Hsc70 Contributes to Cancer Cell Survival by Preventing Rab1A Degradation under Stress Conditions
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{"title"=>"Hsc70 contributes to cancer cell survival by preventing Rab1A degradation under stress conditions", "type"=>"journal", "authors"=>[{"first_name"=>"Masako", "last_name"=>"Tanaka", "scopus_author_id"=>"37038633200"}, {"first_name"=>"Saya", "last_name"=>"Mun", "scopus_author_id"=>"37038016500"}, {"first_name"=>"Akihito", "last_name"=>"Harada", "scopus_author_id"=>"35503273400"}, {"first_name"=>"Yasuyuki", "last_name"=>"Ohkawa", "scopus_author_id"=>"8415064400"}, {"first_name"=>"Azusa", "last_name"=>"Inagaki", "scopus_author_id"=>"55995097400"}, {"first_name"=>"Soichi", "last_name"=>"Sano", "scopus_author_id"=>"56035761100"}, {"first_name"=>"Katsuyuki", "last_name"=>"Takahashi", "scopus_author_id"=>"55994525400"}, {"first_name"=>"Yasukatsu", "last_name"=>"Izumi", "scopus_author_id"=>"7202179110"}, {"first_name"=>"Mayuko", "last_name"=>"Osada-Oka", "scopus_author_id"=>"57197724941"}, {"first_name"=>"Hideki", "last_name"=>"Wanibuchi", "scopus_author_id"=>"7005061080"}, {"first_name"=>"Masayo", "last_name"=>"Yamagata", "scopus_author_id"=>"7007008362"}, {"first_name"=>"Tokihito", "last_name"=>"Yukimura", "scopus_author_id"=>"7006581137"}, {"first_name"=>"Katsuyuki", "last_name"=>"Miura", "scopus_author_id"=>"56496123000"}, {"first_name"=>"Masayuki", "last_name"=>"Shiota", "scopus_author_id"=>"8878097500"}, {"first_name"=>"Hiroshi", "last_name"=>"Iwao", "scopus_author_id"=>"7005585900"}], "year"=>2014, "source"=>"PLoS ONE", "identifiers"=>{"pmid"=>"24801886", "doi"=>"10.1371/journal.pone.0096785", "sgr"=>"84900412166", "scopus"=>"2-s2.0-84900412166", "issn"=>"19326203", "pui"=>"373074598"}, "id"=>"0e127698-4021-37c7-bbf8-f8cf0ad1df9d", "abstract"=>"Heat shock cognate protein 70 (Hsc70) acts as a molecular chaperone for the maintenance of intracellular proteins, which allows cancer cells to survive under proteotoxic stress. We attempted to use Hsc70 to identify key molecules in cancer cell survival. Here, we performed mass-spectrometry-based proteomics analysis utilizing affinity purification with anti-Hsc70 antibodies; as a result, 83 differentially expressed proteins were identified under stress conditions. This result implies that there was a change in the proteins with which Hsc70 interacted in response to stress. Among the proteins identified under both serum-depleted and 5-fluorouracil-treated conditions, Rab1A was identified as an essential molecule for cancer cell survival. Hsc70 interacted with Rab1A in a chaperone-dependent manner. In addition, Hsc70 knockdown decreased the level of Rab1A and increased the level of its ubiquitination under stress conditions, suggesting that Hsc70 prevented the degradation of Rab1A denatured by stress exposure. We also found that Rab1A knockdown induced cell death by inhibition of autophagosome formation. Rab1A may therefore contribute to overcoming proteotoxic insults, which allows cancer cells to survive under stress conditions. Analysis of Hsc70 interactors provided insight into changes of intracellular status. We expect further study of the Hsc70 interactome to provide a more comprehensive understanding of cancer cell physiology.", "link"=>"http://www.mendeley.com/research/hsc70-contributes-cancer-cell-survival-preventing-rab1a-degradation-under-stress-conditions", "reader_count"=>66, "reader_count_by_academic_status"=>{"Professor > Associate Professor"=>1, "Researcher"=>23, "Student > Ph. D. Student"=>11, "Student > Postgraduate"=>2, "Other"=>24, "Student > Master"=>3, "Student > Bachelor"=>1, "Professor"=>1}, "reader_count_by_user_role"=>{"Professor > Associate Professor"=>1, "Researcher"=>23, "Student > Ph. D. Student"=>11, "Student > Postgraduate"=>2, "Other"=>24, "Student > Master"=>3, "Student > Bachelor"=>1, "Professor"=>1}, "reader_count_by_subject_area"=>{"Unspecified"=>1, "Engineering"=>1, "Biochemistry, Genetics and Molecular Biology"=>5, "Mathematics"=>1, "Agricultural and Biological Sciences"=>52, "Medicine and Dentistry"=>2, "Neuroscience"=>1, "Chemistry"=>2, "Immunology and Microbiology"=>1}, "reader_count_by_subdiscipline"=>{"Engineering"=>{"Engineering"=>1}, "Medicine and Dentistry"=>{"Medicine and Dentistry"=>2}, "Neuroscience"=>{"Neuroscience"=>1}, "Chemistry"=>{"Chemistry"=>2}, "Immunology and Microbiology"=>{"Immunology and Microbiology"=>1}, "Agricultural and Biological Sciences"=>{"Agricultural and Biological Sciences"=>52}, "Biochemistry, Genetics and Molecular Biology"=>{"Biochemistry, Genetics and Molecular Biology"=>5}, "Mathematics"=>{"Mathematics"=>1}, "Unspecified"=>{"Unspecified"=>1}}, "reader_count_by_country"=>{"United States"=>1}, "group_count"=>1}

Scopus | Further Information

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Figshare

  • {"files"=>["https://ndownloader.figshare.com/files/1486606"], "description"=>"<p>HT29 cells were transfected with siRNA for <i>Rab1A</i> or scramble control. Protein identification in Rab1A knockdown cells was performed through quantitative proteomics by stable isotope labeling, using iTRAQ. (A) Upregulated proteins with iTRAQ ratio ≥1.2. (B) Downregulated proteins with iTRAQ ratio <0.8.</p>", "links"=>[], "tags"=>["Biochemistry", "proteins", "protein structure", "Protein folding", "Chaperone proteins", "Protein interactions", "proteomes", "proteomics", "Spectrometric identification of proteins", "cell biology", "Cell processes", "Cellular stress responses", "Molecular cell biology", "oncology", "Cancers and neoplasms", "carcinomas", "adenocarcinomas", "Colon adenocarcinoma", "Basic cancer research", "annotation", "upregulated", "downregulated", "rab1a", "knockdown"], "article_id"=>1017729, "categories"=>["Biological Sciences"], "users"=>["Masako Tanaka", "Saya Mun", "Akihito Harada", "Yasuyuki Ohkawa", "Azusa Inagaki", "Soichi Sano", "Katsuyuki Takahashi", "Yasukatsu Izumi", "Mayuko Osada-Oka", "Hideki Wanibuchi", "Masayo Yamagata", "Tokihito Yukimura", "Katsuyuki Miura", "Masayuki Shiota", "Hiroshi Iwao"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0096785.g006", "stats"=>{"downloads"=>1, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Functional_annotation_of_upregulated_or_downregulated_proteins_in_Rab1A_knockdown_cells_/1017729", "title"=>"Functional annotation of upregulated or downregulated proteins in Rab1A knockdown cells.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2014-05-06 03:07:24"}
  • {"files"=>["https://ndownloader.figshare.com/files/1486607"], "description"=>"<p>(A) BFA induced cell death differently from Rab1A knockdown. HT29 cells were transfected with <i>Hsc70</i> or <i>control</i> siRNA and untransfected cells were treated with 5 µg/ml BFA or DMSO at the onset of IncuCyte cell growth assay. Images were captured to monitor proliferation by IncuCyte inside a cell culture incubator. (B) Phase-contrast images at 48 h after the onset of measurement. Scale bar, 200 µm. (C) Inhibition of autophagy was not caused by the interruption of ER-Golgi traffic. Rab1A knockdown or control cells were subjected to serum depletion, 5-FU, or vehicle treatment for 24 h. Untransfected cells were treated with 5 µg/mL BFA for 6 h, and immunoblotted with anti-p62, LC3B, or Rab1A. β-actin was used as a loading control. (D) Hsc70 knockdown allowed autophagosome formation. HT29 cells transfected with <i>Hsc70</i>, <i>Rab1A</i>, <i>Ran</i>, or <i>control</i> siRNA were subjected to serum depletion or vehicle treatment for 24 h, and immunoblotted. Immunoblotting data are representative of at least two separate experiments yielding similar results.</p>", "links"=>[], "tags"=>["Biochemistry", "proteins", "protein structure", "Protein folding", "Chaperone proteins", "Protein interactions", "proteomes", "proteomics", "Spectrometric identification of proteins", "cell biology", "Cell processes", "Cellular stress responses", "Molecular cell biology", "oncology", "Cancers and neoplasms", "carcinomas", "adenocarcinomas", "Colon adenocarcinoma", "Basic cancer research", "caused", "inhibition", "autophagy", "er-golgi"], "article_id"=>1017730, "categories"=>["Biological Sciences"], "users"=>["Masako Tanaka", "Saya Mun", "Akihito Harada", "Yasuyuki Ohkawa", "Azusa Inagaki", "Soichi Sano", "Katsuyuki Takahashi", "Yasukatsu Izumi", "Mayuko Osada-Oka", "Hideki Wanibuchi", "Masayo Yamagata", "Tokihito Yukimura", "Katsuyuki Miura", "Masayuki Shiota", "Hiroshi Iwao"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0096785.g007", "stats"=>{"downloads"=>2, "page_views"=>24, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Rab1A_knockdown_induced_cell_death_was_caused_by_inhibition_of_autophagy_but_not_ER_Golgi_traffic_/1017730", "title"=>"Rab1A-knockdown-induced cell death was caused by inhibition of autophagy but not ER-Golgi traffic.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2014-05-06 03:07:24"}
  • {"files"=>["https://ndownloader.figshare.com/files/1486611", "https://ndownloader.figshare.com/files/1486612", "https://ndownloader.figshare.com/files/1486613", "https://ndownloader.figshare.com/files/1486614", "https://ndownloader.figshare.com/files/1486615"], "description"=>"<div><p>Heat shock cognate protein 70 (Hsc70) acts as a molecular chaperone for the maintenance of intracellular proteins, which allows cancer cells to survive under proteotoxic stress. We attempted to use Hsc70 to identify key molecules in cancer cell survival. Here, we performed mass-spectrometry-based proteomics analysis utilizing affinity purification with anti-Hsc70 antibodies; as a result, 83 differentially expressed proteins were identified under stress conditions. This result implies that there was a change in the proteins with which Hsc70 interacted in response to stress. Among the proteins identified under both serum-depleted and 5-fluorouracil-treated conditions, Rab1A was identified as an essential molecule for cancer cell survival. Hsc70 interacted with Rab1A in a chaperone-dependent manner. In addition, Hsc70 knockdown decreased the level of Rab1A and increased the level of its ubiquitination under stress conditions, suggesting that Hsc70 prevented the degradation of Rab1A denatured by stress exposure. We also found that Rab1A knockdown induced cell death by inhibition of autophagosome formation. Rab1A may therefore contribute to overcoming proteotoxic insults, which allows cancer cells to survive under stress conditions. Analysis of Hsc70 interactors provided insight into changes of intracellular status. We expect further study of the Hsc70 interactome to provide a more comprehensive understanding of cancer cell physiology.</p></div>", "links"=>[], "tags"=>["Biochemistry", "proteins", "protein structure", "Protein folding", "Chaperone proteins", "Protein interactions", "proteomes", "proteomics", "Spectrometric identification of proteins", "cell biology", "Cell processes", "Cellular stress responses", "Molecular cell biology", "oncology", "Cancers and neoplasms", "carcinomas", "adenocarcinomas", "Colon adenocarcinoma", "Basic cancer research", "contributes", "cancer", "preventing", "rab1a", "degradation"], "article_id"=>1017734, "categories"=>["Biological Sciences"], "users"=>["Masako Tanaka", "Saya Mun", "Akihito Harada", "Yasuyuki Ohkawa", "Azusa Inagaki", "Soichi Sano", "Katsuyuki Takahashi", "Yasukatsu Izumi", "Mayuko Osada-Oka", "Hideki Wanibuchi", "Masayo Yamagata", "Tokihito Yukimura", "Katsuyuki Miura", "Masayuki Shiota", "Hiroshi Iwao"], "doi"=>["https://dx.doi.org/10.1371/journal.pone.0096785.s001", "https://dx.doi.org/10.1371/journal.pone.0096785.s002", "https://dx.doi.org/10.1371/journal.pone.0096785.s003", "https://dx.doi.org/10.1371/journal.pone.0096785.s004", "https://dx.doi.org/10.1371/journal.pone.0096785.s005"], "stats"=>{"downloads"=>22, "page_views"=>13, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Hsc70_Contributes_to_Cancer_Cell_Survival_by_Preventing_Rab1A_Degradation_under_Stress_Conditions_/1017734", "title"=>"Hsc70 Contributes to Cancer Cell Survival by Preventing Rab1A Degradation under Stress Conditions", "pos_in_sequence"=>0, "defined_type"=>4, "published_date"=>"2014-05-06 03:07:24"}
  • {"files"=>["https://ndownloader.figshare.com/files/1486585"], "description"=>"<p>(A) Knockdown of Hsc70 decreased cancer cell viability. HT29 cells were transfected with siRNA for <i>Hsc70</i> or scramble control. At 48 h after transfection of siRNA, cells were subjected to serum starvation or were treated with 5-FU at the indicated concentration for 48 h. Cell viability was determined by MTS assay. Data points represent the mean ± S.D. (n = 5). (B) Effect of Hsc70 knockdown on cellular morphology. Hsc70 or control knockdown cells were treated the same as in <i>A</i>. Phase-contrast images of cells under serum-fed or serum-free conditions 24 h after treatments. Scale bar, 200 µm. (C) Hsc70 knockdown induced compensatory expression of Hsp72. At 48 h after transfection of siRNA, Hsc70 knockdown or control cells were subjected to serum depletion for 6, 12, or 24 h. After cell lysis, Hsc70 and Hsp72 were detected by immunoblotting. SD, serum depletion.</p>", "links"=>[], "tags"=>["Biochemistry", "proteins", "protein structure", "Protein folding", "Chaperone proteins", "Protein interactions", "proteomes", "proteomics", "Spectrometric identification of proteins", "cell biology", "Cell processes", "Cellular stress responses", "Molecular cell biology", "oncology", "Cancers and neoplasms", "carcinomas", "adenocarcinomas", "Colon adenocarcinoma", "Basic cancer research", "cancer"], "article_id"=>1017722, "categories"=>["Biological Sciences"], "users"=>["Masako Tanaka", "Saya Mun", "Akihito Harada", "Yasuyuki Ohkawa", "Azusa Inagaki", "Soichi Sano", "Katsuyuki Takahashi", "Yasukatsu Izumi", "Mayuko Osada-Oka", "Hideki Wanibuchi", "Masayo Yamagata", "Tokihito Yukimura", "Katsuyuki Miura", "Masayuki Shiota", "Hiroshi Iwao"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0096785.g001", "stats"=>{"downloads"=>3, "page_views"=>5, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Hsc70_is_critical_for_cancer_cell_survival_/1017722", "title"=>"Hsc70 is critical for cancer cell survival.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2014-05-06 03:07:24"}
  • {"files"=>["https://ndownloader.figshare.com/files/1486586"], "description"=>"<p>(A) A schematic view of the identification of Hsc70 interactors. Cells were exposed to serum depletion (SD), 5-FU, or DMSO for 6 h. Hsc70 interactors were isolated with anti-Hsc70 antibodies from the cell extract, and were identified through subsequent analysis by liquid chromatography-tandem mass spectrometry (LC-MS/MS). (B) Identification and functional classification of Hsc70 interactors that were associated with changes in stress response. A Venn diagram depicting Hsc70 interactors that were identified at >95% confidence score (1.3 ProtScore) using ProteinPilot 2.0 software. Column graphs indicate the number and functionality of identified proteins.</p>", "links"=>[], "tags"=>["Biochemistry", "proteins", "protein structure", "Protein folding", "Chaperone proteins", "Protein interactions", "proteomes", "proteomics", "Spectrometric identification of proteins", "cell biology", "Cell processes", "Cellular stress responses", "Molecular cell biology", "oncology", "Cancers and neoplasms", "carcinomas", "adenocarcinomas", "Colon adenocarcinoma", "Basic cancer research", "interactors", "serum-depleted", "5-fu-treated", "ht29"], "article_id"=>1017723, "categories"=>["Biological Sciences"], "users"=>["Masako Tanaka", "Saya Mun", "Akihito Harada", "Yasuyuki Ohkawa", "Azusa Inagaki", "Soichi Sano", "Katsuyuki Takahashi", "Yasukatsu Izumi", "Mayuko Osada-Oka", "Hideki Wanibuchi", "Masayo Yamagata", "Tokihito Yukimura", "Katsuyuki Miura", "Masayuki Shiota", "Hiroshi Iwao"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0096785.g002", "stats"=>{"downloads"=>1, "page_views"=>12, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Hsc70_interactors_identified_in_serum_depleted_and_5_FU_treated_HT29_cells_/1017723", "title"=>"Hsc70 interactors identified in serum-depleted and 5-FU-treated HT29 cells.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2014-05-06 03:07:24"}
  • {"files"=>["https://ndownloader.figshare.com/files/1486587"], "description"=>"<p>HT29 cells transfected with <i>Hsc70</i>, <i>Rab1A</i>, or <i>control</i> siRNA were subjected to serum depletion, 5-FU, or vehicle treatment for 24 h. (A) Effects of suppression of Hsc70 and its interactors on cellular morphology. Representative phase-contrast images of cells. Scale bar, 100 µm. (B) Rab1A knockdown decreased cell viability. Cell viability was determined by MTS assay. Asterisks indicate statistical significance. **, <i>p</i><0.01, *, <i>p</i><0.05 vs. vehicle; <sup>†</sup>, <i>p</i><0.05 vs. control knockdown by two-way ANOVA followed by Tukey-Kramer post hoc test; values are the means ± S.D. (<i>n</i> = 7). Veh, vehicle. SD, serum depletion. FU, 5-fluorouracil.</p>", "links"=>[], "tags"=>["Biochemistry", "proteins", "protein structure", "Protein folding", "Chaperone proteins", "Protein interactions", "proteomes", "proteomics", "Spectrometric identification of proteins", "cell biology", "Cell processes", "Cellular stress responses", "Molecular cell biology", "oncology", "Cancers and neoplasms", "carcinomas", "adenocarcinomas", "Colon adenocarcinoma", "Basic cancer research", "knockdown", "exacerbated", "serum", "depletion", "5-fu"], "article_id"=>1017725, "categories"=>["Biological Sciences"], "users"=>["Masako Tanaka", "Saya Mun", "Akihito Harada", "Yasuyuki Ohkawa", "Azusa Inagaki", "Soichi Sano", "Katsuyuki Takahashi", "Yasukatsu Izumi", "Mayuko Osada-Oka", "Hideki Wanibuchi", "Masayo Yamagata", "Tokihito Yukimura", "Katsuyuki Miura", "Masayuki Shiota", "Hiroshi Iwao"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0096785.g003", "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Rab1A_knockdown_exacerbated_stress_damage_due_to_serum_depletion_and_5_FU_treatment_/1017725", "title"=>"Rab1A knockdown exacerbated stress damage due to serum depletion and 5-FU treatment.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2014-05-06 03:07:24"}
  • {"files"=>["https://ndownloader.figshare.com/files/1486601"], "description"=>"<p>(A) Hsc70-Rab1A interaction through chaperone activity. HT29 cells were subjected to serum depletion for 24 h, and then lysed. To verify the interaction between Hsc70 and Rab1A in a chaperone-dependent manner, anti-Hsc70 or anti-Rab1A immunoprecipitant was eluted with ATP, followed by elution with SDS sample buffer and immunoblotting in order to confirm the bait proteins. (B) Hsc70 knockdown decreased the level of Rab1A protein under stress conditions. HT29 cells transfected with <i>Hsc70</i> or <i>control</i> siRNA were subjected to serum depletion, 5-FU, or vehicle treatment for 24 h. Immunoblotting for endogenous Rab1A and Hsc70 proteins. β-actin was used as a loading control. (C) Hsc70 knockdown did not decrease <i>Rab1A</i> mRNA level. After knockdown of Hsc70 and in the control, <i>Rab1A</i> mRNA levels were determined by qPCR at 48 h post-transfection. (D) Hsc70 knockdown promoted the ubiquitination of Rab1A. After Hsc70 knockdown or control cells were lysed, immunoprecipitation (IP) with anti-Rab1A or anti-ubiquitin antibodies was performed, followed by immunoblotting with anti-ubiquitin or anti-Rab1A antibodies. (E) MG132 treatment inhibited Rab1A degradation. Hsc70 knockdown cells were subjected to serum depletion or 5-FU treatment, and then MG132 (10 µM) or vehicle was added for the last 8 h before sampling. SD, serum depletion. FU, 5-fluorouracil. Ub, ubiquitin, IgG LC, immunoglobulin light chain. Data (except in C) are representative of at least two separate experiments yielding similar results.</p>", "links"=>[], "tags"=>["Biochemistry", "proteins", "protein structure", "Protein folding", "Chaperone proteins", "Protein interactions", "proteomes", "proteomics", "Spectrometric identification of proteins", "cell biology", "Cell processes", "Cellular stress responses", "Molecular cell biology", "oncology", "Cancers and neoplasms", "carcinomas", "adenocarcinomas", "Colon adenocarcinoma", "Basic cancer research", "prevented", "rab1a"], "article_id"=>1017726, "categories"=>["Biological Sciences"], "users"=>["Masako Tanaka", "Saya Mun", "Akihito Harada", "Yasuyuki Ohkawa", "Azusa Inagaki", "Soichi Sano", "Katsuyuki Takahashi", "Yasukatsu Izumi", "Mayuko Osada-Oka", "Hideki Wanibuchi", "Masayo Yamagata", "Tokihito Yukimura", "Katsuyuki Miura", "Masayuki Shiota", "Hiroshi Iwao"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0096785.g004", "stats"=>{"downloads"=>4, "page_views"=>5, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Hsc70_prevented_Rab1A_degradation_/1017726", "title"=>"Hsc70 prevented Rab1A degradation.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2014-05-06 03:07:24"}
  • {"files"=>["https://ndownloader.figshare.com/files/1486604"], "description"=>"<p>HT29 cells transfected with <i>Hsc70</i>, <i>Rab1A</i>, <i>Ran</i>, or <i>control</i> siRNA were subjected to serum depletion, 5-FU, or vehicle treatment for 24 h. (A) Rab1A knockdown had little effect on the induction of apoptosis. The induction of apoptosis was analyzed by staining with Hoechst 33258. White arrowheads indicate apoptotic nuclei with condensed chromatin. Scale bar, 50 µm. (B, C) The decrease in cell number by Rab1A knockdown was not due to apoptosis. Numbers of total cells and apoptotic cells were quantified by counting Hoechst-stained cells and cells with nuclear condensation in (A), respectively. *, <i>p</i><0.05, **, <i>p</i><0.01 vs. control/veh; <sup>†</sup>, <i>p</i><0.05, <sup>††</sup>, <i>p</i><0.01 vs. control/SD; <sup>##</sup>, <i>p</i><0.01 vs. Rab1A/SD by two-way ANOVA followed by Bonferroni/Dunn post hoc test; values are the means ± S.D. (<i>n</i> = 3). (D) Rab1A suppression did not induce apoptosis. Apoptosis was determined by the cleavages of PARP-1 and caspase-3, detected by immunoblotting. β-actin was used as a loading control. Veh, vehicle. SD, serum depletion. FU, 5-fluorouracil. Immunoblotting data are representative of at least three separate experiments yielding similar results.</p>", "links"=>[], "tags"=>["Biochemistry", "proteins", "protein structure", "Protein folding", "Chaperone proteins", "Protein interactions", "proteomes", "proteomics", "Spectrometric identification of proteins", "cell biology", "Cell processes", "Cellular stress responses", "Molecular cell biology", "oncology", "Cancers and neoplasms", "carcinomas", "adenocarcinomas", "Colon adenocarcinoma", "Basic cancer research", "knockdown", "induced"], "article_id"=>1017727, "categories"=>["Biological Sciences"], "users"=>["Masako Tanaka", "Saya Mun", "Akihito Harada", "Yasuyuki Ohkawa", "Azusa Inagaki", "Soichi Sano", "Katsuyuki Takahashi", "Yasukatsu Izumi", "Mayuko Osada-Oka", "Hideki Wanibuchi", "Masayo Yamagata", "Tokihito Yukimura", "Katsuyuki Miura", "Masayuki Shiota", "Hiroshi Iwao"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0096785.g005", "stats"=>{"downloads"=>0, "page_views"=>6, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Rab1A_knockdown_induced_cell_death_not_including_apoptosis_/1017727", "title"=>"Rab1A knockdown induced cell death not including apoptosis.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2014-05-06 03:07:24"}

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Relative Metric

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