Biological effects of stable overexpression of aromatase in human hormone-dependent breast cancer cells

Macaulay, Valentine M.; Nicholls, Joanne E.; Gledhill, Judith; Rowlands, Martin; Dowsett, Mitchell; Ashworth, Alan

doi:10.1038/bjc.1994.12

Cited by 31 publications

(27 citation statements)

References 27 publications

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“…Therefore these experiments were repeated in a non-replicative transfection system. WT MCF-7 cells express very low levels of aromatase activity detected only on prolonged (24 h) enzyme assay, and endogenous P450arom transcripts are not detectable by Northern blotting [16]. Transfected MCF-7 cultures expressed measurable P450arom transcripts and aromatase enzyme activity after 72 h. There was significant reduction in the level of full-length P450arom transcripts and enzyme activity in cultures transfected with P450arom cDNA cross-linked to Pso20T.…”

Section: Discussionmentioning

confidence: 95%

“…P450arom expression constructs WT P450arom cDNA was cloned from human placental cDNA [16]. t was subcloned into expression vectors pCDM8 [17] (Invitrogen Co. ~an Diego) and pRc/CMV (Invitrogen) to create expression vectors ~3610 and p3681 respectively [16].…”

Section: Electrophoretic Mobility Shift Assaysmentioning

confidence: 99%

“…After one hour's incubation at room temperature the reactions were irradiated at 365 nm for 5 min on ice. Subconfluent cultures of COS and MCF-7 cells were transfected by electroporation in HEPES-buffered saline [16]. A fl-galactosidase expression vector pCH110 (2 #g; Pharmacia) was cotransfected into COS cells for measurement of transfection efficiency.…”

Section: Cell Culture and Transjectionmentioning

confidence: 99%

“…Aromatase activity was measured in intact cells by the tritiated water release method, using as substrate 1 #Ci of 250 nM [lfl-3H]androstenedione (specific activity 24 Ci/mmol, New England Nuclear) as previously described [16]. The activity was measured at three time points between 30 min and 4 h to confirm linearity of tritiated water release.…”

Section: Enzyme Assaysmentioning

confidence: 99%

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Inhibition of aromatase expression by a psoralen‐linked triplex‐forming oligonucleotide targeted to a coding sequence

et al. 1995

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The cytochrome P450 enzyme aromatase (P450arom) is an important target in breast cancer treatment. We have designed a 20-base pyrimidine oligodeoxynucleotide (ODN) which forms a sequence-specific triple helix (triplex) with a purine-rich tract in the P450arom coding sequence. The psoralen-linked ODN (Pso20T) formed photo-induced cross-linked products with target double-stranded DNA. Cross-linked adducts formed in vitro between ODNs and P450arom expression constructs were used to transfect COS and human MCF-7 breast cancer cells. Levels of aromatase transcripts and enzyme activity were significantly lower in cultures transfected with Pso20T-treated cDNA relative to controls. Pso20T had a lesser inhibitory effect on aromatase expression from a mutant P450arom construct, consistent with predicted effects of the mutations on triplex formation. These results are compatible with triplex-mediated interruption of transcription within intact cells.

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Section: Discussionmentioning

confidence: 95%

Section: Electrophoretic Mobility Shift Assaysmentioning

confidence: 99%

Section: Cell Culture and Transjectionmentioning

confidence: 99%

Section: Enzyme Assaysmentioning

confidence: 99%

See 2 more Smart Citations

Inhibition of aromatase expression by a psoralen‐linked triplex‐forming oligonucleotide targeted to a coding sequence

et al. 1995

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“…Irahara and colleagues observed an elevated level of aromatase mRNA in breast cancer cells when compared to normal breast tissue (Irahara et al, 2006). Furthermore, aromatase has been shown to stimulate the growth of breast cancer cells in vitro (Macaulay et al, 1994). The aromatase is the product of the CYP19 gene which is a member of the cytochrome P450 enzymes family.…”

Section: Aromatase Enzymementioning

confidence: 99%

Is Mammographic Density a Biomarker to Study the Molecular Causes of Breast Cancer?

Hanna¹,

Diorio²

2012

Mammography - Recent Advances

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Characterization by thermal analysis of high density polyethylene/polypropylene blends with enhanced biodegradability

Contat‐Rodrigo

Ribes‐Greus

Imrie

2002

J of Applied Polymer Sci

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Blends of high density polyethylene (HDPE) and polypropylene (PP) with different biodegradable additives have been subjected to an outdoor soil burial test. The effect of the degradation process on the structural and morphological properties of the samples has been studied by thermogravimetry, differential scanning calorimetry, and dynamic-mechanical spectroscopy. The thermogravimetric results show that the additive is more affected by the degradation process than the polymeric matrix. Changes both in the crystalline morphology and the activation energies of the relaxation processes take place in different stages, and can be described using polynomial equations. These changes occur on different time scales depending on the additive used.

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Biological effects of stable overexpression of aromatase in human hormone-dependent breast cancer cells

Cited by 31 publications

References 27 publications

Inhibition of aromatase expression by a psoralen‐linked triplex‐forming oligonucleotide targeted to a coding sequence

Inhibition of aromatase expression by a psoralen‐linked triplex‐forming oligonucleotide targeted to a coding sequence

Is Mammographic Density a Biomarker to Study the Molecular Causes of Breast Cancer?

Characterization by thermal analysis of high density polyethylene/polypropylene blends with enhanced biodegradability

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