Please use this identifier to cite or link to this item: https://doi.org/10.1016/S0304-3835(99)00364-X
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dc.titleGlutathione-related factors are not correlated with sensitivity of human tumour cells to actinomycin D
dc.contributor.authorZhang, K.
dc.contributor.authorYang, E.B.
dc.contributor.authorZhao, Y.N.
dc.contributor.authorWong, K.P.
dc.contributor.authorMack, P.
dc.date.accessioned2014-11-10T09:52:23Z
dc.date.available2014-11-10T09:52:23Z
dc.date.issued2000-02-28
dc.identifier.citationZhang, K., Yang, E.B., Zhao, Y.N., Wong, K.P., Mack, P. (2000-02-28). Glutathione-related factors are not correlated with sensitivity of human tumour cells to actinomycin D. Cancer Letters 149 (1-2) : 213-220. ScholarBank@NUS Repository. https://doi.org/10.1016/S0304-3835(99)00364-X
dc.identifier.issn03043835
dc.identifier.urihttp://scholarbank.nus.edu.sg/handle/10635/107778
dc.description.abstractGlutathione (GSH) contents and activities of glutathione S-transferases (GST), glutathione reductase (GSH-RD), glutathione peroxidase (GSHpx) and glutathione conjugate export pump (GS-X pump) were determined in eight human tumour cell lines with different sensitivities to melphalan, a substrate of glutathione conjugation, and actinomycin D which has not been shown to be detoxified by glutathione-related mechanisms. Chang liver cells with highest GSH content and highest activities of GST, GSH-RD, GSHpx and GS-X pump were found to be most resistant to melphalan. Statistical analysis showed significant correlations between sensitivities of the human tumour cells to melphalan and the glutathione-related factors (r = 0.72-0.79; except for GST, r = 0.65, P = 0.08), while there were no significant correlations observed between sensitivities of the human tumour cells to actinomycin D and all the glutathione-related factors tested (r = -0.25-0.14). Significant correlations of the glutathione-related factors to resistance of human tumour cells to melphalan, a substrate of glutathione conjugation, but not to resistance of the human tumour cells to actinomycin D which has not been shown to be detoxified by glutathione-related mechanisms suggested that glutathione- related mechanisms contribute to drug resistance by increased detoxification of the drugs involved. (C) 2000 Elsevier Science Ireland Ltd.
dc.description.urihttp://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.1016/S0304-3835(99)00364-X
dc.sourceScopus
dc.subjectActinomycin D
dc.subjectGlutathione
dc.subjectGlutathione conjugate export pump
dc.subjectGlutathione peroxidase
dc.subjectGlutathione reductase
dc.subjectGlutathione S-transferase
dc.subjectHuman tumour cells
dc.subjectMelphalan
dc.typeArticle
dc.contributor.departmentBIOCHEMISTRY
dc.description.doi10.1016/S0304-3835(99)00364-X
dc.description.sourcetitleCancer Letters
dc.description.volume149
dc.description.issue1-2
dc.description.page213-220
dc.description.codenCALED
dc.identifier.isiut000085712200027
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