Cisplatinum and Taxol Induce Different Patterns of p53 Phosphorylation

Posttranslational modifications of p53 induced by two widely used anticancer agents, cisplatinum (DDP) and taxol were investigated in two human cancer cell lines. Although both drugs were able to induce phosphorylation at serine 20 (Ser20), only DDP treatment induced p53 phosphorylation at serine 15...
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Gespeichert in:

Autor*in:	Giovanna Damia [verfasserIn] Laura Filiberti [verfasserIn] Faina Vikhanskaya [verfasserIn] Laura Carrassa [verfasserIn] Yoichi Taya [verfasserIn] Maurizio Dincalci [verfasserIn] Massimo Broggini [verfasserIn]

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2001

Schlagwörter:	phosphorylation cell cycle checkpoints anticancer agents p53

Übergeordnetes Werk:	In: Neoplasia: An International Journal for Oncology Research - Elsevier, 2008, 3(2001), 1, Seite 10-16
Übergeordnetes Werk:	volume:3 ; year:2001 ; number:1 ; pages:10-16

Links:	Link aufrufen Link aufrufen Link aufrufen Journal toc Journal toc

DOI / URN:	10.1038/sj.neo.7900122

Katalog-ID:	DOAJ060015926

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allfields	10.1038/sj.neo.7900122 doi (DE-627)DOAJ060015926 (DE-599)DOAJa31c7b40578e4a19980d0994c3df9efe DE-627 ger DE-627 rakwb eng RC254-282 Giovanna Damia verfasserin aut Cisplatinum and Taxol Induce Different Patterns of p53 Phosphorylation 2001 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Posttranslational modifications of p53 induced by two widely used anticancer agents, cisplatinum (DDP) and taxol were investigated in two human cancer cell lines. Although both drugs were able to induce phosphorylation at serine 20 (Ser20), only DDP treatment induced p53 phosphorylation at serine 15 (Ser15). Moreover, both drug treatments were able to increase p53 levels and consequently the transcription of waf1 and mdm-2 genes, although DDP treatment resulted in a stronger inducer of both genes. Using two ataxia telangiectasia mutated (ATM) cell lines, the role of ATM in druginduced p53 phosphorylations was investigated. No differences in drug-induced p53 phosphorylation could be observed, indicating that ATM is not the kinase involved in these phosphorylation events. In addition, inhibition of DNA-dependent protein kinase activity by wortmannin did not abolish p53 phosphorylation at Ser15 and Ser20, again indicating that DNA-PK is unlikely to be the kinase involved. After both taxol and DDP treatments, an activation of hCHK2 was found and this is likely to be responsible for phosphorylation at Ser20. In contrast, only DDP was able to activate ATR, which is the candidate kinase for phosphorylation of Ser15 by this drug. This data clearly suggests that differential mechanisms are involved in phosphorylation and activation of p53 depending on the drug type. phosphorylation cell cycle checkpoints anticancer agents p53 Neoplasms. Tumors. Oncology. Including cancer and carcinogens Laura Filiberti verfasserin aut Faina Vikhanskaya verfasserin aut Laura Carrassa verfasserin aut Yoichi Taya verfasserin aut Maurizio Dincalci verfasserin aut Massimo Broggini verfasserin aut In Neoplasia: An International Journal for Oncology Research Elsevier, 2008 3(2001), 1, Seite 10-16 (DE-627)320468690 (DE-600)2008231-9 14765586 nnns volume:3 year:2001 number:1 pages:10-16 https://doi.org/10.1038/sj.neo.7900122 kostenfrei https://doaj.org/article/a31c7b40578e4a19980d0994c3df9efe kostenfrei http://www.sciencedirect.com/science/article/pii/S1476558601800117 kostenfrei https://doaj.org/toc/1476-5586 Journal toc kostenfrei https://doaj.org/toc/1522-8002 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2088 GBV_ILN_2106 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2507 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4393 GBV_ILN_4700 AR 3 2001 1 10-16
spelling	10.1038/sj.neo.7900122 doi (DE-627)DOAJ060015926 (DE-599)DOAJa31c7b40578e4a19980d0994c3df9efe DE-627 ger DE-627 rakwb eng RC254-282 Giovanna Damia verfasserin aut Cisplatinum and Taxol Induce Different Patterns of p53 Phosphorylation 2001 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Posttranslational modifications of p53 induced by two widely used anticancer agents, cisplatinum (DDP) and taxol were investigated in two human cancer cell lines. Although both drugs were able to induce phosphorylation at serine 20 (Ser20), only DDP treatment induced p53 phosphorylation at serine 15 (Ser15). Moreover, both drug treatments were able to increase p53 levels and consequently the transcription of waf1 and mdm-2 genes, although DDP treatment resulted in a stronger inducer of both genes. Using two ataxia telangiectasia mutated (ATM) cell lines, the role of ATM in druginduced p53 phosphorylations was investigated. No differences in drug-induced p53 phosphorylation could be observed, indicating that ATM is not the kinase involved in these phosphorylation events. In addition, inhibition of DNA-dependent protein kinase activity by wortmannin did not abolish p53 phosphorylation at Ser15 and Ser20, again indicating that DNA-PK is unlikely to be the kinase involved. After both taxol and DDP treatments, an activation of hCHK2 was found and this is likely to be responsible for phosphorylation at Ser20. In contrast, only DDP was able to activate ATR, which is the candidate kinase for phosphorylation of Ser15 by this drug. This data clearly suggests that differential mechanisms are involved in phosphorylation and activation of p53 depending on the drug type. phosphorylation cell cycle checkpoints anticancer agents p53 Neoplasms. Tumors. Oncology. Including cancer and carcinogens Laura Filiberti verfasserin aut Faina Vikhanskaya verfasserin aut Laura Carrassa verfasserin aut Yoichi Taya verfasserin aut Maurizio Dincalci verfasserin aut Massimo Broggini verfasserin aut In Neoplasia: An International Journal for Oncology Research Elsevier, 2008 3(2001), 1, Seite 10-16 (DE-627)320468690 (DE-600)2008231-9 14765586 nnns volume:3 year:2001 number:1 pages:10-16 https://doi.org/10.1038/sj.neo.7900122 kostenfrei https://doaj.org/article/a31c7b40578e4a19980d0994c3df9efe kostenfrei http://www.sciencedirect.com/science/article/pii/S1476558601800117 kostenfrei https://doaj.org/toc/1476-5586 Journal toc kostenfrei https://doaj.org/toc/1522-8002 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2088 GBV_ILN_2106 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2507 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4393 GBV_ILN_4700 AR 3 2001 1 10-16
allfields_unstemmed	10.1038/sj.neo.7900122 doi (DE-627)DOAJ060015926 (DE-599)DOAJa31c7b40578e4a19980d0994c3df9efe DE-627 ger DE-627 rakwb eng RC254-282 Giovanna Damia verfasserin aut Cisplatinum and Taxol Induce Different Patterns of p53 Phosphorylation 2001 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Posttranslational modifications of p53 induced by two widely used anticancer agents, cisplatinum (DDP) and taxol were investigated in two human cancer cell lines. Although both drugs were able to induce phosphorylation at serine 20 (Ser20), only DDP treatment induced p53 phosphorylation at serine 15 (Ser15). Moreover, both drug treatments were able to increase p53 levels and consequently the transcription of waf1 and mdm-2 genes, although DDP treatment resulted in a stronger inducer of both genes. Using two ataxia telangiectasia mutated (ATM) cell lines, the role of ATM in druginduced p53 phosphorylations was investigated. No differences in drug-induced p53 phosphorylation could be observed, indicating that ATM is not the kinase involved in these phosphorylation events. In addition, inhibition of DNA-dependent protein kinase activity by wortmannin did not abolish p53 phosphorylation at Ser15 and Ser20, again indicating that DNA-PK is unlikely to be the kinase involved. After both taxol and DDP treatments, an activation of hCHK2 was found and this is likely to be responsible for phosphorylation at Ser20. In contrast, only DDP was able to activate ATR, which is the candidate kinase for phosphorylation of Ser15 by this drug. This data clearly suggests that differential mechanisms are involved in phosphorylation and activation of p53 depending on the drug type. phosphorylation cell cycle checkpoints anticancer agents p53 Neoplasms. Tumors. Oncology. Including cancer and carcinogens Laura Filiberti verfasserin aut Faina Vikhanskaya verfasserin aut Laura Carrassa verfasserin aut Yoichi Taya verfasserin aut Maurizio Dincalci verfasserin aut Massimo Broggini verfasserin aut In Neoplasia: An International Journal for Oncology Research Elsevier, 2008 3(2001), 1, Seite 10-16 (DE-627)320468690 (DE-600)2008231-9 14765586 nnns volume:3 year:2001 number:1 pages:10-16 https://doi.org/10.1038/sj.neo.7900122 kostenfrei https://doaj.org/article/a31c7b40578e4a19980d0994c3df9efe kostenfrei http://www.sciencedirect.com/science/article/pii/S1476558601800117 kostenfrei https://doaj.org/toc/1476-5586 Journal toc kostenfrei https://doaj.org/toc/1522-8002 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2088 GBV_ILN_2106 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2507 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4393 GBV_ILN_4700 AR 3 2001 1 10-16
allfieldsGer	10.1038/sj.neo.7900122 doi (DE-627)DOAJ060015926 (DE-599)DOAJa31c7b40578e4a19980d0994c3df9efe DE-627 ger DE-627 rakwb eng RC254-282 Giovanna Damia verfasserin aut Cisplatinum and Taxol Induce Different Patterns of p53 Phosphorylation 2001 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Posttranslational modifications of p53 induced by two widely used anticancer agents, cisplatinum (DDP) and taxol were investigated in two human cancer cell lines. Although both drugs were able to induce phosphorylation at serine 20 (Ser20), only DDP treatment induced p53 phosphorylation at serine 15 (Ser15). Moreover, both drug treatments were able to increase p53 levels and consequently the transcription of waf1 and mdm-2 genes, although DDP treatment resulted in a stronger inducer of both genes. Using two ataxia telangiectasia mutated (ATM) cell lines, the role of ATM in druginduced p53 phosphorylations was investigated. No differences in drug-induced p53 phosphorylation could be observed, indicating that ATM is not the kinase involved in these phosphorylation events. In addition, inhibition of DNA-dependent protein kinase activity by wortmannin did not abolish p53 phosphorylation at Ser15 and Ser20, again indicating that DNA-PK is unlikely to be the kinase involved. After both taxol and DDP treatments, an activation of hCHK2 was found and this is likely to be responsible for phosphorylation at Ser20. In contrast, only DDP was able to activate ATR, which is the candidate kinase for phosphorylation of Ser15 by this drug. This data clearly suggests that differential mechanisms are involved in phosphorylation and activation of p53 depending on the drug type. phosphorylation cell cycle checkpoints anticancer agents p53 Neoplasms. Tumors. Oncology. Including cancer and carcinogens Laura Filiberti verfasserin aut Faina Vikhanskaya verfasserin aut Laura Carrassa verfasserin aut Yoichi Taya verfasserin aut Maurizio Dincalci verfasserin aut Massimo Broggini verfasserin aut In Neoplasia: An International Journal for Oncology Research Elsevier, 2008 3(2001), 1, Seite 10-16 (DE-627)320468690 (DE-600)2008231-9 14765586 nnns volume:3 year:2001 number:1 pages:10-16 https://doi.org/10.1038/sj.neo.7900122 kostenfrei https://doaj.org/article/a31c7b40578e4a19980d0994c3df9efe kostenfrei http://www.sciencedirect.com/science/article/pii/S1476558601800117 kostenfrei https://doaj.org/toc/1476-5586 Journal toc kostenfrei https://doaj.org/toc/1522-8002 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2088 GBV_ILN_2106 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2507 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4393 GBV_ILN_4700 AR 3 2001 1 10-16
allfieldsSound	10.1038/sj.neo.7900122 doi (DE-627)DOAJ060015926 (DE-599)DOAJa31c7b40578e4a19980d0994c3df9efe DE-627 ger DE-627 rakwb eng RC254-282 Giovanna Damia verfasserin aut Cisplatinum and Taxol Induce Different Patterns of p53 Phosphorylation 2001 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Posttranslational modifications of p53 induced by two widely used anticancer agents, cisplatinum (DDP) and taxol were investigated in two human cancer cell lines. Although both drugs were able to induce phosphorylation at serine 20 (Ser20), only DDP treatment induced p53 phosphorylation at serine 15 (Ser15). Moreover, both drug treatments were able to increase p53 levels and consequently the transcription of waf1 and mdm-2 genes, although DDP treatment resulted in a stronger inducer of both genes. Using two ataxia telangiectasia mutated (ATM) cell lines, the role of ATM in druginduced p53 phosphorylations was investigated. No differences in drug-induced p53 phosphorylation could be observed, indicating that ATM is not the kinase involved in these phosphorylation events. In addition, inhibition of DNA-dependent protein kinase activity by wortmannin did not abolish p53 phosphorylation at Ser15 and Ser20, again indicating that DNA-PK is unlikely to be the kinase involved. After both taxol and DDP treatments, an activation of hCHK2 was found and this is likely to be responsible for phosphorylation at Ser20. In contrast, only DDP was able to activate ATR, which is the candidate kinase for phosphorylation of Ser15 by this drug. This data clearly suggests that differential mechanisms are involved in phosphorylation and activation of p53 depending on the drug type. phosphorylation cell cycle checkpoints anticancer agents p53 Neoplasms. Tumors. Oncology. Including cancer and carcinogens Laura Filiberti verfasserin aut Faina Vikhanskaya verfasserin aut Laura Carrassa verfasserin aut Yoichi Taya verfasserin aut Maurizio Dincalci verfasserin aut Massimo Broggini verfasserin aut In Neoplasia: An International Journal for Oncology Research Elsevier, 2008 3(2001), 1, Seite 10-16 (DE-627)320468690 (DE-600)2008231-9 14765586 nnns volume:3 year:2001 number:1 pages:10-16 https://doi.org/10.1038/sj.neo.7900122 kostenfrei https://doaj.org/article/a31c7b40578e4a19980d0994c3df9efe kostenfrei http://www.sciencedirect.com/science/article/pii/S1476558601800117 kostenfrei https://doaj.org/toc/1476-5586 Journal toc kostenfrei https://doaj.org/toc/1522-8002 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2088 GBV_ILN_2106 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2507 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4393 GBV_ILN_4700 AR 3 2001 1 10-16
language	English
source	In Neoplasia: An International Journal for Oncology Research 3(2001), 1, Seite 10-16 volume:3 year:2001 number:1 pages:10-16
sourceStr	In Neoplasia: An International Journal for Oncology Research 3(2001), 1, Seite 10-16 volume:3 year:2001 number:1 pages:10-16
format_phy_str_mv	Article
institution	findex.gbv.de
topic_facet	phosphorylation cell cycle checkpoints anticancer agents p53 Neoplasms. Tumors. Oncology. Including cancer and carcinogens
isfreeaccess_bool	true
container_title	Neoplasia: An International Journal for Oncology Research
authorswithroles_txt_mv	Giovanna Damia @@aut@@ Laura Filiberti @@aut@@ Faina Vikhanskaya @@aut@@ Laura Carrassa @@aut@@ Yoichi Taya @@aut@@ Maurizio Dincalci @@aut@@ Massimo Broggini @@aut@@
publishDateDaySort_date	2001-01-01T00:00:00Z
hierarchy_top_id	320468690
id	DOAJ060015926
language_de	englisch
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callnumber-first	R - Medicine
author	Giovanna Damia
spellingShingle	Giovanna Damia misc RC254-282 misc phosphorylation misc cell cycle misc checkpoints misc anticancer agents misc p53 misc Neoplasms. Tumors. Oncology. Including cancer and carcinogens Cisplatinum and Taxol Induce Different Patterns of p53 Phosphorylation
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topic_title	RC254-282 Cisplatinum and Taxol Induce Different Patterns of p53 Phosphorylation phosphorylation cell cycle checkpoints anticancer agents p53
topic	misc RC254-282 misc phosphorylation misc cell cycle misc checkpoints misc anticancer agents misc p53 misc Neoplasms. Tumors. Oncology. Including cancer and carcinogens
topic_unstemmed	misc RC254-282 misc phosphorylation misc cell cycle misc checkpoints misc anticancer agents misc p53 misc Neoplasms. Tumors. Oncology. Including cancer and carcinogens
topic_browse	misc RC254-282 misc phosphorylation misc cell cycle misc checkpoints misc anticancer agents misc p53 misc Neoplasms. Tumors. Oncology. Including cancer and carcinogens
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title	Cisplatinum and Taxol Induce Different Patterns of p53 Phosphorylation
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title_full	Cisplatinum and Taxol Induce Different Patterns of p53 Phosphorylation
author_sort	Giovanna Damia
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title_sort	cisplatinum and taxol induce different patterns of p53 phosphorylation
callnumber	RC254-282
title_auth	Cisplatinum and Taxol Induce Different Patterns of p53 Phosphorylation
abstract	Posttranslational modifications of p53 induced by two widely used anticancer agents, cisplatinum (DDP) and taxol were investigated in two human cancer cell lines. Although both drugs were able to induce phosphorylation at serine 20 (Ser20), only DDP treatment induced p53 phosphorylation at serine 15 (Ser15). Moreover, both drug treatments were able to increase p53 levels and consequently the transcription of waf1 and mdm-2 genes, although DDP treatment resulted in a stronger inducer of both genes. Using two ataxia telangiectasia mutated (ATM) cell lines, the role of ATM in druginduced p53 phosphorylations was investigated. No differences in drug-induced p53 phosphorylation could be observed, indicating that ATM is not the kinase involved in these phosphorylation events. In addition, inhibition of DNA-dependent protein kinase activity by wortmannin did not abolish p53 phosphorylation at Ser15 and Ser20, again indicating that DNA-PK is unlikely to be the kinase involved. After both taxol and DDP treatments, an activation of hCHK2 was found and this is likely to be responsible for phosphorylation at Ser20. In contrast, only DDP was able to activate ATR, which is the candidate kinase for phosphorylation of Ser15 by this drug. This data clearly suggests that differential mechanisms are involved in phosphorylation and activation of p53 depending on the drug type.
abstractGer	Posttranslational modifications of p53 induced by two widely used anticancer agents, cisplatinum (DDP) and taxol were investigated in two human cancer cell lines. Although both drugs were able to induce phosphorylation at serine 20 (Ser20), only DDP treatment induced p53 phosphorylation at serine 15 (Ser15). Moreover, both drug treatments were able to increase p53 levels and consequently the transcription of waf1 and mdm-2 genes, although DDP treatment resulted in a stronger inducer of both genes. Using two ataxia telangiectasia mutated (ATM) cell lines, the role of ATM in druginduced p53 phosphorylations was investigated. No differences in drug-induced p53 phosphorylation could be observed, indicating that ATM is not the kinase involved in these phosphorylation events. In addition, inhibition of DNA-dependent protein kinase activity by wortmannin did not abolish p53 phosphorylation at Ser15 and Ser20, again indicating that DNA-PK is unlikely to be the kinase involved. After both taxol and DDP treatments, an activation of hCHK2 was found and this is likely to be responsible for phosphorylation at Ser20. In contrast, only DDP was able to activate ATR, which is the candidate kinase for phosphorylation of Ser15 by this drug. This data clearly suggests that differential mechanisms are involved in phosphorylation and activation of p53 depending on the drug type.
abstract_unstemmed	Posttranslational modifications of p53 induced by two widely used anticancer agents, cisplatinum (DDP) and taxol were investigated in two human cancer cell lines. Although both drugs were able to induce phosphorylation at serine 20 (Ser20), only DDP treatment induced p53 phosphorylation at serine 15 (Ser15). Moreover, both drug treatments were able to increase p53 levels and consequently the transcription of waf1 and mdm-2 genes, although DDP treatment resulted in a stronger inducer of both genes. Using two ataxia telangiectasia mutated (ATM) cell lines, the role of ATM in druginduced p53 phosphorylations was investigated. No differences in drug-induced p53 phosphorylation could be observed, indicating that ATM is not the kinase involved in these phosphorylation events. In addition, inhibition of DNA-dependent protein kinase activity by wortmannin did not abolish p53 phosphorylation at Ser15 and Ser20, again indicating that DNA-PK is unlikely to be the kinase involved. After both taxol and DDP treatments, an activation of hCHK2 was found and this is likely to be responsible for phosphorylation at Ser20. In contrast, only DDP was able to activate ATR, which is the candidate kinase for phosphorylation of Ser15 by this drug. This data clearly suggests that differential mechanisms are involved in phosphorylation and activation of p53 depending on the drug type.
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title_short	Cisplatinum and Taxol Induce Different Patterns of p53 Phosphorylation
url	https://doi.org/10.1038/sj.neo.7900122 https://doaj.org/article/a31c7b40578e4a19980d0994c3df9efe http://www.sciencedirect.com/science/article/pii/S1476558601800117 https://doaj.org/toc/1476-5586 https://doaj.org/toc/1522-8002
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doi_str	10.1038/sj.neo.7900122
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up_date	2024-07-04T01:44:44.134Z
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Although both drugs were able to induce phosphorylation at serine 20 (Ser20), only DDP treatment induced p53 phosphorylation at serine 15 (Ser15). Moreover, both drug treatments were able to increase p53 levels and consequently the transcription of waf1 and mdm-2 genes, although DDP treatment resulted in a stronger inducer of both genes. Using two ataxia telangiectasia mutated (ATM) cell lines, the role of ATM in druginduced p53 phosphorylations was investigated. No differences in drug-induced p53 phosphorylation could be observed, indicating that ATM is not the kinase involved in these phosphorylation events. In addition, inhibition of DNA-dependent protein kinase activity by wortmannin did not abolish p53 phosphorylation at Ser15 and Ser20, again indicating that DNA-PK is unlikely to be the kinase involved. After both taxol and DDP treatments, an activation of hCHK2 was found and this is likely to be responsible for phosphorylation at Ser20. 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Cisplatinum and Taxol Induce Different Patterns of p53 Phosphorylation

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