Potentiation of CYP1A1 Gene Expression in MCF-7 Human Breast Cancer Cells Cotreated with 2,3,7,8-Tetrachlorodibenzo-p-Dioxin and 12-O-Tetradecanoylphorbol-13-Acetate

Moore, Michael J.; Narasimhan, T.R.; Steinberg, Michael A.; Safe, Stephen

doi:10.1006/abbi.1993.1451

Cited by 25 publications

(13 citation statements)

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“…These results suggest that the Ah nonresponsiveness of Hs578T cells is not due to the failure of these cells to express the AhR and form a nuclear 6.9 S AhR complex or to interact with DREs. The results are in contrast to mutant benzo[a]pyrene-resistant MCF-7 breast cancer cells that also express the nuclear AhR but do not bind to a DRE (Moore et al, 1993). The failure of the AhR to form a DRE complex is consistent with the Ah non-responsiveness of the mutant MCF-7 cells; however, the results obtained with Hs578T cells indicate that other factors must be associated with the failure to observe an induction response with TCDD.…”

Section: Discussioncontrasting

confidence: 44%

“…Studies in this laboratory have focused on determining the regulation of Ah responsiveness in human breast cancer cell lines using induction of CYPlAI and inhibition of oestrogeninduced gene expression as models (Harris et al, 1989;Arellano et al, 1993;Moore et al, 1993;Wang et al, 1993;Thomsen et al, 1994;Chaloupka et al, 1995). Several reports suggest that induction of CYPlAI in human breast cancer cells by AhR agonists requires a functional ER (Jaiswal et al, 1985;Ivy et al, 1988;Pasanen et al, 1988;Harris et al, 1989;Thomsen et al, 1991Thomsen et al, ,1994.…”

Section: Discussionmentioning

confidence: 99%

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Effect of transient expression of the oestrogen receptor on constitutive and inducible CYP1A1 in Hs578T human breast cancer cells

Thomsen²,

Porter³

et al. 1996

Br J Cancer

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Summary Hs578T human breast cancer cells are an oestrogen receptor (ER)-negative cell line. Treatment of these cells with 2,3,7,8-tetrachlorodibenzo-p-dioxin (TCDD) resulted in formation of a 6.9 S nuclear aryl hydrocarbon (Ah) receptor complex, which bound to a [32P]dioxin-responsive element in a gel electrophoretic mobility shift assay. However, TCDD does not induce CYPlAl gene expression or chloramphenicol acetyl transferase (CAT) activity in cells transiently transfected with pRNHllc or pMCAT5.12, which are Ahresponsive plasmids derived from the 5'-flanking region of the human and murine CYP1A1 genes respectively. Restoration of Ah responsiveness was investigated by co-transfecting Hs578T cells with pRNH1 lc or pMCAT5.12 and plasmids that express the ER (hER), Ah receptor (AhR) and AhR nuclear translocator (Arnt) proteins. ER expression resulted in significantly increased basal CAT activity; however, TCDD did not induce CAT activity in the transiently transfected cells. Expression of the AhR or Arnt proteins did not alter basal or inducible CAT activity. Expression of N-or C-terminal truncated ER in Hs578T resulted in differential regulation of Ah responsiveness. In Hs578T cells transiently expressing the ER, which contains Cterminal deletions (amino acids 282-595), basal CAT activity was also increased; however, Ah responsiveness was not restored. In contrast, transient expression of N-terminal-deleted (amino acids 1 -178) ER resulted in a marked decrease in basal CAT activity but a restoration of Ah responsiveness. These results suggest that basal and inducible CAT activity in Hs578T cells transiently transfected with pRNHl lc is modulated differentially by ER domains that are present in the N-and C-terminal regions of the ER.

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Section: Discussioncontrasting

confidence: 44%

Section: Discussionmentioning

confidence: 99%

Effect of transient expression of the oestrogen receptor on constitutive and inducible CYP1A1 in Hs578T human breast cancer cells

Thomsen²,

Porter³

et al. 1996

Br J Cancer

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“…This was first observed by Nebert et al (20) almost 30 years ago, when reduced cytochrome P450-catalyzed aryl hydrocarbon hydroxylase activity in both animals and cultured cells was observed after exposure to 17␤-estradiol. This observation has appeared periodically in the literature, but no mechanism has unequivocally defined the effect (21)(22)(23)(24)(25).…”

Section: Tcddmentioning

confidence: 99%

Estrogen Receptor Reduces CYP1A1 Induction in Cultured Human Endometrial Cells

Ricci¹,

Toscano

Mattingly

et al. 1999

Journal of Biological Chemistry

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“…In fact, after 12 hours the activity recovers by reaching 78% of value of the control (MC treated, time 0) and remains constant up to 24 hours. The biphasic effect of TPA on MC-induced CYP1A, was already demonstrated by Moore et al [58] who found that TPA causes a time and concentration-dependent modulation of TCDD-induced CYP1A1 gene expression in MCF-7 cells.…”

Section: Discussionmentioning

confidence: 73%

“…These observations are consistent with many studies in the last decade which have reported the modulation mediated by PKC of CYP1A1 activity and expression in many cell types and tissues. A various number of data and papers on in vitro and in vivo studies suggest that serine/threonine kinase PKC plays an important role in the regulation of AhR signal transduction pathway [14,15,23,25,58,59].…”

Section: Discussionmentioning

confidence: 99%

Modulation of CYP1A1 by PKC Inhibitors and TPA Pre-Treatments in MH1C1 Rat Hepatoma Cells Exposed to 3 -Methylcholanthrene

Pascale¹,

Domenicotti²,

Nitti³

et al. 2009

TOTOXIJ

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Cytochrome P4501A1 (CYP1A1), an enzyme known to metabolize polycyclic aromatic hydrocarbons, is regulated by the aryl hydrocarbon receptor (AhR). The involvement of protein kinase C (PKC) in the regulation of AhR signal transduction pathway, has been widely studied but the role of specific PKC isoform(s) involved in this process it is not well clarified. To study which PKC isoform(s) is implicated in the regulation of CYP1A1, in the poorly tumorigenic MH1C1 rat hepatoma cells, we examined the effects of some PKC pharmacological inhibitors, Calphostin C (CAL), Staurosporine (STA) and H7, and of 12-0-tetradecanoyl phorbol 13-acetate (TPA), a PKC activator, on basal and 3-methylcholanthrene (MC)-induced CYP1A1 protein expression and mediated ethoxyresorufin O-deethylation (EROD) activity. In parallel, the activities of PKC-, -I, -and -isoforms, the most expressed in MH1C1 cells, were monitored. After pre-treatment with CAL, STA and H7, the MC-induced CYP1A1 protein and EROD activity were rapidly reduced with temporal profile similar to the profile of the activity of and 1 PKC isoforms. Moreover, TPA pre-treatment induced a biphasic effect on EROD activity, and a decline of PKC -I and -, in first instance, and -and -activities later on. These findings clearly show that, in MH1C1 cells, PKC is involved in CYP1A1 regulation and that and I classic PKC isoforms play an active role in modulating this process.

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Potentiation of CYP1A1 Gene Expression in MCF-7 Human Breast Cancer Cells Cotreated with 2,3,7,8-Tetrachlorodibenzo-p-Dioxin and 12-O-Tetradecanoylphorbol-13-Acetate

Cited by 25 publications

References 0 publications

Effect of transient expression of the oestrogen receptor on constitutive and inducible CYP1A1 in Hs578T human breast cancer cells

Effect of transient expression of the oestrogen receptor on constitutive and inducible CYP1A1 in Hs578T human breast cancer cells

Estrogen Receptor Reduces CYP1A1 Induction in Cultured Human Endometrial Cells

Modulation of CYP1A1 by PKC Inhibitors and TPA Pre-Treatments in MH1C1 Rat Hepatoma Cells Exposed to 3 -Methylcholanthrene

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