Regulation of Cigarette Smoke (CS)-Induced Autophagy by Nrf2
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{"title"=>"Regulation of Cigarette Smoke (CS)-Induced Autophagy by Nrf2", "type"=>"journal", "authors"=>[{"first_name"=>"Lingxiang", "last_name"=>"Zhu", "scopus_author_id"=>"55647955300"}, {"first_name"=>"Erika C.", "last_name"=>"Barret", "scopus_author_id"=>"55915782000"}, {"first_name"=>"Yuxue", "last_name"=>"Xu", "scopus_author_id"=>"57198773983"}, {"first_name"=>"Zuguo", "last_name"=>"Liu", "scopus_author_id"=>"13609468800"}, {"first_name"=>"Aditya", "last_name"=>"Manoharan", "scopus_author_id"=>"55647746500"}, {"first_name"=>"Yin", "last_name"=>"Chen", "scopus_author_id"=>"53065190900"}], "year"=>2013, "source"=>"PLoS ONE", "identifiers"=>{"scopus"=>"2-s2.0-84876064507", "pui"=>"368705060", "pmid"=>"23585825", "issn"=>"19326203", "doi"=>"10.1371/journal.pone.0055695", "sgr"=>"84876064507"}, "id"=>"7a6c7e83-7324-3b05-8ed8-612ff214dc45", "abstract"=>"Cigarette smoke (CS) has been reported to induce autophagy in airway epithelial cells. The subsequent autophagic cell death has been proposed to play an important pathogenic role in chronic obstructive pulmonary disease (COPD); however, the underlying molecular mechanism is not entirely clear. Using CS extract (CSE) as a surrogate for CS, we found that it markedly increased the expressions of both LC3B-I and LC3B-II as well as autophagosomes in airway epithelial cells. This is in contrast to the common autophagy inducer (i.e., starvation) that increases LC3B-II but reduces LC3B-I. Further studies indicate that CSE regulated LC3B at transcriptional and post-translational levels. In addition, CSE, but not starvation, activated Nrf2-mediated adaptive response. Increase of cellular Nrf2 by either Nrf2 overexpression or the knockdown of Keap1 (an Nrf2 inhibitor) significantly repressed CSE-induced LC3B-I and II as well as autophagosomes. Supplement of NAC (a GSH precursor) or GSH recapitulated the effect of Nrf2, suggesting the increase of cellular GSH level is responsible for Nrf2 effect on LC3B and autophagosome. Interestingly, neither Nrf2 activation nor GSH supplement could restore the repressed activities of mTOR or its downstream effctor-S6K. Thus, the Nrf2-dependent autophagy-suppression was not due to the re-activation of mTOR-the master repressor of autophagy. To search for the downstream effector of Nrf2 on LC3B and autophagosome, we tested Nrf2-dependent genes (i.e., NQO1 and P62) that are also increased by CSE treatment. We found that P62, but not NQO1, could mimic the effect of Nrf2 activation by repressing LC3B expression. Thus, Nrf2->P62 appears to play an important role in the regulation of CSE-induced LC3B and autophagosome.", "link"=>"http://www.mendeley.com/research/regulation-cigarette-smoke-csinduced-autophagy-nrf2", "reader_count"=>11, "reader_count_by_academic_status"=>{"Researcher"=>2, "Student > Ph. D. Student"=>5, "Student > Postgraduate"=>1, "Student > Master"=>3}, "reader_count_by_user_role"=>{"Researcher"=>2, "Student > Ph. D. Student"=>5, "Student > Postgraduate"=>1, "Student > Master"=>3}, "reader_count_by_subject_area"=>{"Biochemistry, Genetics and Molecular Biology"=>1, "Agricultural and Biological Sciences"=>6, "Medicine and Dentistry"=>3, "Immunology and Microbiology"=>1}, "reader_count_by_subdiscipline"=>{"Medicine and Dentistry"=>{"Medicine and Dentistry"=>3}, "Immunology and Microbiology"=>{"Immunology and Microbiology"=>1}, "Agricultural and Biological Sciences"=>{"Agricultural and Biological Sciences"=>6}, "Biochemistry, Genetics and Molecular Biology"=>{"Biochemistry, Genetics and Molecular Biology"=>1}}, "group_count"=>0}

Scopus | Further Information

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Figshare

  • {"files"=>["https://ndownloader.figshare.com/files/1019767"], "description"=>"<p>Realtime Primers.</p>", "links"=>[], "tags"=>["Biochemistry", "proteins", "Defense proteins", "Molecular cell biology", "Cellular types", "Epithelial cells", "Nucleic acids", "rna", "RNA interference", "Cell death", "Clinical immunology", "immunity", "Aging and immunity", "Innate immunity", "Pulmonology", "Environmental and occupational lung diseases"], "article_id"=>678810, "categories"=>["Medicine", "Biological Sciences"], "users"=>["Lingxiang Zhu", "Erika C. Barret", "Yuxue Xu", "Zuguo Liu", "Aditya Manoharan", "Yin Chen"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0055695.t001", "stats"=>{"downloads"=>0, "page_views"=>7, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Realtime_Primers_/678810", "title"=>"Realtime Primers.", "pos_in_sequence"=>0, "defined_type"=>3, "published_date"=>"2013-04-09 02:26:50"}
  • {"files"=>["https://ndownloader.figshare.com/files/1019762"], "description"=>"<p>All western blot images were the representative image from at least three independent analyses, and Actin was use as a loading control. A) Time course of CSE induced LC3B and Nrf2. Cells were treated with 10% CSE. At each indicated time point, total protein was collected and subject to western blots analysis. B) CSE increased LC3B steady-state RNA. Cells were treated with 10% CSE. At each indicated time point, total RNA was collected and subject to Real-time PCR analysis. *: p<0.05, n = 5. C) CSE regulates LC3B-I and II at posttranslational levels. Cells were treated with 10% CSE for 24 hrs with either 3-MA (3MA) or lysozymal protease inhibitors-E64D and Pepstatin A (E+P). D) Pulse-chase study. Cells were treated with or without 10% CSE for 24 hrs. Then, CSE was removed and thoroughly washed. The cells were left alone (C) or treated with various inhibitors: cycloheximide (Cy), 3-MA (3MA) or E64D + Pepstatin A (E+P) for additional 6 hrs. Total protein was collected and subject to western blots analysis.</p>", "links"=>[], "tags"=>["Biochemistry", "proteins", "Defense proteins", "Molecular cell biology", "Cellular types", "Epithelial cells", "Nucleic acids", "rna", "RNA interference", "Cell death", "Clinical immunology", "immunity", "Aging and immunity", "Innate immunity", "Pulmonology", "Environmental and occupational lung diseases", "induced", "lc3b"], "article_id"=>678805, "categories"=>["Medicine", "Biological Sciences"], "users"=>["Lingxiang Zhu", "Erika C. Barret", "Yuxue Xu", "Zuguo Liu", "Aditya Manoharan", "Yin Chen"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0055695.g002", "stats"=>{"downloads"=>0, "page_views"=>10, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_CSE_induced_LC3B_through_at_multiple_levels_/678805", "title"=>"CSE induced LC3B through at multiple levels.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-04-09 02:26:45"}
  • {"files"=>["https://ndownloader.figshare.com/files/1019764"], "description"=>"<p>A) Antioxidants neutralized CSE-induced cellular ROS. Cells were treated with 10% CSE or plus NAC (CSE+NAC) or GSH (CSE+GSH). Images were recorded 30 min after dye loading. Green fluorescence indicates generation of reactive oxygen species that oxidized the dye to emit fluorescence. B) Antioxidants downregulated CSE-induced LC3B. C) Antioxidants downregulated CSE-induced autophagosome. D) Quantification of autophagosome (GFP-LC3B+ dots) was described in Materials and Methods. *, $: p<0.05, n = 3.</p>", "links"=>[], "tags"=>["Biochemistry", "proteins", "Defense proteins", "Molecular cell biology", "Cellular types", "Epithelial cells", "Nucleic acids", "rna", "RNA interference", "Cell death", "Clinical immunology", "immunity", "Aging and immunity", "Innate immunity", "Pulmonology", "Environmental and occupational lung diseases", "supplement", "repressed", "cse-induced", "lc3b"], "article_id"=>678807, "categories"=>["Medicine", "Biological Sciences"], "users"=>["Lingxiang Zhu", "Erika C. Barret", "Yuxue Xu", "Zuguo Liu", "Aditya Manoharan", "Yin Chen"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0055695.g004", "stats"=>{"downloads"=>0, "page_views"=>12, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Antioxidant_supplement_repressed_CSE_induced_LC3B_and_autophagosome_/678807", "title"=>"Antioxidant supplement repressed CSE-induced LC3B and autophagosome.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-04-09 02:26:47"}
  • {"files"=>["https://ndownloader.figshare.com/files/1019765"], "description"=>"<p>All western blot images were the representative image from at least three independent analyses, and Actin was use as a loading control. A) NQO1 knockdown couldn't rescue Keap1 knockdown. Cells were transfected with siRNA control (siC), siRNA against NQO1 (siN), siRNA against Keap1 (siK), and their combinations as indicated. 24 hrs later, cells were treated without or with 10% CSE for 24 hrs. Total proteins were collected for western blot analysis. B) P62 knockdown couldn't rescue Keap1 knockdown. Cells were transfected with siRNA control (siC), siRNA against P62 (siP), siRNA against Keap1 (siK), and their combinations as indicated. 24 hrs later, cells were treated without or with 10% CSE for 24 hrs. Total proteins were collected for western blot analysis. C) Effect of P62 overexpression. Cells were transfected with P62 plasmid (P62) or empty vector (PCDNA3, or PC). 24 hrs later, cells were treated without (C) or with (CSE) at increasing doses (8%, 10%, 12%) for 24 hrs. D) overexpression of P62 represses LC3B. Cells stably transfected with GFP-LC3B were transfected with P62 plasmid (P62) or empty vector (PCDNA3, or PC). These cells were treated without (C) or with (CSE) 10% CSE for 24 hrs. Live images were recorded. “punctate dots” of GFP-LC3B were the indication of autophagosomes. E) Quantification of autophagosome (GFP-LC3B+ dots) was described in Materials and Methods. *, $: p<0.05, n = 3.</p>", "links"=>[], "tags"=>["Biochemistry", "proteins", "Defense proteins", "Molecular cell biology", "Cellular types", "Epithelial cells", "Nucleic acids", "rna", "RNA interference", "Cell death", "Clinical immunology", "immunity", "Aging and immunity", "Innate immunity", "Pulmonology", "Environmental and occupational lung diseases", "replicated", "nrf2"], "article_id"=>678808, "categories"=>["Medicine", "Biological Sciences"], "users"=>["Lingxiang Zhu", "Erika C. Barret", "Yuxue Xu", "Zuguo Liu", "Aditya Manoharan", "Yin Chen"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0055695.g005", "stats"=>{"downloads"=>1, "page_views"=>16, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_P62_but_not_NQO1_replicated_Nrf2_phenotype_/678808", "title"=>"P62, but not NQO1, replicated Nrf2 phenotype.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-04-09 02:26:48"}
  • {"files"=>["https://ndownloader.figshare.com/files/1019763"], "description"=>"<p>All western blot images were the representative image from at least three independent analyses, and Actin was use as a loading control. A) Effect of Nrf2 overexpression. Cells were transfected with Nrf2 plasmid (Nrf2) or empty vector (PCDNA3, or PC). 24 hrs later, cells were treated without (C) or with (CSE) 10% CSE for 24 hrs. B) Effect of siRNA knockdown of siNrf2 and/or Keap1. Cells were transfected with siRNA control (siC), siRNA against Nrf2 (siNrf2), siRNA against Keap1 (siKeap1), and siNrf2+siKeap1 (siN+K). 24 hrs later, cells were treated without (C) or with (CSE) 10% CSE for 24 hrs. C) Negative regulation of autophagosome by Nrf2. Cells stably transfected with GFP-LC3B were transfected with Nrf2 plasmid (Nrf2) or siRNA against Keap1 (siKeap1). Control was the mock-transfected cells. These cells were treated without (C) or with (CSE) 10% CSE for 24 hrs. Live images were recorded. “punctate dots” of GFP-LC3B were the indication of autophagosomes. D) Quantification of autophagosome (GFP-LC3B+ dots) was described in Materials and Methods. *, $: p<0.05, n = 3.</p>", "links"=>[], "tags"=>["Biochemistry", "proteins", "Defense proteins", "Molecular cell biology", "Cellular types", "Epithelial cells", "Nucleic acids", "rna", "RNA interference", "Cell death", "Clinical immunology", "immunity", "Aging and immunity", "Innate immunity", "Pulmonology", "Environmental and occupational lung diseases", "negatively", "lc3b"], "article_id"=>678806, "categories"=>["Medicine", "Biological Sciences"], "users"=>["Lingxiang Zhu", "Erika C. Barret", "Yuxue Xu", "Zuguo Liu", "Aditya Manoharan", "Yin Chen"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0055695.g003", "stats"=>{"downloads"=>1, "page_views"=>42, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Nrf2_negatively_regulate_LC3B_I_and_II_/678806", "title"=>"Nrf2 negatively regulate LC3B I and II.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-04-09 02:26:46"}
  • {"files"=>["https://ndownloader.figshare.com/files/1019760"], "description"=>"<p>All western blot images were the representative image from at least three independent analyses, and Actin was use as a loading control. A) Increase of cellular autophagosome by live imaging. Cells stably transfected with GFP-LC3B were treated either with 10% CSE for 24 hrs or were immersed in HBSS buffer (starvation or S) for 6 hrs. Control (C) was sham (medium)-treated sample. Live images were recorded. “punctate dots” of GFP-LC3B were the indication of autophagosomes. B) Starvation induced autophagy but not Nrf2. Cells were immersed in HBSS (S) without or with 3-Methyladenine (3-MA). Total protein was collected at the indicated time point and subject to western blot analysis. C) CSE induced both autophagy and Nrf2. Cells were treated with different dose (as indicated in the figure) for either 6 hrs or 24 hrs. Total protein was collected and subject to western analysis. D) CSE induced ARE-reporter activation. Two different ARE-reporters were transfected into cells. 24 hrs later, the cells were treated with 10% CSE for 24 hrs or immersed in HBSS (S) for 6 hrs. Cell lysates were prepared and subject to dual luciferase assay. Relative luciferase unit (RLU) was calculated as described in the Materials and Methods. Fold induction  =  RLU of treated cells/RLU of control cells. *: p<0.05, n = 5. NS: not significant.</p>", "links"=>[], "tags"=>["Biochemistry", "proteins", "Defense proteins", "Molecular cell biology", "Cellular types", "Epithelial cells", "Nucleic acids", "rna", "RNA interference", "Cell death", "Clinical immunology", "immunity", "Aging and immunity", "Innate immunity", "Pulmonology", "Environmental and occupational lung diseases", "autophagy", "starvation-induced", "airway", "epithelial"], "article_id"=>678803, "categories"=>["Medicine", "Biological Sciences"], "users"=>["Lingxiang Zhu", "Erika C. Barret", "Yuxue Xu", "Zuguo Liu", "Aditya Manoharan", "Yin Chen"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0055695.g001", "stats"=>{"downloads"=>0, "page_views"=>16, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_CSE_enhanced_autophagy_is_different_from_the_starvation_induced_autophagy_in_airway_epithelial_cells_/678803", "title"=>"CSE-enhanced autophagy is different from the starvation-induced autophagy in airway epithelial cells.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-04-09 02:26:43"}

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Relative Metric

{"start_date"=>"2013-01-01T00:00:00Z", "end_date"=>"2013-12-31T00:00:00Z", "subject_areas"=>[{"subject_area"=>"/Biology and life sciences", "average_usage"=>[269, 466, 588, 697, 800, 896, 988, 1076, 1165, 1254, 1340, 1417]}, {"subject_area"=>"/Biology and life sciences/Biochemistry", "average_usage"=>[266, 468, 593, 703, 804, 903, 993, 1084, 1171, 1256, 1339, 1422, 1492]}, {"subject_area"=>"/Biology and life sciences/Genetics", "average_usage"=>[284, 491, 620, 738, 843, 945, 1043, 1137, 1225, 1315, 1400, 1479, 1555]}, {"subject_area"=>"/Medicine and health sciences/Pulmonology", "average_usage"=>[241, 428, 552, 659, 752, 848, 934, 1028, 1106, 1183, 1267, 1350, 1401]}]}
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