DNA topoisomerase inhibitor, etoposide, enhances GC‐box‐dependent promoter activity via Sp1 phosphorylation
Modification of transcription factors by anticancer agents plays an important role in both apoptotic and survival signaling. Here we report that both DNA topoisomerase I and II inhibitors such as SN‐38 and etoposide, but not cisplatin, 5‐fluorouracil or actinomycin D, can induce phosphorylation of t...
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| Veröffentlicht in: | Cancer science 2007-06, Vol.98 (6), p.858-863 |
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| creator | Niina, Ichiro Uchiumi, Takeshi Izumi, Hiroto Torigoe, Takayuki Wakasugi, Tetsuro Igarashi, Tomonori Miyamoto, Naoya Onitsuka, Takamitsu Shiota, Masaki Okayasu, Ryuichi Chijiiwa, Kazuo Kohno, Kimitoshi |
| description | Modification of transcription factors by anticancer agents plays an important role in both apoptotic and survival signaling. Here we report that both DNA topoisomerase I and II inhibitors such as SN‐38 and etoposide, but not cisplatin, 5‐fluorouracil or actinomycin D, can induce phosphorylation of the transcription factor Sp1. Furthermore, DNA topoisomerase inhibitors were shown to transactivate GC‐box‐dependent promoters such as the SV40 and vascular endothelial growth factor promoters. The phosphorylated form of Sp1 was detectable within 30 min of etoposide treatment and was greatly diminished by the presence of the PI3K inhibitor wortmannin and by DNA‐dependent protein kinase (DNA‐PK) knockdown. We also confirmed that the phosphorylated form of DNA‐PK was increased by treatment with both etoposide and SN‐38. Taken together, these findings demonstrate a novel genomic response to anticancer agents that induce Sp1 phosphorylation, and might contribute to tumor progression and drug resistance. (Cancer Sci 2007; 98: 858–863) |
| doi_str_mv | 10.1111/j.1349-7006.2007.00476.x |
| format | Article |
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Here we report that both DNA topoisomerase I and II inhibitors such as SN‐38 and etoposide, but not cisplatin, 5‐fluorouracil or actinomycin D, can induce phosphorylation of the transcription factor Sp1. Furthermore, DNA topoisomerase inhibitors were shown to transactivate GC‐box‐dependent promoters such as the SV40 and vascular endothelial growth factor promoters. The phosphorylated form of Sp1 was detectable within 30 min of etoposide treatment and was greatly diminished by the presence of the PI3K inhibitor wortmannin and by DNA‐dependent protein kinase (DNA‐PK) knockdown. We also confirmed that the phosphorylated form of DNA‐PK was increased by treatment with both etoposide and SN‐38. Taken together, these findings demonstrate a novel genomic response to anticancer agents that induce Sp1 phosphorylation, and might contribute to tumor progression and drug resistance. (Cancer Sci 2007; 98: 858–863)</description><identifier>ISSN: 1347-9032</identifier><identifier>EISSN: 1349-7006</identifier><identifier>DOI: 10.1111/j.1349-7006.2007.00476.x</identifier><identifier>PMID: 17441964</identifier><language>eng</language><publisher>Melbourne, Australia: Blackwell Publishing Asia</publisher><subject>Antineoplastic Agents, Phytogenic - pharmacology ; Biological and medical sciences ; Camptothecin - analogs & derivatives ; Camptothecin - pharmacology ; DNA-Activated Protein Kinase - metabolism ; Enzyme Inhibitors ; Etoposide - pharmacology ; GC Rich Sequence ; Humans ; Irinotecan ; Medical sciences ; Original ; Phosphorylation ; Promoter Regions, Genetic ; Simian virus 40 ; Sp1 Transcription Factor - metabolism ; Topoisomerase I Inhibitors ; Transfection ; Tumor Cells, Cultured ; Tumors</subject><ispartof>Cancer science, 2007-06, Vol.98 (6), p.858-863</ispartof><rights>2007 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c6176-4f9b93df0e400f0ab3844b95faaa98d9276b541cfdf340007f735ced50c242a13</citedby><cites>FETCH-LOGICAL-c6176-4f9b93df0e400f0ab3844b95faaa98d9276b541cfdf340007f735ced50c242a13</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC11158573/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC11158573/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,727,780,784,885,1416,11560,27922,27923,45572,45573,46050,46474,53789,53791</link.rule.ids><linktorsrc>$$Uhttps://onlinelibrary.wiley.com/doi/abs/10.1111%2Fj.1349-7006.2007.00476.x$$EView_record_in_Wiley-Blackwell$$FView_record_in_$$GWiley-Blackwell</linktorsrc><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=18787743$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/17441964$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Niina, Ichiro</creatorcontrib><creatorcontrib>Uchiumi, Takeshi</creatorcontrib><creatorcontrib>Izumi, Hiroto</creatorcontrib><creatorcontrib>Torigoe, Takayuki</creatorcontrib><creatorcontrib>Wakasugi, Tetsuro</creatorcontrib><creatorcontrib>Igarashi, Tomonori</creatorcontrib><creatorcontrib>Miyamoto, Naoya</creatorcontrib><creatorcontrib>Onitsuka, Takamitsu</creatorcontrib><creatorcontrib>Shiota, Masaki</creatorcontrib><creatorcontrib>Okayasu, Ryuichi</creatorcontrib><creatorcontrib>Chijiiwa, Kazuo</creatorcontrib><creatorcontrib>Kohno, Kimitoshi</creatorcontrib><title>DNA topoisomerase inhibitor, etoposide, enhances GC‐box‐dependent promoter activity via Sp1 phosphorylation</title><title>Cancer science</title><addtitle>Cancer Sci</addtitle><description>Modification of transcription factors by anticancer agents plays an important role in both apoptotic and survival signaling. Here we report that both DNA topoisomerase I and II inhibitors such as SN‐38 and etoposide, but not cisplatin, 5‐fluorouracil or actinomycin D, can induce phosphorylation of the transcription factor Sp1. Furthermore, DNA topoisomerase inhibitors were shown to transactivate GC‐box‐dependent promoters such as the SV40 and vascular endothelial growth factor promoters. The phosphorylated form of Sp1 was detectable within 30 min of etoposide treatment and was greatly diminished by the presence of the PI3K inhibitor wortmannin and by DNA‐dependent protein kinase (DNA‐PK) knockdown. We also confirmed that the phosphorylated form of DNA‐PK was increased by treatment with both etoposide and SN‐38. Taken together, these findings demonstrate a novel genomic response to anticancer agents that induce Sp1 phosphorylation, and might contribute to tumor progression and drug resistance. (Cancer Sci 2007; 98: 858–863)</description><subject>Antineoplastic Agents, Phytogenic - pharmacology</subject><subject>Biological and medical sciences</subject><subject>Camptothecin - analogs & derivatives</subject><subject>Camptothecin - pharmacology</subject><subject>DNA-Activated Protein Kinase - metabolism</subject><subject>Enzyme Inhibitors</subject><subject>Etoposide - pharmacology</subject><subject>GC Rich Sequence</subject><subject>Humans</subject><subject>Irinotecan</subject><subject>Medical sciences</subject><subject>Original</subject><subject>Phosphorylation</subject><subject>Promoter Regions, Genetic</subject><subject>Simian virus 40</subject><subject>Sp1 Transcription Factor - metabolism</subject><subject>Topoisomerase I Inhibitors</subject><subject>Transfection</subject><subject>Tumor Cells, Cultured</subject><subject>Tumors</subject><issn>1347-9032</issn><issn>1349-7006</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2007</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkcFu1DAQhiNERUvhFZAvcCLpOHbsWEJCq4UWpAoOhbPlODbrVRIHO7vs3ngEnpEnqdNdtXACS7ZHmm_G__jPMoShwGldrAtMqMg5ACtKAF4AUM6K3aPs7D7x-C7muQBSnmZPY1wDEEYFfZKdYk4pFoyeZf7dpwWa_Ohd9L0JKhrkhpVr3OTDa2TmTHStSeGwUoM2EV0tf__81fhdOlszmqE1w4TG4Hs_mYCUntzWTXu0dQrdjBiNKx_TDvtOTc4Pz7ITq7ponh_v8-zr5fsvyw_59eerj8vFda4Z5iynVjSCtBYMBbCgGlJT2ojKKqVE3YqSs6aiWNvWkkQAt5xU2rQV6JKWCpPz7O2h77hpetPqJDKoTo7B9SrspVdO_p0Z3Ep-81uZvreqK05Sh1fHDsF_35g4yd5FbbpODcZvouRAkwLg_wRLwARqxhJYH0AdfIzB2Hs5GOZ3sVzL2T452ydnX-Wdr3KXSl_8Oc5D4dHIBLw8Aipq1dmQzHLxgat5zTmdp3pz4H64zuz_W4BcLm5SQG4BNMzCnQ</recordid><startdate>200706</startdate><enddate>200706</enddate><creator>Niina, Ichiro</creator><creator>Uchiumi, Takeshi</creator><creator>Izumi, Hiroto</creator><creator>Torigoe, Takayuki</creator><creator>Wakasugi, Tetsuro</creator><creator>Igarashi, Tomonori</creator><creator>Miyamoto, Naoya</creator><creator>Onitsuka, Takamitsu</creator><creator>Shiota, Masaki</creator><creator>Okayasu, Ryuichi</creator><creator>Chijiiwa, Kazuo</creator><creator>Kohno, Kimitoshi</creator><general>Blackwell Publishing Asia</general><general>Blackwell</general><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7TM</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>200706</creationdate><title>DNA topoisomerase inhibitor, etoposide, enhances GC‐box‐dependent promoter activity via Sp1 phosphorylation</title><author>Niina, Ichiro ; Uchiumi, Takeshi ; Izumi, Hiroto ; Torigoe, Takayuki ; Wakasugi, Tetsuro ; Igarashi, Tomonori ; Miyamoto, Naoya ; Onitsuka, Takamitsu ; Shiota, Masaki ; Okayasu, Ryuichi ; Chijiiwa, Kazuo ; Kohno, Kimitoshi</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c6176-4f9b93df0e400f0ab3844b95faaa98d9276b541cfdf340007f735ced50c242a13</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2007</creationdate><topic>Antineoplastic Agents, Phytogenic - pharmacology</topic><topic>Biological and medical sciences</topic><topic>Camptothecin - analogs & derivatives</topic><topic>Camptothecin - pharmacology</topic><topic>DNA-Activated Protein Kinase - metabolism</topic><topic>Enzyme Inhibitors</topic><topic>Etoposide - pharmacology</topic><topic>GC Rich Sequence</topic><topic>Humans</topic><topic>Irinotecan</topic><topic>Medical sciences</topic><topic>Original</topic><topic>Phosphorylation</topic><topic>Promoter Regions, Genetic</topic><topic>Simian virus 40</topic><topic>Sp1 Transcription Factor - metabolism</topic><topic>Topoisomerase I Inhibitors</topic><topic>Transfection</topic><topic>Tumor Cells, Cultured</topic><topic>Tumors</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Niina, Ichiro</creatorcontrib><creatorcontrib>Uchiumi, Takeshi</creatorcontrib><creatorcontrib>Izumi, Hiroto</creatorcontrib><creatorcontrib>Torigoe, Takayuki</creatorcontrib><creatorcontrib>Wakasugi, Tetsuro</creatorcontrib><creatorcontrib>Igarashi, Tomonori</creatorcontrib><creatorcontrib>Miyamoto, Naoya</creatorcontrib><creatorcontrib>Onitsuka, Takamitsu</creatorcontrib><creatorcontrib>Shiota, Masaki</creatorcontrib><creatorcontrib>Okayasu, Ryuichi</creatorcontrib><creatorcontrib>Chijiiwa, Kazuo</creatorcontrib><creatorcontrib>Kohno, Kimitoshi</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Nucleic Acids Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Cancer science</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext_linktorsrc</fulltext></delivery><addata><au>Niina, Ichiro</au><au>Uchiumi, Takeshi</au><au>Izumi, Hiroto</au><au>Torigoe, Takayuki</au><au>Wakasugi, Tetsuro</au><au>Igarashi, Tomonori</au><au>Miyamoto, Naoya</au><au>Onitsuka, Takamitsu</au><au>Shiota, Masaki</au><au>Okayasu, Ryuichi</au><au>Chijiiwa, Kazuo</au><au>Kohno, Kimitoshi</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>DNA topoisomerase inhibitor, etoposide, enhances GC‐box‐dependent promoter activity via Sp1 phosphorylation</atitle><jtitle>Cancer science</jtitle><addtitle>Cancer Sci</addtitle><date>2007-06</date><risdate>2007</risdate><volume>98</volume><issue>6</issue><spage>858</spage><epage>863</epage><pages>858-863</pages><issn>1347-9032</issn><eissn>1349-7006</eissn><abstract>Modification of transcription factors by anticancer agents plays an important role in both apoptotic and survival signaling. Here we report that both DNA topoisomerase I and II inhibitors such as SN‐38 and etoposide, but not cisplatin, 5‐fluorouracil or actinomycin D, can induce phosphorylation of the transcription factor Sp1. Furthermore, DNA topoisomerase inhibitors were shown to transactivate GC‐box‐dependent promoters such as the SV40 and vascular endothelial growth factor promoters. The phosphorylated form of Sp1 was detectable within 30 min of etoposide treatment and was greatly diminished by the presence of the PI3K inhibitor wortmannin and by DNA‐dependent protein kinase (DNA‐PK) knockdown. We also confirmed that the phosphorylated form of DNA‐PK was increased by treatment with both etoposide and SN‐38. Taken together, these findings demonstrate a novel genomic response to anticancer agents that induce Sp1 phosphorylation, and might contribute to tumor progression and drug resistance. (Cancer Sci 2007; 98: 858–863)</abstract><cop>Melbourne, Australia</cop><pub>Blackwell Publishing Asia</pub><pmid>17441964</pmid><doi>10.1111/j.1349-7006.2007.00476.x</doi><tpages>6</tpages></addata></record> |
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| identifier | ISSN: 1347-9032 |
| ispartof | Cancer science, 2007-06, Vol.98 (6), p.858-863 |
| issn | 1347-9032 1349-7006 |
| language | eng |
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| subjects | Antineoplastic Agents, Phytogenic - pharmacology Biological and medical sciences Camptothecin - analogs & derivatives Camptothecin - pharmacology DNA-Activated Protein Kinase - metabolism Enzyme Inhibitors Etoposide - pharmacology GC Rich Sequence Humans Irinotecan Medical sciences Original Phosphorylation Promoter Regions, Genetic Simian virus 40 Sp1 Transcription Factor - metabolism Topoisomerase I Inhibitors Transfection Tumor Cells, Cultured Tumors |
| title | DNA topoisomerase inhibitor, etoposide, enhances GC‐box‐dependent promoter activity via Sp1 phosphorylation |
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