β-Catenin signaling induces CYP1A1 expression by disrupting adherens junctions in Caco-2 human colon carcinoma cells
The aryl hydrocarbon (Ah) receptor is one of the best known ligand-activated transcription factors. The present study has focused on the wound-healing process on Ah receptor function. Depletion of calcium from culture medium of Caco-2 human colon carcinoma cells by transfer to Minimal Essential Medi...
Uloženo v:
| Vydáno v: | Biochimica et biophysica acta Ročník 1830; číslo 3; s. 2509 - 2516 |
|---|---|
| Hlavní autoři: | , , , , |
| Médium: | Journal Article |
| Jazyk: | angličtina |
| Vydáno: |
Netherlands
Elsevier B.V
01.03.2013
|
| Témata: | |
| ISSN: | 0304-4165, 0006-3002, 1872-8006 |
| On-line přístup: | Získat plný text |
| Tagy: |
Přidat tag
Žádné tagy, Buďte první, kdo vytvoří štítek k tomuto záznamu!
|
| Abstract | The aryl hydrocarbon (Ah) receptor is one of the best known ligand-activated transcription factors. The present study has focused on the wound-healing process on Ah receptor function.
Depletion of calcium from culture medium of Caco-2 human colon carcinoma cells by transfer to Minimal Essential Medium (Spinner Modification; S-MEM) destroyed adherens junctions and the cells were used as the model of wound-healing process.
Calcium depletion induced both nuclear translocation of the Ah receptor, and increased expression of CYP1A1 and Slug mRNAs in Caco-2 cells. However, expression of Slug mRNA was not significantly induced by treatment with 2,3,7,8-tetrachlorodibenzo-p-dioxin. Knockdown of the Ah receptor and treatment with Ah receptor antagonists decreased level of CYP1A1 mRNA. The fragment of E-cadherin released by γ-secretase was not involved in induction of CYP1A1 mRNA following S-MEM treatment. Knockdown of β-catenin increased levels of Ah receptor mRNA, which may be attributable to direct or indirect involvement of β-catenin in suppression of the Ah receptor gene.
Our results suggest that mRNA induction of some genes by destruction of adherens junctions depends on the Ah receptor. β-Catenin, one of the components of the adherens junction, was released from the E-cadherin complex, which resulted in its increased interaction with the Ah receptor, and was translocated into the nucleus, and consequently the target genes would be transcribed.
Our observations suggest that some aspects of the molecular mechanism of wound healing involve the Ah receptor.
► Depletion of calcium by transfer of cells to S-MEM destroyed adherens junctions. ► Nuclear translocation of the Ah receptor induced CYP1A1 and Slug mRNAs. ► β-Catenin was released from E-cadherin complexes by destruction of adherens junctions. ► Interaction between β-catenin and the Ah receptor increased after S-MEM treatment. ► Knockdown of β-catenin increased the level of Ah receptor mRNA. |
|---|---|
| AbstractList | The aryl hydrocarbon (Ah) receptor is one of the best known ligand-activated transcription factors. The present study has focused on the wound-healing process on Ah receptor function.
Depletion of calcium from culture medium of Caco-2 human colon carcinoma cells by transfer to Minimal Essential Medium (Spinner Modification; S-MEM) destroyed adherens junctions and the cells were used as the model of wound-healing process.
Calcium depletion induced both nuclear translocation of the Ah receptor, and increased expression of CYP1A1 and Slug mRNAs in Caco-2 cells. However, expression of Slug mRNA was not significantly induced by treatment with 2,3,7,8-tetrachlorodibenzo-p-dioxin. Knockdown of the Ah receptor and treatment with Ah receptor antagonists decreased level of CYP1A1 mRNA. The fragment of E-cadherin released by γ-secretase was not involved in induction of CYP1A1 mRNA following S-MEM treatment. Knockdown of β-catenin increased levels of Ah receptor mRNA, which may be attributable to direct or indirect involvement of β-catenin in suppression of the Ah receptor gene.
Our results suggest that mRNA induction of some genes by destruction of adherens junctions depends on the Ah receptor. β-Catenin, one of the components of the adherens junction, was released from the E-cadherin complex, which resulted in its increased interaction with the Ah receptor, and was translocated into the nucleus, and consequently the target genes would be transcribed.
Our observations suggest that some aspects of the molecular mechanism of wound healing involve the Ah receptor.
► Depletion of calcium by transfer of cells to S-MEM destroyed adherens junctions. ► Nuclear translocation of the Ah receptor induced CYP1A1 and Slug mRNAs. ► β-Catenin was released from E-cadherin complexes by destruction of adherens junctions. ► Interaction between β-catenin and the Ah receptor increased after S-MEM treatment. ► Knockdown of β-catenin increased the level of Ah receptor mRNA. The aryl hydrocarbon (Ah) receptor is one of the best known ligand-activated transcription factors. The present study has focused on the wound-healing process on Ah receptor function. Depletion of calcium from culture medium of Caco-2 human colon carcinoma cells by transfer to Minimal Essential Medium (Spinner Modification; S-MEM) destroyed adherens junctions and the cells were used as the model of wound-healing process. Calcium depletion induced both nuclear translocation of the Ah receptor, and increased expression of CYP1A1 and Slug mRNAs in Caco-2 cells. However, expression of Slug mRNA was not significantly induced by treatment with 2,3,7,8-tetrachlorodibenzo-p-dioxin. Knockdown of the Ah receptor and treatment with Ah receptor antagonists decreased level of CYP1A1 mRNA. The fragment of E-cadherin released by gamma-secretase was not involved in induction of CYP1A1 mRNA following S-MEM treatment. Knockdown of beta-catenin increased levels of Ah receptor mRNA, which may be attributable to direct or indirect involvement of beta-catenin in suppression of the Ah receptor gene. Our results suggest that mRNA induction of some genes by destruction of adherens junctions depends on the Ah receptor. beta-Catenin, one of the components of the adherens junction, was released from the E-cadherin complex, which resulted in its increased interaction with the Ah receptor, and was translocated into the nucleus, and consequently the target genes would be transcribed. Our observations suggest that some aspects of the molecular mechanism of wound healing involve the Ah receptor. The aryl hydrocarbon (Ah) receptor is one of the best known ligand-activated transcription factors. The present study has focused on the wound-healing process on Ah receptor function.BACKGROUNDThe aryl hydrocarbon (Ah) receptor is one of the best known ligand-activated transcription factors. The present study has focused on the wound-healing process on Ah receptor function.Depletion of calcium from culture medium of Caco-2 human colon carcinoma cells by transfer to Minimal Essential Medium (Spinner Modification; S-MEM) destroyed adherens junctions and the cells were used as the model of wound-healing process.METHODSDepletion of calcium from culture medium of Caco-2 human colon carcinoma cells by transfer to Minimal Essential Medium (Spinner Modification; S-MEM) destroyed adherens junctions and the cells were used as the model of wound-healing process.Calcium depletion induced both nuclear translocation of the Ah receptor, and increased expression of CYP1A1 and Slug mRNAs in Caco-2 cells. However, expression of Slug mRNA was not significantly induced by treatment with 2,3,7,8-tetrachlorodibenzo-p-dioxin. Knockdown of the Ah receptor and treatment with Ah receptor antagonists decreased level of CYP1A1 mRNA. The fragment of E-cadherin released by gamma-secretase was not involved in induction of CYP1A1 mRNA following S-MEM treatment. Knockdown of beta-catenin increased levels of Ah receptor mRNA, which may be attributable to direct or indirect involvement of beta-catenin in suppression of the Ah receptor gene.RESULTSCalcium depletion induced both nuclear translocation of the Ah receptor, and increased expression of CYP1A1 and Slug mRNAs in Caco-2 cells. However, expression of Slug mRNA was not significantly induced by treatment with 2,3,7,8-tetrachlorodibenzo-p-dioxin. Knockdown of the Ah receptor and treatment with Ah receptor antagonists decreased level of CYP1A1 mRNA. The fragment of E-cadherin released by gamma-secretase was not involved in induction of CYP1A1 mRNA following S-MEM treatment. Knockdown of beta-catenin increased levels of Ah receptor mRNA, which may be attributable to direct or indirect involvement of beta-catenin in suppression of the Ah receptor gene.Our results suggest that mRNA induction of some genes by destruction of adherens junctions depends on the Ah receptor. beta-Catenin, one of the components of the adherens junction, was released from the E-cadherin complex, which resulted in its increased interaction with the Ah receptor, and was translocated into the nucleus, and consequently the target genes would be transcribed.CONCLUSIONSOur results suggest that mRNA induction of some genes by destruction of adherens junctions depends on the Ah receptor. beta-Catenin, one of the components of the adherens junction, was released from the E-cadherin complex, which resulted in its increased interaction with the Ah receptor, and was translocated into the nucleus, and consequently the target genes would be transcribed.Our observations suggest that some aspects of the molecular mechanism of wound healing involve the Ah receptor.GENERAL SIGNIFICANCEOur observations suggest that some aspects of the molecular mechanism of wound healing involve the Ah receptor. BACKGROUND: The aryl hydrocarbon (Ah) receptor is one of the best known ligand-activated transcription factors. The present study has focused on the wound-healing process on Ah receptor function. METHODS: Depletion of calcium from culture medium of Caco-2 human colon carcinoma cells by transfer to Minimal Essential Medium (Spinner Modification; S-MEM) destroyed adherens junctions and the cells were used as the model of wound-healing process. RESULTS: Calcium depletion induced both nuclear translocation of the Ah receptor, and increased expression of CYP1A1 and Slug mRNAs in Caco-2 cells. However, expression of Slug mRNA was not significantly induced by treatment with 2,3,7,8-tetrachlorodibenzo-p-dioxin. Knockdown of the Ah receptor and treatment with Ah receptor antagonists decreased level of CYP1A1 mRNA. The fragment of E-cadherin released by γ-secretase was not involved in induction of CYP1A1 mRNA following S-MEM treatment. Knockdown of β-catenin increased levels of Ah receptor mRNA, which may be attributable to direct or indirect involvement of β-catenin in suppression of the Ah receptor gene. CONCLUSIONS: Our results suggest that mRNA induction of some genes by destruction of adherens junctions depends on the Ah receptor. β-Catenin, one of the components of the adherens junction, was released from the E-cadherin complex, which resulted in its increased interaction with the Ah receptor, and was translocated into the nucleus, and consequently the target genes would be transcribed. GENERAL SIGNIFICANCE: Our observations suggest that some aspects of the molecular mechanism of wound healing involve the Ah receptor. The aryl hydrocarbon (Ah) receptor is one of the best known ligand-activated transcription factors. The present study has focused on the wound-healing process on Ah receptor function.Depletion of calcium from culture medium of Caco-2 human colon carcinoma cells by transfer to Minimal Essential Medium (Spinner Modification; S-MEM) destroyed adherens junctions and the cells were used as the model of wound-healing process.Calcium depletion induced both nuclear translocation of the Ah receptor, and increased expression of CYP1A1 and Slug mRNAs in Caco-2 cells. However, expression of Slug mRNA was not significantly induced by treatment with 2,3,7,8-tetrachlorodibenzo-p-dioxin. Knockdown of the Ah receptor and treatment with Ah receptor antagonists decreased level of CYP1A1 mRNA. The fragment of E-cadherin released by γ-secretase was not involved in induction of CYP1A1 mRNA following S-MEM treatment. Knockdown of β-catenin increased levels of Ah receptor mRNA, which may be attributable to direct or indirect involvement of β-catenin in suppression of the Ah receptor gene.Our results suggest that mRNA induction of some genes by destruction of adherens junctions depends on the Ah receptor. β-Catenin, one of the components of the adherens junction, was released from the E-cadherin complex, which resulted in its increased interaction with the Ah receptor, and was translocated into the nucleus, and consequently the target genes would be transcribed.Our observations suggest that some aspects of the molecular mechanism of wound healing involve the Ah receptor. |
| Author | Takumi, Ryo Kikuchi, Hideaki Kasai, Shuya Kamimura, Toru Ishigaki, Takanori |
| Author_xml | – sequence: 1 givenname: Shuya surname: Kasai fullname: Kasai, Shuya organization: Science of Biosources, United Graduate School of Agricultural Science, Iwate University, Morioka 020-8551, Japan – sequence: 2 givenname: Takanori surname: Ishigaki fullname: Ishigaki, Takanori organization: Department of Biochemistry and Molecular Biology, Faculty of Agriculture and Life Science, Hirosaki University, Hirosaki 036-8561, Japan – sequence: 3 givenname: Ryo surname: Takumi fullname: Takumi, Ryo organization: Department of Biochemistry and Molecular Biology, Faculty of Agriculture and Life Science, Hirosaki University, Hirosaki 036-8561, Japan – sequence: 4 givenname: Toru surname: Kamimura fullname: Kamimura, Toru organization: Department of Biochemistry and Molecular Biology, Faculty of Agriculture and Life Science, Hirosaki University, Hirosaki 036-8561, Japan – sequence: 5 givenname: Hideaki surname: Kikuchi fullname: Kikuchi, Hideaki email: hkikuchi@cc.hirosaki-u.ac.jp organization: Science of Biosources, United Graduate School of Agricultural Science, Iwate University, Morioka 020-8551, Japan |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/23174221$$D View this record in MEDLINE/PubMed |
| BookMark | eNqFks9u1DAQxi1URLeFN0DgI5cEj5PYWQ5IVcQ_qRJI0AMny3YmW6-y9mIniL5WH6TPhKO0Fw7Ulzn4983Y3zdn5MQHj4S8BFYCA_F2Xxqjd-hLzoCXACVj8gnZQCt50TImTsiGVawuahDNKTlLac_yabbNM3LKK5A157Ah891t0ekJvfM0uZ3Xo_M76nw_W0y0-_kNLoDin2PElFzw1NzQ3qU4H6eF0_01RvSJ7mdvp3yfspR22oaC0-v5oD21Ycwyq6N1Phw0tTiO6Tl5Ougx4Yv7ek6uPn740X0uLr9--tJdXBa2hu1UGMkayeQgeSOHQUDV2MroBgEEDNzUDDWy1lbCVEZKyXtZsx4ta7em7kWP1Tl5s_Y9xvBrxjSpg0vLC7THMCfFF0taKaB-FM3DQTDJ621GX92jszlgr47RHXS8UQ-uZuDdCtgYUoo4KOsmvfgzRe1GBUwtEaq9WiNUS4QKQOUIs7j-R_zQ_xHZ61U26KD0Lrqkrr5nQOQf8rwDLBPvVwKz478dRpWsQ2-xdxHtpPrg_j_iL3McwGE |
| CitedBy_id | crossref_primary_10_1007_s00204_016_1887_4 crossref_primary_10_1016_j_ajpath_2019_10_005 crossref_primary_10_3389_fimmu_2021_638725 crossref_primary_10_3390_nu15020305 crossref_primary_10_3390_biomedicines12122912 crossref_primary_10_3390_ijms21249614 crossref_primary_10_1155_2016_4326194 crossref_primary_10_1016_j_jsbmb_2014_11_003 crossref_primary_10_1093_mutage_gev019 crossref_primary_10_1371_journal_pone_0224613 crossref_primary_10_1038_bjc_2014_540 crossref_primary_10_1371_journal_pone_0082487 |
| Cites_doi | 10.1073/pnas.1118467109 10.1016/j.yexcr.2006.08.003 10.1016/j.ccr.2011.08.016 10.1016/S0021-9258(17)33974-1 10.1158/0008-5472.CAN-03-3309 10.1016/S0092-8674(00)81279-9 10.1016/j.bcp.2008.10.003 10.1124/mol.63.6.1373 10.1074/jbc.M708887200 10.1091/mbc.e06-04-0348 10.1126/science.2006419 10.1016/S1357-2725(03)00211-5 10.1074/jbc.M109.094847 10.1093/toxsci/kfr080 10.1016/j.yexcr.2006.08.002 10.1073/pnas.97.2.779 10.2183/pjab.86.40 10.1042/BST0360149 10.1074/jbc.M111319200 10.1016/j.bbrc.2005.08.162 10.1006/taap.1996.0210 10.1016/j.abb.2007.11.021 10.1093/toxsci/kfr129 10.1111/j.1365-2036.1995.tb00344.x 10.1083/jcb.200308162 10.1016/0003-2697(87)90021-2 10.1023/B:PHAM.0000048201.00143.72 10.1271/bbb.90438 10.1093/nar/11.5.1475 10.1016/S0092-8674(00)80112-9 10.1016/j.bbagrm.2009.06.003 10.1038/nature10491 |
| ContentType | Journal Article |
| Copyright | 2012 Elsevier B.V. |
| Copyright_xml | – notice: 2012 Elsevier B.V. |
| DBID | FBQ AAYXX CITATION CGR CUY CVF ECM EIF NPM 7X8 7S9 L.6 |
| DOI | 10.1016/j.bbagen.2012.11.007 |
| DatabaseName | AGRIS CrossRef Medline MEDLINE MEDLINE (Ovid) MEDLINE MEDLINE PubMed MEDLINE - Academic AGRICOLA AGRICOLA - Academic |
| DatabaseTitle | CrossRef MEDLINE Medline Complete MEDLINE with Full Text PubMed MEDLINE (Ovid) MEDLINE - Academic AGRICOLA AGRICOLA - Academic |
| DatabaseTitleList | MEDLINE MEDLINE - Academic AGRICOLA |
| Database_xml | – sequence: 1 dbid: NPM name: PubMed url: http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed sourceTypes: Index Database – sequence: 2 dbid: 7X8 name: MEDLINE - Academic url: https://search.proquest.com/medline sourceTypes: Aggregation Database |
| DeliveryMethod | fulltext_linktorsrc |
| Discipline | Chemistry Biology |
| EISSN | 1872-8006 |
| EndPage | 2516 |
| ExternalDocumentID | 23174221 10_1016_j_bbagen_2012_11_007 US201600024160 S0304416512003182 |
| Genre | Research Support, Non-U.S. Gov't Journal Article |
| GroupedDBID | --- --K --M .~1 0R~ 1B1 1RT 1~. 1~5 23N 3O- 4.4 457 4G. 53G 5GY 5RE 5VS 7-5 71M 8P~ 9JM AACTN AAEDT AAEDW AAIAV AAIKJ AAKOC AALRI AAOAW AAQFI AAQXK AAXUO ABEFU ABFNM ABGSF ABMAC ABUDA ABXDB ABYKQ ACDAQ ACIUM ACRLP ADBBV ADEZE ADMUD ADUVX AEBSH AEHWI AEKER AFKWA AFTJW AFXIZ AGHFR AGRDE AGUBO AGYEJ AHHHB AIEXJ AIKHN AITUG AJBFU AJOXV ALMA_UNASSIGNED_HOLDINGS AMFUW AMRAJ ASPBG AVWKF AXJTR AZFZN BKOJK BLXMC CS3 DOVZS EBS EFJIC EFLBG EJD EO8 EO9 EP2 EP3 FDB FEDTE FGOYB FIRID FNPLU FYGXN G-2 G-Q GBLVA HLW HVGLF HZ~ IHE J1W KOM LX3 M41 MO0 N9A O-L O9- OAUVE OHT OZT P-8 P-9 PC. Q38 R2- ROL RPZ SBG SCC SDF SDG SDP SES SEW SPCBC SSU SSZ T5K UQL WH7 WUQ XJT XPP ~G- AAHBH AATTM AAXKI ABWVN ACRPL ADNMO AEIPS AFJKZ AKRWK ANKPU FBQ SSH 9DU AAYWO AAYXX ACLOT ACVFH ADCNI AEUPX AFPUW AGQPQ AIGII AIIUN AKBMS AKYEP APXCP CITATION EFKBS ~HD -~X .55 .GJ AAYJJ ABJNI AFFNX AI. CGR CUY CVF ECM EIF F5P H~9 K-O MVM NPM RIG TWZ UHS VH1 X7M Y6R YYP ZE2 ZGI ~KM 7X8 ABUFD 7S9 L.6 |
| ID | FETCH-LOGICAL-c419t-b705707f7257ff6135c3ba5e1161f2b40eae08c36b3b7772d740dec089b4d6de3 |
| ISICitedReferencesCount | 16 |
| ISICitedReferencesURI | http://www.webofscience.com/api/gateway?GWVersion=2&SrcApp=Summon&SrcAuth=ProQuest&DestLinkType=CitingArticles&DestApp=WOS_CPL&KeyUT=000315307900001&url=https%3A%2F%2Fcvtisr.summon.serialssolutions.com%2F%23%21%2Fsearch%3Fho%3Df%26include.ft.matches%3Dt%26l%3Dnull%26q%3D |
| ISSN | 0304-4165 0006-3002 |
| IngestDate | Sat Sep 27 18:34:57 EDT 2025 Sun Nov 09 13:58:02 EST 2025 Mon Jul 21 06:09:26 EDT 2025 Tue Nov 18 22:32:14 EST 2025 Sat Nov 29 07:19:44 EST 2025 Thu Apr 03 09:45:01 EDT 2025 Fri Feb 23 02:32:43 EST 2024 |
| IsPeerReviewed | true |
| IsScholarly | true |
| Issue | 3 |
| Keywords | HSP90 CTF2 PAS TCDD ARNT XRE Lef EMT E-cadherin Cytochrome P-450 1A1 bHLH Aryl hydrocarbon receptor MAF E-cadherin carboxy terminal fragment 2 CYP1A1 β-Catenin XAP-2 S-MEM FoxM1 GAPDH DAPT |
| Language | English |
| LinkModel | OpenURL |
| MergedId | FETCHMERGED-LOGICAL-c419t-b705707f7257ff6135c3ba5e1161f2b40eae08c36b3b7772d740dec089b4d6de3 |
| Notes | http://dx.doi.org/10.1016/j.bbagen.2012.11.007 ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
| PMID | 23174221 |
| PQID | 1351607249 |
| PQPubID | 23479 |
| PageCount | 8 |
| ParticipantIDs | proquest_miscellaneous_2000087614 proquest_miscellaneous_1351607249 pubmed_primary_23174221 crossref_citationtrail_10_1016_j_bbagen_2012_11_007 crossref_primary_10_1016_j_bbagen_2012_11_007 fao_agris_US201600024160 elsevier_sciencedirect_doi_10_1016_j_bbagen_2012_11_007 |
| PublicationCentury | 2000 |
| PublicationDate | 2013-03-01 |
| PublicationDateYYYYMMDD | 2013-03-01 |
| PublicationDate_xml | – month: 03 year: 2013 text: 2013-03-01 day: 01 |
| PublicationDecade | 2010 |
| PublicationPlace | Netherlands |
| PublicationPlace_xml | – name: Netherlands |
| PublicationTitle | Biochimica et biophysica acta |
| PublicationTitleAlternate | Biochim Biophys Acta |
| PublicationYear | 2013 |
| Publisher | Elsevier B.V |
| Publisher_xml | – name: Elsevier B.V |
| References | Zeng, Apte, Micsenyi, Bell, Monga (bb0095) 2006; 312 Ferber, Kajita, Wadlow, Tobiansky, Niessen, Ariga, Daniel, Fujita (bb0100) 2008; 283 Le Ferrec, Lagadic Gossmann, Rauch, Bardiau, Maheo, Massiere, Le Vee, Guillouzo, Morel (bb0105) 2002; 277 Fujii Kuriyama, Kawajiri (bb0025) 2010; 86 Opitz, Litzenburger, Sahm, Ott, Tritschler, Trump, Schumacher, Jestaedt, Schrenk, Weller, Jugold, Guillemin, Miller, Lutz, Radlwimmer, Lehmann, von Deimling, Wick, Platten (bb0155) 2011; 478 Chesire, Dunn, Ewing, Luo, Isaacs (bb0150) 2004; 64 Conacci Sorrell, Simcha, Ben Yedidia, Blechman, Savagner, Ben Ze'ev (bb0075) 2003; 163 Prochazkova, Kabatkova, Bryja, Umannova, Bernatik, Kozubik, Machala, Vondracek (bb0145) 2011; 122 Zhang, Wei, Gong, Chiu, Lee, Colman, Huang, Xue, Liu, Wang, Sawaya, Xie, Yung, Medema, He, Huang (bb0135) 2011; 20 Shimizu, Nakatsuru, Ichinose, Takahashi, Kume, Mimura, Fujii Kuriyama, Ishikawa (bb0015) 2000; 97 Verma, Surabhi, Schmaltieg, Becerra, Gaynor (bb0125) 2003; 9 Nishiumi, Yamamoto, Kodoi, Fukuda, Yoshida, Ashida (bb0090) 2008; 470 Gumbiner (bb0070) 1996; 84 Sadek, Allen Hoffmann (bb0040) 1994; 269 Mitra, Menezes, Shevde, Samant (bb0165) 2010; 285 Wincent, Bengtsson, Mohammadi Bardbori, Alsberg, Luecke, Rannug, Rannug (bb0160) 2012; 109 Petersen (bb0030) 1995; 9 Perrais, Chen, Perez Moreno, Gumbiner (bb0130) 2007; 18 Calcagno, Fostel, Reyner, Sinaga, Alston, Mattes, Siahaan, Ware (bb0050) 2004; 21 Dignam, Lebovitz, Roeder (bb0085) 1983; 11 Ikuta, Kawajiri (bb0045) 2006; 312 Fernandez Salguero, Hilbert, Rudikoff, Ward, Gonzalez (bb0005) 1996; 140 Nelson (bb0055) 2008; 36 Molenaar, van de Wetering, Oosterwegel, Peterson Maduro, Godsave, Korinek, Roose, Destree, Clevers (bb0060) 1996; 86 Takeichi (bb0065) 1991; 251 Braeuning, Kohle, Buchmann, Schwarz (bb0140) 2011; 122 Ikuta, Namiki, Fujii Kuriyama, Kawajiri (bb0035) 2009; 77 Fujii Kuriyama, Mimura (bb0115) 2005; 338 Kasai, Kikuchi (bb0120) 2010; 74 Kudo, Takeuchi, Murakami, Ebina, Kikuchi (bb0110) 2009; 1789 Abdelrahim, Smith, Safe (bb0010) 2003; 63 Kewley, Whitelaw, Chapman Smith (bb0020) 2004; 36 Chomczynski, Sacchi (bb0080) 1987; 162 Molenaar (10.1016/j.bbagen.2012.11.007_bb0060) 1996; 86 Le Ferrec (10.1016/j.bbagen.2012.11.007_bb0105) 2002; 277 Kudo (10.1016/j.bbagen.2012.11.007_bb0110) 2009; 1789 Zhang (10.1016/j.bbagen.2012.11.007_bb0135) 2011; 20 Mitra (10.1016/j.bbagen.2012.11.007_bb0165) 2010; 285 Takeichi (10.1016/j.bbagen.2012.11.007_bb0065) 1991; 251 Wincent (10.1016/j.bbagen.2012.11.007_bb0160) 2012; 109 Shimizu (10.1016/j.bbagen.2012.11.007_bb0015) 2000; 97 Zeng (10.1016/j.bbagen.2012.11.007_bb0095) 2006; 312 Kasai (10.1016/j.bbagen.2012.11.007_bb0120) 2010; 74 Calcagno (10.1016/j.bbagen.2012.11.007_bb0050) 2004; 21 Chesire (10.1016/j.bbagen.2012.11.007_bb0150) 2004; 64 Conacci Sorrell (10.1016/j.bbagen.2012.11.007_bb0075) 2003; 163 Fernandez Salguero (10.1016/j.bbagen.2012.11.007_bb0005) 1996; 140 Petersen (10.1016/j.bbagen.2012.11.007_bb0030) 1995; 9 Ferber (10.1016/j.bbagen.2012.11.007_bb0100) 2008; 283 Braeuning (10.1016/j.bbagen.2012.11.007_bb0140) 2011; 122 Prochazkova (10.1016/j.bbagen.2012.11.007_bb0145) 2011; 122 Fujii Kuriyama (10.1016/j.bbagen.2012.11.007_bb0025) 2010; 86 Gumbiner (10.1016/j.bbagen.2012.11.007_bb0070) 1996; 84 Nishiumi (10.1016/j.bbagen.2012.11.007_bb0090) 2008; 470 Chomczynski (10.1016/j.bbagen.2012.11.007_bb0080) 1987; 162 Abdelrahim (10.1016/j.bbagen.2012.11.007_bb0010) 2003; 63 Ikuta (10.1016/j.bbagen.2012.11.007_bb0035) 2009; 77 Verma (10.1016/j.bbagen.2012.11.007_bb0125) 2003; 9 Sadek (10.1016/j.bbagen.2012.11.007_bb0040) 1994; 269 Nelson (10.1016/j.bbagen.2012.11.007_bb0055) 2008; 36 Perrais (10.1016/j.bbagen.2012.11.007_bb0130) 2007; 18 Dignam (10.1016/j.bbagen.2012.11.007_bb0085) 1983; 11 Opitz (10.1016/j.bbagen.2012.11.007_bb0155) 2011; 478 Fujii Kuriyama (10.1016/j.bbagen.2012.11.007_bb0115) 2005; 338 Kewley (10.1016/j.bbagen.2012.11.007_bb0020) 2004; 36 Ikuta (10.1016/j.bbagen.2012.11.007_bb0045) 2006; 312 |
| References_xml | – volume: 109 start-page: 4479 year: 2012 end-page: 4484 ident: bb0160 article-title: Inhibition of cytochrome P4501-dependent clearance of the endogenous agonist FICZ as a mechanism for activation of the aryl hydrocarbon receptor publication-title: Proc. Natl. Acad. Sci. U. S. A. – volume: 11 start-page: 1475 year: 1983 end-page: 1489 ident: bb0085 article-title: Accurate transcription initiation by RNA polymerase II in a soluble extract from isolated mammalian nuclei publication-title: Nucleic Acids Res. – volume: 36 start-page: 149 year: 2008 end-page: 155 ident: bb0055 article-title: Regulation of cell–cell adhesion by the cadherin-catenin complex publication-title: Biochem. Soc. Trans. – volume: 269 start-page: 16067 year: 1994 end-page: 16074 ident: bb0040 article-title: Cytochrome P450IA1 is rapidly induced in normal human keratinocytes in the absence of xenobiotics publication-title: J. Biol. Chem. – volume: 97 start-page: 779 year: 2000 end-page: 782 ident: bb0015 article-title: Benzo[a]pyrene carcinogenicity is lost in mice lacking the aryl hydrocarbon receptor publication-title: Proc. Natl. Acad. Sci. U. S. A. – volume: 1789 start-page: 477 year: 2009 end-page: 486 ident: bb0110 article-title: Characterization of the region of the aryl hydrocarbon receptor required for ligand dependency of transactivation using chimeric receptor between publication-title: Biochim. Biophys. Acta – volume: 470 start-page: 187 year: 2008 end-page: 199 ident: bb0090 article-title: Antagonistic and agonistic effects of indigoids on the transformation of an aryl hydrocarbon receptor publication-title: Arch. Biochem. Biophys. – volume: 338 start-page: 311 year: 2005 end-page: 317 ident: bb0115 article-title: Molecular mechanisms of AhR functions in the regulation of cytochrome P450 genes publication-title: Biochem. Biophys. Res. Commun. – volume: 9 start-page: 1 year: 1995 end-page: 9 ident: bb0030 article-title: Review article: omeprazole and the cytochrome P450 system publication-title: Aliment. Pharmacol. Ther. – volume: 312 start-page: 3585 year: 2006 end-page: 3594 ident: bb0045 article-title: Zinc finger transcription factor Slug is a novel target gene of aryl hydrocarbon receptor publication-title: Exp. Cell Res. – volume: 312 start-page: 3620 year: 2006 end-page: 3630 ident: bb0095 article-title: Tyrosine residues 654 and 670 in beta-catenin are crucial in regulation of Met-beta-catenin interactions publication-title: Exp. Cell Res. – volume: 21 start-page: 2085 year: 2004 end-page: 2094 ident: bb0050 article-title: Effects of an E-cadherin-derived peptide on the gene expression of Caco-2 cells publication-title: Pharm. Res. – volume: 163 start-page: 847 year: 2003 end-page: 857 ident: bb0075 article-title: Autoregulation of E-cadherin expression by cadherin–cadherin interactions: the roles of beta-catenin signaling, Slug, and MAPK publication-title: J. Cell Biol. – volume: 285 start-page: 24686 year: 2010 end-page: 24694 ident: bb0165 article-title: DNAJB6 induces degradation of beta-catenin and causes partial reversal of mesenchymal phenotype publication-title: J. Biol. Chem. – volume: 86 start-page: 391 year: 1996 end-page: 399 ident: bb0060 article-title: XTcf-3 transcription factor mediates beta-catenin-induced axis formation in Xenopus embryos publication-title: Cell – volume: 122 start-page: 16 year: 2011 end-page: 25 ident: bb0140 article-title: Coordinate regulation of cytochrome P450 1A1 expression in mouse liver by the aryl hydrocarbon receptor and the {beta}-catenin pathway publication-title: Toxicol. Sci. – volume: 18 start-page: 2013 year: 2007 end-page: 2025 ident: bb0130 article-title: E-cadherin homophilic ligation inhibits cell growth and epidermal growth factor receptor signaling independently of other cell interactions publication-title: Mol. Biol. Cell – volume: 77 start-page: 588 year: 2009 end-page: 596 ident: bb0035 article-title: AhR protein trafficking and function in the skin publication-title: Biochem. Pharmacol. – volume: 63 start-page: 1373 year: 2003 end-page: 1381 ident: bb0010 article-title: Aryl hydrocarbon receptor gene silencing with small inhibitory RNA differentially modulates Ah-responsiveness in MCF-7 and HepG2 cancer cells publication-title: Mol. Pharmacol. – volume: 140 start-page: 173 year: 1996 end-page: 179 ident: bb0005 article-title: Aryl-hydrocarbon receptor-deficient mice are resistant to 2,3,7,8-tetrachlorodibenzo-p-dioxin-induced toxicity publication-title: Toxicol. Appl. Pharmacol. – volume: 20 start-page: 427 year: 2011 end-page: 442 ident: bb0135 article-title: FoxM1 promotes beta-catenin nuclear localization and controls Wnt target-gene expression and glioma tumorigenesis publication-title: Cancer Cell – volume: 64 start-page: 2523 year: 2004 end-page: 2533 ident: bb0150 article-title: Identification of aryl hydrocarbon receptor as a putative Wnt/beta-catenin pathway target gene in prostate cancer cells publication-title: Cancer Res. – volume: 84 start-page: 345 year: 1996 end-page: 357 ident: bb0070 article-title: Cell adhesion: the molecular basis of tissue architecture and morphogenesis publication-title: Cell – volume: 74 start-page: 36 year: 2010 end-page: 43 ident: bb0120 article-title: The inhibitory mechanisms of the tyrosine kinase inhibitors herbimycin a, genistein, and tyrphostin B48 with regard to the function of the aryl hydrocarbon receptor in Caco-2 cells publication-title: Biosci. Biotechnol. Biochem. – volume: 86 start-page: 40 year: 2010 end-page: 53 ident: bb0025 article-title: Molecular mechanisms of the physiological functions of the aryl hydrocarbon (dioxin) receptor, a multifunctional regulator that senses and responds to environmental stimuli publication-title: Proc. Jpn. Acad. Ser. B Phys. Biol. Sci. – volume: 251 start-page: 1451 year: 1991 end-page: 1455 ident: bb0065 article-title: Cadherin cell adhesion receptors as a morphogenetic regulator publication-title: Science – volume: 9 start-page: 1291 year: 2003 end-page: 1300 ident: bb0125 article-title: Small interfering RNAs directed against beta-catenin inhibit the in vitro and in vivo growth of colon cancer cells publication-title: Clin. Cancer Res. – volume: 283 start-page: 12691 year: 2008 end-page: 12700 ident: bb0100 article-title: A role for the cleaved cytoplasmic domain of E-cadherin in the nucleus publication-title: J. Biol. Chem. – volume: 36 start-page: 189 year: 2004 end-page: 204 ident: bb0020 article-title: The mammalian basic helix-loop-helix/PAS family of transcriptional regulators publication-title: Int. J. Biochem. Cell Biol. – volume: 478 start-page: 197 year: 2011 end-page: 203 ident: bb0155 article-title: An endogenous tumour-promoting ligand of the human aryl hydrocarbon receptor publication-title: Nature – volume: 122 start-page: 349 year: 2011 end-page: 360 ident: bb0145 article-title: The interplay of the aryl hydrocarbon receptor and β-catenin alters both AhR-dependent transcription and Wnt/β-catenin signaling in liver progenitors publication-title: Toxicol. Sci. – volume: 277 start-page: 24780 year: 2002 end-page: 24787 ident: bb0105 article-title: Transcriptional induction of CYP1A1 by oltipraz in human Caco-2 cells is aryl hydrocarbon receptor- and calcium-dependent publication-title: J. Biol. Chem. – volume: 162 start-page: 156 year: 1987 end-page: 159 ident: bb0080 article-title: Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction publication-title: Anal. Biochem. – volume: 109 start-page: 4479 year: 2012 ident: 10.1016/j.bbagen.2012.11.007_bb0160 article-title: Inhibition of cytochrome P4501-dependent clearance of the endogenous agonist FICZ as a mechanism for activation of the aryl hydrocarbon receptor publication-title: Proc. Natl. Acad. Sci. U. S. A. doi: 10.1073/pnas.1118467109 – volume: 312 start-page: 3620 year: 2006 ident: 10.1016/j.bbagen.2012.11.007_bb0095 article-title: Tyrosine residues 654 and 670 in beta-catenin are crucial in regulation of Met-beta-catenin interactions publication-title: Exp. Cell Res. doi: 10.1016/j.yexcr.2006.08.003 – volume: 20 start-page: 427 year: 2011 ident: 10.1016/j.bbagen.2012.11.007_bb0135 article-title: FoxM1 promotes beta-catenin nuclear localization and controls Wnt target-gene expression and glioma tumorigenesis publication-title: Cancer Cell doi: 10.1016/j.ccr.2011.08.016 – volume: 269 start-page: 16067 year: 1994 ident: 10.1016/j.bbagen.2012.11.007_bb0040 article-title: Cytochrome P450IA1 is rapidly induced in normal human keratinocytes in the absence of xenobiotics publication-title: J. Biol. Chem. doi: 10.1016/S0021-9258(17)33974-1 – volume: 64 start-page: 2523 year: 2004 ident: 10.1016/j.bbagen.2012.11.007_bb0150 article-title: Identification of aryl hydrocarbon receptor as a putative Wnt/beta-catenin pathway target gene in prostate cancer cells publication-title: Cancer Res. doi: 10.1158/0008-5472.CAN-03-3309 – volume: 84 start-page: 345 year: 1996 ident: 10.1016/j.bbagen.2012.11.007_bb0070 article-title: Cell adhesion: the molecular basis of tissue architecture and morphogenesis publication-title: Cell doi: 10.1016/S0092-8674(00)81279-9 – volume: 77 start-page: 588 year: 2009 ident: 10.1016/j.bbagen.2012.11.007_bb0035 article-title: AhR protein trafficking and function in the skin publication-title: Biochem. Pharmacol. doi: 10.1016/j.bcp.2008.10.003 – volume: 63 start-page: 1373 year: 2003 ident: 10.1016/j.bbagen.2012.11.007_bb0010 article-title: Aryl hydrocarbon receptor gene silencing with small inhibitory RNA differentially modulates Ah-responsiveness in MCF-7 and HepG2 cancer cells publication-title: Mol. Pharmacol. doi: 10.1124/mol.63.6.1373 – volume: 9 start-page: 1291 year: 2003 ident: 10.1016/j.bbagen.2012.11.007_bb0125 article-title: Small interfering RNAs directed against beta-catenin inhibit the in vitro and in vivo growth of colon cancer cells publication-title: Clin. Cancer Res. – volume: 283 start-page: 12691 year: 2008 ident: 10.1016/j.bbagen.2012.11.007_bb0100 article-title: A role for the cleaved cytoplasmic domain of E-cadherin in the nucleus publication-title: J. Biol. Chem. doi: 10.1074/jbc.M708887200 – volume: 18 start-page: 2013 year: 2007 ident: 10.1016/j.bbagen.2012.11.007_bb0130 article-title: E-cadherin homophilic ligation inhibits cell growth and epidermal growth factor receptor signaling independently of other cell interactions publication-title: Mol. Biol. Cell doi: 10.1091/mbc.e06-04-0348 – volume: 251 start-page: 1451 year: 1991 ident: 10.1016/j.bbagen.2012.11.007_bb0065 article-title: Cadherin cell adhesion receptors as a morphogenetic regulator publication-title: Science doi: 10.1126/science.2006419 – volume: 36 start-page: 189 year: 2004 ident: 10.1016/j.bbagen.2012.11.007_bb0020 article-title: The mammalian basic helix-loop-helix/PAS family of transcriptional regulators publication-title: Int. J. Biochem. Cell Biol. doi: 10.1016/S1357-2725(03)00211-5 – volume: 285 start-page: 24686 year: 2010 ident: 10.1016/j.bbagen.2012.11.007_bb0165 article-title: DNAJB6 induces degradation of beta-catenin and causes partial reversal of mesenchymal phenotype publication-title: J. Biol. Chem. doi: 10.1074/jbc.M109.094847 – volume: 122 start-page: 16 year: 2011 ident: 10.1016/j.bbagen.2012.11.007_bb0140 article-title: Coordinate regulation of cytochrome P450 1A1 expression in mouse liver by the aryl hydrocarbon receptor and the {beta}-catenin pathway publication-title: Toxicol. Sci. doi: 10.1093/toxsci/kfr080 – volume: 312 start-page: 3585 year: 2006 ident: 10.1016/j.bbagen.2012.11.007_bb0045 article-title: Zinc finger transcription factor Slug is a novel target gene of aryl hydrocarbon receptor publication-title: Exp. Cell Res. doi: 10.1016/j.yexcr.2006.08.002 – volume: 97 start-page: 779 year: 2000 ident: 10.1016/j.bbagen.2012.11.007_bb0015 article-title: Benzo[a]pyrene carcinogenicity is lost in mice lacking the aryl hydrocarbon receptor publication-title: Proc. Natl. Acad. Sci. U. S. A. doi: 10.1073/pnas.97.2.779 – volume: 86 start-page: 40 year: 2010 ident: 10.1016/j.bbagen.2012.11.007_bb0025 article-title: Molecular mechanisms of the physiological functions of the aryl hydrocarbon (dioxin) receptor, a multifunctional regulator that senses and responds to environmental stimuli publication-title: Proc. Jpn. Acad. Ser. B Phys. Biol. Sci. doi: 10.2183/pjab.86.40 – volume: 36 start-page: 149 year: 2008 ident: 10.1016/j.bbagen.2012.11.007_bb0055 article-title: Regulation of cell–cell adhesion by the cadherin-catenin complex publication-title: Biochem. Soc. Trans. doi: 10.1042/BST0360149 – volume: 277 start-page: 24780 year: 2002 ident: 10.1016/j.bbagen.2012.11.007_bb0105 article-title: Transcriptional induction of CYP1A1 by oltipraz in human Caco-2 cells is aryl hydrocarbon receptor- and calcium-dependent publication-title: J. Biol. Chem. doi: 10.1074/jbc.M111319200 – volume: 338 start-page: 311 year: 2005 ident: 10.1016/j.bbagen.2012.11.007_bb0115 article-title: Molecular mechanisms of AhR functions in the regulation of cytochrome P450 genes publication-title: Biochem. Biophys. Res. Commun. doi: 10.1016/j.bbrc.2005.08.162 – volume: 140 start-page: 173 year: 1996 ident: 10.1016/j.bbagen.2012.11.007_bb0005 article-title: Aryl-hydrocarbon receptor-deficient mice are resistant to 2,3,7,8-tetrachlorodibenzo-p-dioxin-induced toxicity publication-title: Toxicol. Appl. Pharmacol. doi: 10.1006/taap.1996.0210 – volume: 470 start-page: 187 year: 2008 ident: 10.1016/j.bbagen.2012.11.007_bb0090 article-title: Antagonistic and agonistic effects of indigoids on the transformation of an aryl hydrocarbon receptor publication-title: Arch. Biochem. Biophys. doi: 10.1016/j.abb.2007.11.021 – volume: 122 start-page: 349 year: 2011 ident: 10.1016/j.bbagen.2012.11.007_bb0145 article-title: The interplay of the aryl hydrocarbon receptor and β-catenin alters both AhR-dependent transcription and Wnt/β-catenin signaling in liver progenitors publication-title: Toxicol. Sci. doi: 10.1093/toxsci/kfr129 – volume: 9 start-page: 1 year: 1995 ident: 10.1016/j.bbagen.2012.11.007_bb0030 article-title: Review article: omeprazole and the cytochrome P450 system publication-title: Aliment. Pharmacol. Ther. doi: 10.1111/j.1365-2036.1995.tb00344.x – volume: 163 start-page: 847 year: 2003 ident: 10.1016/j.bbagen.2012.11.007_bb0075 article-title: Autoregulation of E-cadherin expression by cadherin–cadherin interactions: the roles of beta-catenin signaling, Slug, and MAPK publication-title: J. Cell Biol. doi: 10.1083/jcb.200308162 – volume: 162 start-page: 156 year: 1987 ident: 10.1016/j.bbagen.2012.11.007_bb0080 article-title: Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction publication-title: Anal. Biochem. doi: 10.1016/0003-2697(87)90021-2 – volume: 21 start-page: 2085 year: 2004 ident: 10.1016/j.bbagen.2012.11.007_bb0050 article-title: Effects of an E-cadherin-derived peptide on the gene expression of Caco-2 cells publication-title: Pharm. Res. doi: 10.1023/B:PHAM.0000048201.00143.72 – volume: 74 start-page: 36 year: 2010 ident: 10.1016/j.bbagen.2012.11.007_bb0120 article-title: The inhibitory mechanisms of the tyrosine kinase inhibitors herbimycin a, genistein, and tyrphostin B48 with regard to the function of the aryl hydrocarbon receptor in Caco-2 cells publication-title: Biosci. Biotechnol. Biochem. doi: 10.1271/bbb.90438 – volume: 11 start-page: 1475 year: 1983 ident: 10.1016/j.bbagen.2012.11.007_bb0085 article-title: Accurate transcription initiation by RNA polymerase II in a soluble extract from isolated mammalian nuclei publication-title: Nucleic Acids Res. doi: 10.1093/nar/11.5.1475 – volume: 86 start-page: 391 year: 1996 ident: 10.1016/j.bbagen.2012.11.007_bb0060 article-title: XTcf-3 transcription factor mediates beta-catenin-induced axis formation in Xenopus embryos publication-title: Cell doi: 10.1016/S0092-8674(00)80112-9 – volume: 1789 start-page: 477 year: 2009 ident: 10.1016/j.bbagen.2012.11.007_bb0110 article-title: Characterization of the region of the aryl hydrocarbon receptor required for ligand dependency of transactivation using chimeric receptor between Drosophila and Mus musculus publication-title: Biochim. Biophys. Acta doi: 10.1016/j.bbagrm.2009.06.003 – volume: 478 start-page: 197 year: 2011 ident: 10.1016/j.bbagen.2012.11.007_bb0155 article-title: An endogenous tumour-promoting ligand of the human aryl hydrocarbon receptor publication-title: Nature doi: 10.1038/nature10491 |
| SSID | ssj0000595 ssj0025309 |
| Score | 2.14231 |
| Snippet | The aryl hydrocarbon (Ah) receptor is one of the best known ligand-activated transcription factors. The present study has focused on the wound-healing process... BACKGROUND: The aryl hydrocarbon (Ah) receptor is one of the best known ligand-activated transcription factors. The present study has focused on the... |
| SourceID | proquest pubmed crossref fao elsevier |
| SourceType | Aggregation Database Index Database Enrichment Source Publisher |
| StartPage | 2509 |
| SubjectTerms | adherens junctions Adherens Junctions - drug effects Adherens Junctions - metabolism Adherens Junctions - pathology Amyloid Precursor Protein Secretases - genetics Amyloid Precursor Protein Secretases - metabolism antagonists Aryl hydrocarbon receptor beta Catenin - genetics beta Catenin - metabolism Caco-2 Cells cadherins Cadherins - genetics Cadherins - metabolism calcium Calcium - deficiency Cell Nucleus - drug effects Cell Nucleus - metabolism colorectal neoplasms Culture Media Cytochrome P-450 1A1 Cytochrome P-450 CYP1A1 - genetics Cytochrome P-450 CYP1A1 - metabolism E-cadherin E-cadherin carboxy terminal fragment 2 Gene Expression Regulation - drug effects genes human cell lines Humans messenger RNA Models, Biological neoplasm cells Peptide Fragments - genetics Peptide Fragments - metabolism Polychlorinated Dibenzodioxins - pharmacology Protein Transport Receptors, Aryl Hydrocarbon - antagonists & inhibitors Receptors, Aryl Hydrocarbon - genetics Receptors, Aryl Hydrocarbon - metabolism RNA, Messenger - genetics RNA, Messenger - metabolism RNA, Small Interfering - genetics S-MEM Signal Transduction - drug effects Signal Transduction - genetics Snail Family Transcription Factors tetrachlorodibenzo-p-dioxin tissue repair transcription factors Transcription Factors - genetics Transcription Factors - metabolism Wound Healing - drug effects Wound Healing - genetics β-Catenin |
| Title | β-Catenin signaling induces CYP1A1 expression by disrupting adherens junctions in Caco-2 human colon carcinoma cells |
| URI | https://dx.doi.org/10.1016/j.bbagen.2012.11.007 https://www.ncbi.nlm.nih.gov/pubmed/23174221 https://www.proquest.com/docview/1351607249 https://www.proquest.com/docview/2000087614 |
| Volume | 1830 |
| WOSCitedRecordID | wos000315307900001&url=https%3A%2F%2Fcvtisr.summon.serialssolutions.com%2F%23%21%2Fsearch%3Fho%3Df%26include.ft.matches%3Dt%26l%3Dnull%26q%3D |
| hasFullText | 1 |
| inHoldings | 1 |
| isFullTextHit | |
| isPrint | |
| journalDatabaseRights | – providerCode: PRVESC databaseName: Elsevier SD Freedom Collection Journals 2021 customDbUrl: eissn: 1872-8006 dateEnd: 99991231 omitProxy: false ssIdentifier: ssj0000595 issn: 0304-4165 databaseCode: AIEXJ dateStart: 19950118 isFulltext: true titleUrlDefault: https://www.sciencedirect.com providerName: Elsevier |
| link | http://cvtisr.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwtV1bb9MwFLZ2AcELgsFYuUxGYrxEqRInqZPHUXUCVMrEOqk8WU7irOnWpLTNtP4tnvgV_CaO4zjZNFUbD7ykuTlVcj7b59jH34fQezuCfj1yElMQ3jHdyO9AnSNywpHYwrVC349KEtc-HQz80Sg43tj4rdfCXF7QLPOvroLZfzU1nANjy6Wz_2Du-qFwAvbB6LAFs8P2XoY_6PYOPhKzC06kJE6VCRr8Qq1ciQuZf9X9cWwf2pLbX-XAZtIFjdPFvJiVOdA8Hss1gAtjAn1enWrehabTJJWmn6S6ziSrdZRm-ZQbcvh_cWN-OM2jcSqpCAyxNMI0VyMoXHJ38LYmuzYWRSjHgZoJJb5Q8tgn42LFG9iO0zOu9LWH_Jxn-TxtRhzOi2l55fsqbx4zTadFqaBkDPN5cX1oQ8pM6NwuvaTLcgE1Skyiaa4dy5i1wXULTHDObrS-nhVc68n11Vu9hBqwmLTDEG6TJLg2aUsqV6W_e5OUe_CNHZ32-2zYGw0_zH6aUq9MzutX4i2baJtQL4D2dPvwc2_0pfECvFLxp34FvWyzzC28_cfr3KLNhOfrg5_SCRo-RU-q6AUfKtQ9Qxsi20EPlZ7pagc96mr5wOeo-PNLYxDXGMQVBrHCIG4wiMMVbjCINQZxjUEoihUGcYlBXGIQ1xjEJQZfoNOj3rD7yaw0PszItYOlGVIIGCyaUOg6kgR8Sy9yQu4JGyKRhISuJbiw_MjphE5IIRKMqWvFAhqYIHTjTiycXbSV5ZnYQ9i3E5uU3ACx7XqOxx3YjwXpCEGoHbkt5OhPzKKKAF_qsFwwnek4YcowTBoGYmMGhmkhsy41UwQwd9xPtfVY5cQq55QB-u4ouQfGZvwMend2ekIk96N0oeGnhd5pBDAwo_ygPBN5sWBSYLNjUeIG6-8hZWBIwRFvoZcKPvWrQHhHXULsV_co_Ro9bmrpG7S1nBfiLXoQXS4BHvtok478_aoawNHg-OtfWw3log |
| linkProvider | Elsevier |
| openUrl | ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fsummon.serialssolutions.com&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.atitle=%CE%B2-Catenin+signaling+induces+CYP1A1+expression+by+disrupting+adherens+junctions+in+Caco-2+human+colon+carcinoma+cells&rft.jtitle=Biochimica+et+biophysica+acta.+General+subjects&rft.au=Kasai%2C+Shuya&rft.au=Ishigaki%2C+Takanori&rft.au=Takumi%2C+Ryo&rft.au=Kamimura%2C+Toru&rft.date=2013-03-01&rft.issn=0304-4165&rft.volume=1830+p.2509-2516&rft.spage=2509&rft.epage=2516&rft_id=info:doi/10.1016%2Fj.bbagen.2012.11.007&rft.externalDBID=NO_FULL_TEXT |
| thumbnail_l | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=0304-4165&client=summon |
| thumbnail_m | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=0304-4165&client=summon |
| thumbnail_s | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=0304-4165&client=summon |