Inhibiting Heat Shock Factor 1 in Human Cancer Cells with a Potent RNA Aptamer
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{"title"=>"Inhibiting heat shock factor 1 in human cancer cells with a potent RNA aptamer", "type"=>"journal", "authors"=>[{"first_name"=>"H. Hans", "last_name"=>"Salamanca", "scopus_author_id"=>"54391737000"}, {"first_name"=>"Marc A.", "last_name"=>"Antonyak", "scopus_author_id"=>"6602928002"}, {"first_name"=>"Richard A.", "last_name"=>"Cerione", "scopus_author_id"=>"7102225792"}, {"first_name"=>"Hua", "last_name"=>"Shi", "scopus_author_id"=>"7402623732"}, {"first_name"=>"John T.", "last_name"=>"Lis", "scopus_author_id"=>"26643032700"}], "year"=>2014, "source"=>"PLoS ONE", "identifiers"=>{"sgr"=>"84900434881", "doi"=>"10.1371/journal.pone.0096330", "issn"=>"19326203", "pui"=>"373074663", "isbn"=>"1932-6203 (Electronic)\\r1932-6203 (Linking)", "pmid"=>"24800749", "scopus"=>"2-s2.0-84900434881"}, "id"=>"f830f2bd-8ce7-3841-93fe-6cd4609f72ef", "abstract"=>"Heat shock factor 1 (HSF1) is a master regulator that coordinates chaperone protein expression to enhance cellular survival in the face of heat stress. In cancer cells, HSF1 drives a transcriptional program distinct from heat shock to promote metastasis and cell survival. Its strong association with the malignant phenotype implies that HSF1 antagonists may have general and effective utilities in cancer therapy. For this purpose, we had identified an avid RNA aptamer for HSF1 that is portable among different model organisms. Extending our previous work in yeast and Drosophila, here we report the activity of this aptamer in human cancer cell lines. When delivered into cells using a synthetic gene and strong promoter, this aptamer was able to prevent HSF1 from binding to its DNA regulation elements. At the cellular level, expression of this aptamer induced apoptosis and abolished the colony-forming capability of cancer cells. At the molecular level, it reduced chaperones and attenuated the activation of the MAPK signaling pathway. Collectively, these data demonstrate the advantage of aptamers in drug target validation and support the hypothesis that HSF1 DNA binding activity is a potential target for controlling oncogenic transformation and neoplastic growth.", "link"=>"http://www.mendeley.com/research/inhibiting-heat-shock-factor-1-human-cancer-cells-potent-rna-aptamer", "reader_count"=>37, "reader_count_by_academic_status"=>{"Unspecified"=>1, "Professor > Associate Professor"=>1, "Researcher"=>4, "Student > Doctoral Student"=>2, "Student > Ph. D. Student"=>19, "Student > Postgraduate"=>1, "Student > Master"=>4, "Other"=>2, "Student > Bachelor"=>2, "Professor"=>1}, "reader_count_by_user_role"=>{"Unspecified"=>1, "Professor > Associate Professor"=>1, "Researcher"=>4, "Student > Doctoral Student"=>2, "Student > Ph. D. Student"=>19, "Student > Postgraduate"=>1, "Student > Master"=>4, "Other"=>2, "Student > Bachelor"=>2, "Professor"=>1}, "reader_count_by_subject_area"=>{"Unspecified"=>2, "Biochemistry, Genetics and Molecular Biology"=>9, "Mathematics"=>1, "Agricultural and Biological Sciences"=>19, "Medicine and Dentistry"=>3, "Physics and Astronomy"=>1, "Chemistry"=>2}, "reader_count_by_subdiscipline"=>{"Medicine and Dentistry"=>{"Medicine and Dentistry"=>3}, "Chemistry"=>{"Chemistry"=>2}, "Physics and Astronomy"=>{"Physics and Astronomy"=>1}, "Agricultural and Biological Sciences"=>{"Agricultural and Biological Sciences"=>19}, "Biochemistry, Genetics and Molecular Biology"=>{"Biochemistry, Genetics and Molecular Biology"=>9}, "Mathematics"=>{"Mathematics"=>1}, "Unspecified"=>{"Unspecified"=>2}}, "reader_count_by_country"=>{"Austria"=>1, "Germany"=>1}, "group_count"=>1}

Scopus | Further Information

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Figshare

  • {"files"=>["https://ndownloader.figshare.com/files/1487531"], "description"=>"<p>(<b>A</b>) HSF1 inhibition attenuates EGF receptor activation following the addition of EGF to HeLa cells. (<b>B</b>) HSF1 inhibition by iaRNA<sup>HSF1</sup> causes a depletion of the total levels and activated forms of Erk1/2. The left most three lanes are a serial dilution of parental line extracts that provides a quantification standard curve. Ectopic expression of HSP70 or HSP90 suppresses the inhibition of mitogenic signaling in the iaRNA<sup>HSF1</sup> expressing cells.</p>", "links"=>[], "tags"=>["Biochemistry", "Nucleic acids", "rna", "cell biology", "Cell processes", "Cell death", "Cell growth", "Cellular stress responses", "Signal transduction", "cell signaling", "Mitogenic signaling", "Oncogenic signaling", "Molecular cell biology", "genetics", "gene expression", "aptamer", "inhibits", "mitogenic"], "article_id"=>1018462, "categories"=>["Biological Sciences"], "users"=>["H. Hans Salamanca", "Marc A. Antonyak", "Richard A. Cerione", "Hua Shi", "John T. Lis"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0096330.g006", "stats"=>{"downloads"=>2, "page_views"=>5, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_HSF1_aptamer_inhibits_mitogenic_signaling_/1018462", "title"=>"HSF1 aptamer inhibits mitogenic signaling.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2014-05-06 04:04:13"}
  • {"files"=>["https://ndownloader.figshare.com/files/1487528"], "description"=>"<p>HSF1 inhibition by iaRNA<sup>HSF1</sup> inhibits transformed growth in soft agar. Soft agar analysis of non-transfected HeLa cells (top left) or control RNA over-expressing HeLa (bottom left), shows that iaRNA<sup>HSF1</sup> over-expression (bottom right) inhibits cellular transformation (colony formation) in a similar manner as treatment of HeLa cells with 150 nM 17-AAG (top right) (Day 14).</p>", "links"=>[], "tags"=>["Biochemistry", "Nucleic acids", "rna", "cell biology", "Cell processes", "Cell death", "Cell growth", "Cellular stress responses", "Signal transduction", "cell signaling", "Mitogenic signaling", "Oncogenic signaling", "Molecular cell biology", "genetics", "gene expression", "attenuates", "transformed"], "article_id"=>1018459, "categories"=>["Biological Sciences"], "users"=>["H. Hans Salamanca", "Marc A. Antonyak", "Richard A. Cerione", "Hua Shi", "John T. Lis"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0096330.g004", "stats"=>{"downloads"=>1, "page_views"=>4, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_iaRNA_HSF1_expression_attenuates_transformed_growth_/1018459", "title"=>"iaRNA<sup>HSF1</sup> expression attenuates transformed growth.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2014-05-06 04:04:13"}
  • {"files"=>["https://ndownloader.figshare.com/files/1487539", "https://ndownloader.figshare.com/files/1487540", "https://ndownloader.figshare.com/files/1487541", "https://ndownloader.figshare.com/files/1487542", "https://ndownloader.figshare.com/files/1487543"], "description"=>"<div><p>Heat shock factor 1 (HSF1) is a master regulator that coordinates chaperone protein expression to enhance cellular survival in the face of heat stress. In cancer cells, HSF1 drives a transcriptional program distinct from heat shock to promote metastasis and cell survival. Its strong association with the malignant phenotype implies that HSF1 antagonists may have general and effective utilities in cancer therapy. For this purpose, we had identified an avid RNA aptamer for HSF1 that is portable among different model organisms. Extending our previous work in yeast and Drosophila, here we report the activity of this aptamer in human cancer cell lines. When delivered into cells using a synthetic gene and strong promoter, this aptamer was able to prevent HSF1 from binding to its DNA regulation elements. At the cellular level, expression of this aptamer induced apoptosis and abolished the colony-forming capability of cancer cells. At the molecular level, it reduced chaperones and attenuated the activation of the MAPK signaling pathway. Collectively, these data demonstrate the advantage of aptamers in drug target validation and support the hypothesis that HSF1 DNA binding activity is a potential target for controlling oncogenic transformation and neoplastic growth.</p></div>", "links"=>[], "tags"=>["Biochemistry", "Nucleic acids", "rna", "cell biology", "Cell processes", "Cell death", "Cell growth", "Cellular stress responses", "Signal transduction", "cell signaling", "Mitogenic signaling", "Oncogenic signaling", "Molecular cell biology", "genetics", "gene expression", "cancer", "cells", "potent"], "article_id"=>1018470, "categories"=>["Biological Sciences"], "users"=>["H. Hans Salamanca", "Marc A. Antonyak", "Richard A. Cerione", "Hua Shi", "John T. Lis"], "doi"=>["https://dx.doi.org/10.1371/journal.pone.0096330.s001", "https://dx.doi.org/10.1371/journal.pone.0096330.s002", "https://dx.doi.org/10.1371/journal.pone.0096330.s003", "https://dx.doi.org/10.1371/journal.pone.0096330.s004", "https://dx.doi.org/10.1371/journal.pone.0096330.s005"], "stats"=>{"downloads"=>2, "page_views"=>9, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Inhibiting_Heat_Shock_Factor_1_in_Human_Cancer_Cells_with_a_Potent_RNA_Aptamer_/1018470", "title"=>"Inhibiting Heat Shock Factor 1 in Human Cancer Cells with a Potent RNA Aptamer", "pos_in_sequence"=>0, "defined_type"=>4, "published_date"=>"2014-05-06 04:04:13"}
  • {"files"=>["https://ndownloader.figshare.com/files/1487518"], "description"=>"<p>(<b>A</b>) Electrophoretic motility shift assay (EMSA) using radiolabeled iaRNA<sup>HSF1</sup> (1 nM) and increasing amounts of human HSF1 protein shows that the aptamer binds to its target avidly. (<b>B</b>) Quantification of independent EMSA reveals the apparent affinity of the iaRNA<sup>HSF1</sup> for HSF1 as Kd∼25 nM (n = 5).</p>", "links"=>[], "tags"=>["Biochemistry", "Nucleic acids", "rna", "cell biology", "Cell processes", "Cell death", "Cell growth", "Cellular stress responses", "Signal transduction", "cell signaling", "Mitogenic signaling", "Oncogenic signaling", "Molecular cell biology", "genetics", "gene expression", "binding", "aptamer", "hsf1"], "article_id"=>1018449, "categories"=>["Biological Sciences"], "users"=>["H. Hans Salamanca", "Marc A. Antonyak", "Richard A. Cerione", "Hua Shi", "John T. Lis"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0096330.g001", "stats"=>{"downloads"=>1, "page_views"=>18, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Specific_binding_of_the_aptamer_to_human_HSF1_in_vitro_/1018449", "title"=>"Specific binding of the aptamer to human HSF1 <i>in vitro</i>.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2014-05-06 04:04:13"}
  • {"files"=>["https://ndownloader.figshare.com/files/1487529"], "description"=>"<p>(<b>A</b>) Western blot analysis showing the depletion of specific molecular chaperone proteins in aptamer or control expressing cells. Hsp90 co-expression rescues specific molecular chaperones observed in HSF1 inhibited aptamer expressing cells. The asterisk indicates PARP degradation product, a marker of apoptosis. The left most three lanes are a serial dilution of parental line extracts that provides a quantification standard curve. (<b>B</b>) Quantification of the results observed in panel A (n = 4, error indicates %SEM).</p>", "links"=>[], "tags"=>["Biochemistry", "Nucleic acids", "rna", "cell biology", "Cell processes", "Cell death", "Cell growth", "Cellular stress responses", "Signal transduction", "cell signaling", "Mitogenic signaling", "Oncogenic signaling", "Molecular cell biology", "genetics", "gene expression", "targeting", "hsf1", "molecular", "chaperone"], "article_id"=>1018460, "categories"=>["Biological Sciences"], "users"=>["H. Hans Salamanca", "Marc A. Antonyak", "Richard A. Cerione", "Hua Shi", "John T. Lis"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0096330.g005", "stats"=>{"downloads"=>1, "page_views"=>4, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Effective_targeting_of_HSF1_activity_reduces_the_levels_of_molecular_chaperone_proteins_/1018460", "title"=>"Effective targeting of HSF1 activity reduces the levels of molecular chaperone proteins.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2014-05-06 04:04:13"}
  • {"files"=>["https://ndownloader.figshare.com/files/1487526"], "description"=>"<p>(<b>A</b>) iaRNA<sup>HSF1</sup> expression does not affect normal cells (IMR90), yet induces an abnormal morphology in HeLa cervical carcinoma and chemically transformed kidney cells (293T). (<b>B</b>). Nuclear condensation and fragmentation assays reveal that iaRNA<sup>HSF1</sup> expression induces ∼10-fold increase in apoptosis in HeLa cells (p<0.0001) (n = 8), and ∼7-fold increase in apoptosis in 293T cells (p<0.0001) (n>8). Furthermore, iaRNA<sup>HSF1</sup> induced apoptosis in effectively suppressed by the over-expression of molecular chaperones (HSF1 p<0.006, Hsp90 p<0.005, or Hsp70 p<0.002), but not random proteins (GFP or LacZ) (n>8).</p>", "links"=>[], "tags"=>["Biochemistry", "Nucleic acids", "rna", "cell biology", "Cell processes", "Cell death", "Cell growth", "Cellular stress responses", "Signal transduction", "cell signaling", "Mitogenic signaling", "Oncogenic signaling", "Molecular cell biology", "genetics", "gene expression", "inhibition", "attenuates", "cancer"], "article_id"=>1018457, "categories"=>["Biological Sciences"], "users"=>["H. Hans Salamanca", "Marc A. Antonyak", "Richard A. Cerione", "Hua Shi", "John T. Lis"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0096330.g003", "stats"=>{"downloads"=>3, "page_views"=>9, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_HSF1_inhibition_attenuates_cancer_cell_survival_/1018457", "title"=>"HSF1 inhibition attenuates cancer cell survival.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2014-05-06 04:04:13"}
  • {"files"=>["https://ndownloader.figshare.com/files/1487519"], "description"=>"<p>(A) Control RNA (RevRA1) and aptamer RNA (iaRNA<sup>HSF1</sup>) constructs are expressed to similar levels in HeLa and IMR90 cells after 24 hrs post transfection (RNA values normalized to GAPDH, n = 3). (<b>B</b>) Disruption of HSF1's interaction with its cognate DNA elements by iaRNA <sup>HSF1</sup>. ChIP assays in iaRNA<sup>HSF1</sup> (or RevRA1) expressing HeLa cells show that iaRNA<sup>HSF1</sup> expression can effectively inhibit HSF1 binding to the <i>Hsp90</i> and <i>Hsp70</i> promoter loci <i>in vivo</i> (n = 3). Antibodies used in ChIP assays are specific for mammalian HSF1 or HSF2 proteins <a href=\"http://www.plosone.org/article/info:doi/10.1371/journal.pone.0096330#pone.0096330-Sarge2\" target=\"_blank\">[20]</a>. BG  =  Background.</p>", "links"=>[], "tags"=>["Biochemistry", "Nucleic acids", "rna", "cell biology", "Cell processes", "Cell death", "Cell growth", "Cellular stress responses", "Signal transduction", "cell signaling", "Mitogenic signaling", "Oncogenic signaling", "Molecular cell biology", "genetics", "gene expression", "targeting", "hsf1", "inhibits", "occupancy", "loci"], "article_id"=>1018450, "categories"=>["Biological Sciences"], "users"=>["H. Hans Salamanca", "Marc A. Antonyak", "Richard A. Cerione", "Hua Shi", "John T. Lis"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0096330.g002", "stats"=>{"downloads"=>2, "page_views"=>16, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Expression_of_the_RNA_construct_targeting_HSF1_inhibits_its_occupancy_at_heat_shock_loci_in_vivo_/1018450", "title"=>"Expression of the RNA construct targeting HSF1 inhibits its occupancy at heat shock loci <i>in vivo</i>.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2014-05-06 04:04:13"}

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