhesion molecule-1, pecam-1,cgmp, cyclic guanosine monophosphate,enos, endothelial nitric oxide synthase,lc3, microtubule-associated protein 1 light chain 3,lsec, liver sinusoidal endothelial cell,mr, mineralocorticoid receptor,nac, n-acetyl-l-cysteine,no, nitric oxide,pkg, protein kinase g,ros, reactive oxygen species,sem, scanning electron microscopy,sgc, soluble guanylatecyclase,tempo, 2,2,6,6-tetramethylpiperidinooxy,mito-tempo, mitochondria 2,2,6,6-tetramethylpiperidinooxy,tem, transmission electron microscopy,ulk1, unc-51 like autophagy activating kinase 1,vasp, vasodilator-stimulated phosphoprotein,vwf, von willebrand factor,autophagy,liver sinusoidal endothelial cell,defenestration,aldosterone,caveolin 1,oxidation
                Data availability:
                Keywords: 3ma, 3-methyladenine, ampk, amp-activated protein kinase, atp, adenosine triphosphate, atp1b2, atpase na+/k+ transporting subunit beta 2, bdl, bile duct ligation, cav1, caveolin 1, cd31, platelet endothelial cell adhesion molecule-1, pecam-1, cgmp, cyclic guanosine monophosphate, enos, endothelial nitric oxide synthase, lc3, microtubule-associated protein 1 light chain 3, lsec, liver sinusoidal endothelial cell, mr, mineralocorticoid receptor, nac, n-acetyl-l-cysteine, no, nitric oxide, pkg, protein kinase g, ros, reactive oxygen species, sem, scanning electron microscopy, sgc, soluble guanylatecyclase, tempo, 2,2,6,6-tetramethylpiperidinooxy, mito-tempo, mitochondria 2,2,6,6-tetramethylpiperidinooxy, tem, transmission electron microscopy, ulk1, unc-51 like autophagy activating kinase 1, vasp, vasodilator-stimulated phosphoprotein, vwf, von willebrand factor, autophagy, liver sinusoidal endothelial cell, defenestration, aldosterone, caveolin 1, oxidation

                Comments

                Comment on this article

                scite_

                Similar content774

                See all similar

                Cited by16

                See all cited by

                Most referenced authors697

                See all reference authors