Reduction of Drug Accumulation in Cisplatin-Resistant Variants of Human Prostatic Cancer PC-3 Cell Line

Nakagawa, Masayuki; Nomura, Yoshio; Kohno, Kimitoshi; Ono, Masahiro; Mizoguchi, Hiroaki; Ogata, Jiro; Kuwano, Michihiko

doi:10.1016/s0022-5347(17)35948-7

Cited by 23 publications

(20 citation statements)

References 10 publications

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“…16 Cisplatin, transplatin, etoposide, adriamycin and 5-fluorouracil were purchased from Sigma Chemical (St. Louis, MO). Actinomycin-D was purchased from Nacalai Tesque (Kyoto, Japan).…”

Section: Cell Culture Drugs Irradiation and Antibodymentioning

confidence: 99%

ZNF143 activates gene expression in response to DNA damage and binds to cisplatin‐modified DNA

Ishiguchi

Izumi

Torigoe

et al. 2004

Intl Journal of Cancer

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We have identified a cisplatin-inducible gene, the mitochondrial ribosomal protein S11 (MRP S11) gene, by means of mRNA differential display. Functional analysis of the MRP S11 promoter showed that a Staf binding site in the promoter is required for both basal promoter activity and cisplatin-inducible activity. We also found that Cisplatin is a widely used anticancer agent, and DNA damage is believed to be the main basis of the antitumor effect of cisplatin. Since cisplatin resistance is a major obstacle to the treatment of solid tumors, understanding the molecular basis of the DNA damage response and of cisplatin resistance is important for clinical protocols. Cisplatin resistance is thought to involve several mechanisms, including increased drug efflux, the presence of cellular thiols, increased nucleotide excision repair activity and decreased mismatch repair activity. [1][2][3][4] In addition, several mechanisms are thought to contribute to the DNA damage response associated with cisplatin resistance. To understand fully these molecular mechanisms, it is desirable to identify and characterize all the transcription factors that are activated by DNA damage. We have previously shown that transcription factors such as Y-box binding protein (YB-1) and the CCAAT-binding transcription factor 2 (CTF2) are overexpressed in human cancer cell lines resistant to cisplatin. 5,6 YB-1 has been shown to bind preferentially to cisplatin-modified DNA 5 and is activated by nuclear translocation and by transcriptional mechanisms. Oct1 participates in the cellular response to DNA damage, 7,8 and its induction involves posttranscriptional mechanisms. Both c-Myc and AP-1 are also activated and involved in cellular responses to cisplatin. 8 One cisplatininducible cDNA clone has been shown to encode the vacuolar H ϩ -ATPase subunit c (ATP6L), 9,10 and analysis of its expression revealed that both Sp1 and Oct1 are critical for its activation by anticancer agents. 11 In order to identify novel mechanisms involved in the DNA damage response, we have used differential display to compare gene expression between control and cisplatin-treated cells. Here, we characterize one cisplatin-inducible gene, MRP S11, whose product, MRP S11, is a component of the ribosomal small subunit and binds to 12S rRNA. 12 MRP S11 appears to have RNA binding but not DNA binding activity. We have isolated the promoter region of MRP S11 in order to identify its transcriptional activators. Functional analysis revealed a critical Staf binding site in the core of the promoter. The zinc finger transcription factor, Staf, originally identified in the frog, is involved in transcriptional regulation of snRNA type and mRNA promoters transcribed either by RNA polymerase II or III. 13 Two human homologues of Staf, ZNF 76 and ZNF 143, have been isolated. 14 Here we show that activation of the transcriptional activator ZNF 143 upregulates the transcription of MRP S11. We present evidence that ZNF 143, but not ZNF 76, is induced by DNA damage. We further demonstrate that ZN...

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“…16 Cisplatin, transplatin, etoposide, adriamycin and 5-fluorouracil were purchased from Sigma Chemical (St. Louis, MO). Actinomycin-D was purchased from Nacalai Tesque (Kyoto, Japan).…”

Section: Cell Culture Drugs Irradiation and Antibodymentioning

confidence: 99%

ZNF143 activates gene expression in response to DNA damage and binds to cisplatin‐modified DNA

Ishiguchi

Izumi

Torigoe

et al. 2004

Intl Journal of Cancer

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“…4,21,22 The cisplatin-resistant cell line P/CDP5 was derived from human prostate cancer PC3 cells. 23 These cell lines were cultured in Eagle's minimal essential medium (Nissui Seiyaku, Tokyo, Japan) containing 10% FBS. The cisplatin-resistant cell line A2780/E80, derived from human ovarian cancer A2780 cells, 24 was cultured in RPMI-1640 (Nissui Seiyaku) containing 10% FBS.…”

Section: Cell Culture and Cell Linesmentioning

confidence: 99%

“…KB/CP4, P/CDP5 and A2780/E80 cells are 63-, 23-and 92-fold resistant to cisplatin compared to parental cells, respectively. 4,9,23 KB/VP2 cells are 51-fold resistant to etoposide, and KB/VJ300 cells are 394-fold resistant to vincristine compared to their parental cells. 21,22 Drugs BCECF and nigericin were obtained from Molecular Probes (Eugene, OR).…”

Section: Cell Culture and Cell Linesmentioning

confidence: 99%

Elevated expression of vacuolar proton pump genes and cellular ph in cisplatin resistance

et al. 2001

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V-ATPases are proton-translocating enzymes, which are found not only in numerous intracellular organelles but also in the plasma membranes of many eukaryotic cells. Using differential display, we have identified one of the proton pump subunit genes, ATP6C, as a cisplatin-inducible gene. Northern blot analysis demonstrated that expression of other members of the subunit is inducible by cisplatin treatment. Proton pump gene expression is also upregulated in 3 independent cisplatin-resistant cell lines but not in vincristine-or etoposide-resistant cell lines. Cellular pH was significantly higher in cisplatin-resistant cells than in sensitive parental cells. In vitro DNA-binding activity of cisplatin was markedly increased in acidic conditions, suggesting that the cytotoxicity of cisplatin is modulated by cellular pH. Furthermore, the proton pump inhibitor bafilomycin can synergistically potentiate the cytotoxicity of cisplatin but not of etoposide or camptothecin. These results indicate that cellular pH is one of the critical parameters for effective cancer chemotherapy with cisplatin.

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“…However, clinical use of this drug for long periods is often limited because of the appearance of cisplatin-resistant tumor cells [2]. Cisplatin resistance in such cells appears to be mediated through various mechanisms, including inactivation of cisplatin by thiol-containing molecules such as glutathione [3][4][5][6] and metallothionein [7,8], increased DNA repair [9][10][11], decreased drug accumulation [12][13][14][15], increased expression of DNA topoisomerase I [16], and increased abundance of thioredoxin [17]. Moreover, it has been proposed that cisplatin could be transported out of the cell after conjugation with glutathione [18] and a putative corresponding pump has been isolated and identified as human canalicular multispecific organic anion *Corresponding author.…”

Section: Introductionmentioning

confidence: 99%

Increased expression of T‐plastin gene in cisplatin‐resistant human cancer cells: identification by mRNA differential display

et al. 1996

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Key words." Cisplatin; Differential display; Plastin; Drug resistance transporter (cMOAT) [19]. Several of these mechanisms appear to operate in individual resistant cell lines, with each mechanism alone accounting for only a small portion of total resistance. Thus, in contrast to the multidrug-resistance phenotype conferred by expression of the human multidrug resistance 1 gene (MDR1) [20~23] or multidrug resistance-associated protein gene (MRP) [24,25], cisplatin resistance appears to require the simultaneous operation of multiple mechanisms.The techniques of subtractive hybridization [26] and differential hybridization [27] have been used to isolate genes that are expressed differentially between two cell populations. However, these methods are associated with incomplete recovery of the candidate clone and require large quantities of mRNA, and are time consuming and labor intensive. The technique of differential display was recently developed to overcome these problems [28,29]. We have now used differential display to isolate and characterize genes that are expressed differentially in cisplatin-resistant cell lines and their parental counterparts. Materials and methods

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Reduction of Drug Accumulation in Cisplatin-Resistant Variants of Human Prostatic Cancer PC-3 Cell Line

Cited by 23 publications

References 10 publications

ZNF143 activates gene expression in response to DNA damage and binds to cisplatin‐modified DNA

ZNF143 activates gene expression in response to DNA damage and binds to cisplatin‐modified DNA

Elevated expression of vacuolar proton pump genes and cellular ph in cisplatin resistance

Increased expression of T‐plastin gene in cisplatin‐resistant human cancer cells: identification by mRNA differential display

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