Please use this identifier to cite or link to this item:
https://doi.org/10.1016/S0304-3835(99)00364-X
DC Field | Value | |
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dc.title | Glutathione-related factors are not correlated with sensitivity of human tumour cells to actinomycin D | |
dc.contributor.author | Zhang, K. | |
dc.contributor.author | Yang, E.B. | |
dc.contributor.author | Zhao, Y.N. | |
dc.contributor.author | Wong, K.P. | |
dc.contributor.author | Mack, P. | |
dc.date.accessioned | 2014-11-10T09:52:23Z | |
dc.date.available | 2014-11-10T09:52:23Z | |
dc.date.issued | 2000-02-28 | |
dc.identifier.citation | Zhang, 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.issn | 03043835 | |
dc.identifier.uri | http://scholarbank.nus.edu.sg/handle/10635/107778 | |
dc.description.abstract | Glutathione (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.uri | http://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.1016/S0304-3835(99)00364-X | |
dc.source | Scopus | |
dc.subject | Actinomycin D | |
dc.subject | Glutathione | |
dc.subject | Glutathione conjugate export pump | |
dc.subject | Glutathione peroxidase | |
dc.subject | Glutathione reductase | |
dc.subject | Glutathione S-transferase | |
dc.subject | Human tumour cells | |
dc.subject | Melphalan | |
dc.type | Article | |
dc.contributor.department | BIOCHEMISTRY | |
dc.description.doi | 10.1016/S0304-3835(99)00364-X | |
dc.description.sourcetitle | Cancer Letters | |
dc.description.volume | 149 | |
dc.description.issue | 1-2 | |
dc.description.page | 213-220 | |
dc.description.coden | CALED | |
dc.identifier.isiut | 000085712200027 | |
Appears in Collections: | Staff Publications |
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