Identification of DNA-Dependent Protein Kinase Catalytic Subunit (DNA-PKcs) as a Novel Target of Bisphenol A
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{"title"=>"Identification of DNA-Dependent Protein Kinase Catalytic Subunit (DNA-PKcs) as a Novel Target of Bisphenol A", "type"=>"journal", "authors"=>[{"first_name"=>"Yuki", "last_name"=>"Ito", "scopus_author_id"=>"57199761989"}, {"first_name"=>"Takumi", "last_name"=>"Ito", "scopus_author_id"=>"55249619900"}, {"first_name"=>"Satoki", "last_name"=>"Karasawa", "scopus_author_id"=>"37665105900"}, {"first_name"=>"Teruya", "last_name"=>"Enomoto", "scopus_author_id"=>"13806344300"}, {"first_name"=>"Akihiro", "last_name"=>"Nashimoto", "scopus_author_id"=>"34768647600"}, {"first_name"=>"Yasuyoshi", "last_name"=>"Hase", "scopus_author_id"=>"23094455900"}, {"first_name"=>"Satoshi", "last_name"=>"Sakamoto", "scopus_author_id"=>"15056946100"}, {"first_name"=>"Tsuneyo", "last_name"=>"Mimori", "scopus_author_id"=>"7006377392"}, {"first_name"=>"Yoshihisa", "last_name"=>"Matsumoto", "scopus_author_id"=>"36135696200"}, {"first_name"=>"Yuki", "last_name"=>"Yamaguchi", "scopus_author_id"=>"7404477389"}, {"first_name"=>"Hiroshi", "last_name"=>"Handa", "scopus_author_id"=>"7202638173"}], "year"=>2012, "source"=>"PLoS ONE", "identifiers"=>{"issn"=>"19326203", "pui"=>"366234486", "sgr"=>"84870769674", "doi"=>"10.1371/journal.pone.0050481", "scopus"=>"2-s2.0-84870769674", "isbn"=>"1932-6203 (Electronic) 1932-6203 (Linking)", "pmid"=>"23227178"}, "id"=>"db67fc00-93e7-35c1-8282-dcddee0b3a78", "abstract"=>"Bisphenol A (BPA) forms the backbone of plastics and epoxy resins used to produce packaging for various foods and beverages. BPA is also an estrogenic disruptor, interacting with human estrogen receptors (ER) and other related nuclear receptors. Nevertheless, the effects of BPA on human health remain unclear. The present study identified DNA-dependent protein kinase catalytic subunit (DNA-PKcs) as a novel BPA-binding protein. DNA-PKcs, in association with the Ku heterodimer (Ku70/80), is a critical enzyme involved in the repair of DNA double-strand breaks. Low levels of DNA-PK activity are previously reported to be associated with an increased risk of certain types of cancer. Although the Kd for the interaction between BPA and a drug-binding mutant of DNA-PKcs was comparatively low (137 nM), high doses of BPA were required before cellular effects were observed (100-300 μM). The results of an in vitro kinase assay showed that BPA inhibited DNA-PK kinase activity in a concentration-dependent manner. In M059K cells, BPA inhibited the phosphorylation of DNA-PKcs at Ser2056 and H2AX at Ser139 in response to ionizing radiation (IR)-irradiation. BPA also disrupted DNA-PKcs binding to Ku70/80 and increased the radiosensitivity of M059K cells, but not M059J cells (which are DNA-PKcs-deficient). Taken together, these results provide new evidence of the effects of BPA on DNA repair in mammalian cells, which are mediated via inhibition of DNA-PK activity. This study may warrant the consideration of the possible carcinogenic effects of high doses of BPA, which are mediated through its action on DNA-PK.", "link"=>"http://www.mendeley.com/research/identification-dnadependent-protein-kinase-catalytic-subunit-dnapkcs-novel-target-bisphenol", "reader_count"=>15, "reader_count_by_academic_status"=>{"Researcher"=>7, "Student > Ph. D. Student"=>2, "Student > Postgraduate"=>1, "Student > Master"=>2, "Student > Bachelor"=>2, "Lecturer"=>1}, "reader_count_by_user_role"=>{"Researcher"=>7, "Student > Ph. D. Student"=>2, "Student > Postgraduate"=>1, "Student > Master"=>2, "Student > Bachelor"=>2, "Lecturer"=>1}, "reader_count_by_subject_area"=>{"Engineering"=>1, "Biochemistry, Genetics and Molecular Biology"=>2, "Medicine and Dentistry"=>3, "Agricultural and Biological Sciences"=>6, "Pharmacology, Toxicology and Pharmaceutical Science"=>1, "Chemistry"=>2}, "reader_count_by_subdiscipline"=>{"Engineering"=>{"Engineering"=>1}, "Medicine and Dentistry"=>{"Medicine and Dentistry"=>3}, "Chemistry"=>{"Chemistry"=>2}, "Agricultural and Biological Sciences"=>{"Agricultural and Biological Sciences"=>6}, "Biochemistry, Genetics and Molecular Biology"=>{"Biochemistry, Genetics and Molecular Biology"=>2}, "Pharmacology, Toxicology and Pharmaceutical Science"=>{"Pharmacology, Toxicology and Pharmaceutical Science"=>1}}, "reader_count_by_country"=>{"France"=>1}, "group_count"=>0}

Scopus | Further Information

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Figshare

  • {"files"=>["https://ndownloader.figshare.com/files/531238"], "description"=>"<p>(A) Survival of logarithmically growing M059J and M059K cells after exposure to various doses of γ-rays as measured by colony formation. BPA was added to the culture media 3 h prior to irradiation and removed 2 h after irradiation. Cells on the survival curve “M059K+BPA” were treated with BPA at IR dose “0”. The results shown represent the mean from three independent experiments; bar, SE. (B) Expression of DNA-PKcs was detected in M059K, but not in M059J cells.</p>", "links"=>[], "tags"=>["bpa", "cultured"], "article_id"=>201723, "categories"=>["Molecular Biology", "Biochemistry", "Cancer", "Chemistry"], "users"=>["Yuki Ito", "Takumi Ito", "Satoki Karasawa", "Teruya Enomoto", "Akihiro Nashimoto", "Yasuyoshi Hase", "Satoshi Sakamoto", "Tsuneyo Mimori", "Yoshihisa Matsumoto", "Yuki Yamaguchi", "Hiroshi Handa"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0050481.g005", "stats"=>{"downloads"=>1, "page_views"=>7, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Effects_of_BPA_in_cultured_cells_/201723", "title"=>"Effects of BPA in cultured cells.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2012-12-05 00:28:43"}
  • {"files"=>["https://ndownloader.figshare.com/files/531110"], "description"=>"<p>(A) M059K cells extracts were pre-incubated with the indicated concentrations of BPA and, thereafter, with DNA-immobilized beads or control beads. Bound proteins were eluted with SDS sample buffer and detected by immunoblotting. (B) (C) FLAG-Ku80 (B, bottom and C) or FLAG-Ku70 (B, top) was expressed in 293T cells incubated with 300 μM BPA and then irradiated with γ-rays (B) or UV (C). Cell lysates were immunoprecipitated using anti-FLAG agarose beads and immunoblotted with the indicated antibodies.</p>", "links"=>[], "tags"=>["inhibition", "binding", "dna-pkcs", "ku-complexes"], "article_id"=>201594, "categories"=>["Molecular Biology", "Biochemistry", "Cancer", "Chemistry"], "users"=>["Yuki Ito", "Takumi Ito", "Satoki Karasawa", "Teruya Enomoto", "Akihiro Nashimoto", "Yasuyoshi Hase", "Satoshi Sakamoto", "Tsuneyo Mimori", "Yoshihisa Matsumoto", "Yuki Yamaguchi", "Hiroshi Handa"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0050481.g004", "stats"=>{"downloads"=>3, "page_views"=>10, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_The_inhibition_of_binding_between_DNA_PKcs_and_Ku_complexes_by_BPA_/201594", "title"=>"The inhibition of binding between DNA-PKcs and Ku-complexes by BPA.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2012-12-05 00:26:34"}
  • {"files"=>["https://ndownloader.figshare.com/files/285593", "https://ndownloader.figshare.com/files/285619"], "description"=>"<div><p>Bisphenol A (BPA) forms the backbone of plastics and epoxy resins used to produce packaging for various foods and beverages. BPA is also an estrogenic disruptor, interacting with human estrogen receptors (ER) and other related nuclear receptors. Nevertheless, the effects of BPA on human health remain unclear. The present study identified DNA-dependent protein kinase catalytic subunit (DNA-PKcs) as a novel BPA-binding protein. DNA-PKcs, in association with the Ku heterodimer (Ku70/80), is a critical enzyme involved in the repair of DNA double-strand breaks. Low levels of DNA-PK activity are previously reported to be associated with an increased risk of certain types of cancer. Although the Kd for the interaction between BPA and a drug-binding mutant of DNA-PKcs was comparatively low (137 nM), high doses of BPA were required before cellular effects were observed (100–300 μM). The results of an <em>in vitro</em> kinase assay showed that BPA inhibited DNA-PK kinase activity in a concentration-dependent manner. In M059K cells, BPA inhibited the phosphorylation of DNA-PKcs at Ser2056 and H2AX at Ser139 in response to ionizing radiation (IR)-irradiation. BPA also disrupted DNA-PKcs binding to Ku70/80 and increased the radiosensitivity of M059K cells, but not M059J cells (which are DNA-PKcs-deficient). Taken together, these results provide new evidence of the effects of BPA on DNA repair in mammalian cells, which are mediated via inhibition of DNA-PK activity. This study may warrant the consideration of the possible carcinogenic effects of high doses of BPA, which are mediated through its action on DNA-PK.</p> </div>", "links"=>[], "tags"=>["dna-dependent", "kinase", "catalytic", "subunit", "bisphenol", "a"], "article_id"=>116291, "categories"=>["Molecular Biology", "Biochemistry", "Cancer", "Chemistry"], "users"=>["Yuki Ito", "Takumi Ito", "Satoki Karasawa", "Teruya Enomoto", "Akihiro Nashimoto", "Yasuyoshi Hase", "Satoshi Sakamoto", "Tsuneyo Mimori", "Yoshihisa Matsumoto", "Yuki Yamaguchi", "Hiroshi Handa"], "doi"=>["https://dx.doi.org/10.1371/journal.pone.0050481.s001", "https://dx.doi.org/10.1371/journal.pone.0050481.s002"], "stats"=>{"downloads"=>3, "page_views"=>6, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/Identification_of_DNA_Dependent_Protein_Kinase_Catalytic_Subunit_DNA_PKcs_as_a_Novel_Target_of_Bisphenol_A__/116291", "title"=>"Identification of DNA-Dependent Protein Kinase Catalytic Subunit (DNA-PKcs) as a Novel Target of Bisphenol A", "pos_in_sequence"=>0, "defined_type"=>4, "published_date"=>"2012-12-05 01:44:51"}
  • {"files"=>["https://ndownloader.figshare.com/files/530857"], "description"=>"<p>(A) Structure of DNA-PKcs and seven fragments. (B) Recombinant DNA-PKcs fragments (#1 to #7) were purified from 293T cells and incubated with BPA-immobilized (+) or control (−) beads. The input and bound proteins were immunoblotted with an anti-FLAG antibody. (C) The Kd for the binding of BPA to ΔDNA-PKcs #6 was calculated by Scatchard analysis.</p>", "links"=>[], "tags"=>["bpa", "recombinant", "dna-pkcs", "fragments"], "article_id"=>201347, "categories"=>["Molecular Biology", "Biochemistry", "Cancer", "Chemistry"], "users"=>["Yuki Ito", "Takumi Ito", "Satoki Karasawa", "Teruya Enomoto", "Akihiro Nashimoto", "Yasuyoshi Hase", "Satoshi Sakamoto", "Tsuneyo Mimori", "Yoshihisa Matsumoto", "Yuki Yamaguchi", "Hiroshi Handa"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0050481.g002", "stats"=>{"downloads"=>1, "page_views"=>3, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Binding_of_BPA_to_recombinant_DNA_PKcs_fragments_in_vitro_/201347", "title"=>"Binding of BPA to recombinant DNA-PKcs fragments <i>in vitro</i>.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2012-12-05 00:22:27"}
  • {"files"=>["https://ndownloader.figshare.com/files/530755"], "description"=>"<p>(A) The structure of BPA. (B) Preparation of BPA-immobilized beads. (C) BPA-binding proteins were purified from MCF7 cell nuclear extracts using BPA-immobilized (+) or control (−) beads. Bound proteins were eluted with SDS sample buffer. In lanes 3 and 4, BPA was added to extracts before incubation with the beads. Eluted proteins were analyzed by silver staining (C) or immunoblotting (IB) (D).</p>", "links"=>[], "tags"=>["dna-pkcs", "bpa-binding"], "article_id"=>201241, "categories"=>["Molecular Biology", "Biochemistry", "Cancer", "Chemistry"], "users"=>["Yuki Ito", "Takumi Ito", "Satoki Karasawa", "Teruya Enomoto", "Akihiro Nashimoto", "Yasuyoshi Hase", "Satoshi Sakamoto", "Tsuneyo Mimori", "Yoshihisa Matsumoto", "Yuki Yamaguchi", "Hiroshi Handa"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0050481.g001", "stats"=>{"downloads"=>2, "page_views"=>8, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Identification_of_DNA_PKcs_as_a_BPA_binding_protein_/201241", "title"=>"Identification of DNA-PKcs as a BPA-binding protein.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2012-12-05 00:20:41"}
  • {"files"=>["https://ndownloader.figshare.com/files/530993"], "description"=>"<p>(A) Protein kinase activity was assayed <i>in vitro</i> using the SignaTECT®. Purified DNA-PKcs, biotinylated p53-derived peptide substrate, DNA, and [γ-<sup>32</sup>P] ATP were mixed and BPA or NU7026 was added as indicated. Samples were incubated at 30°C for 5 min. Incorporation of <sup>32</sup>P into the substrate was measured using an Imaging plate. (B) 293T cells were exposed to 150 J/m<sup>2</sup> of 254 nm UV followed by incubation at 37°C for 6 h. Cells were harvested and immunoblot analysis was performed using antibodies to DNA-PKcs-phospho-serine 2056, total DNA-PKcs, and actin (loading control). BPA was added 1 h prior to UV-irradiation at the concentrations indicated. (C) M059K cells were exposed to 10 Gy of γ-rays. Cells were pre-incubated with BPA (300 μM, 3 h), Nu7026 (10 μM, 24 h) or Ku55933 (10 μM, 1 h) separately or in combination. One hour after irradiation, cells were harvested and the amount of DNA-PKcs, DNA-PKcs-phospho-serine 2056, H2AX, H2AX-phospho-serine 139, and actin (loading control) were analyzed by immunoblotting.</p>", "links"=>[], "tags"=>["dna-pkcs", "kinase"], "article_id"=>201482, "categories"=>["Molecular Biology", "Biochemistry", "Cancer", "Chemistry"], "users"=>["Yuki Ito", "Takumi Ito", "Satoki Karasawa", "Teruya Enomoto", "Akihiro Nashimoto", "Yasuyoshi Hase", "Satoshi Sakamoto", "Tsuneyo Mimori", "Yoshihisa Matsumoto", "Yuki Yamaguchi", "Hiroshi Handa"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0050481.g003", "stats"=>{"downloads"=>1, "page_views"=>4, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Inhibitory_effect_of_DNA_PKcs_kinase_activity_by_BPA_/201482", "title"=>"Inhibitory effect of DNA-PKcs kinase activity by BPA.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2012-12-05 00:24:42"}

PMC Usage Stats | Further Information

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Relative Metric

{"start_date"=>"2012-01-01T00:00:00Z", "end_date"=>"2012-12-31T00:00:00Z", "subject_areas"=>[{"subject_area"=>"/Biology and life sciences", "average_usage"=>[322, 550, 671, 773, 864, 955, 1048, 1135, 1223, 1308, 1387, 1465, 1534, 1602, 1673, 1744, 1813, 1885, 1955, 2026, 2093, 2160, 2228, 2290, 2349]}, {"subject_area"=>"/Biology and life sciences/Biochemistry", "average_usage"=>[316, 541, 663, 766, 856, 950, 1041, 1128, 1218, 1302, 1382, 1456, 1526, 1593, 1657, 1729, 1796, 1862, 1930, 1999, 2065, 2132, 2202, 2261, 2319]}, {"subject_area"=>"/Biology and life sciences/Molecular biology", "average_usage"=>[324, 551, 679, 782, 879, 971, 1064, 1154, 1245, 1328, 1406, 1476, 1541, 1617, 1683, 1754, 1818, 1893, 1962, 2025, 2092, 2164, 2227, 2294, 2355]}]}
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