Estradiol as an anti-aromatase agent in human breast cancer cells

Pasqualini, Jörge R.; Chétrite, G.

doi:10.1016/j.jsbmb.2005.10.001

Cited by 17 publications

(11 citation statements)

References 39 publications

(54 reference statements)

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“…These latter results suggest that the rapid changes in aromatase activity may represent a general mechanism not related to cell specificity even though it assumes more relevance in breast cancer in which growth and progression are strongly estrogen dependent. Our data appear opposite to previous findings demonstrating that E 2 treatment reduced aromatase activity in breast cancer cells (42,43). However, it is worthwhile to point out that they come from a different experimental design performed after a long-term E 2 exposure of MCF-7 cells either cultured long term in estrogen-deprived medium or stably transfected with the aromatase gene (MCF-7aro).…”

Section: Discussioncontrasting

confidence: 99%

Rapid Estradiol/ERα Signaling Enhances Aromatase Enzymatic Activity in Breast Cancer Cells

Catalano¹,

Barone²,

Giordano

et al. 2009

Molecular Endocrinology

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In situ estrogen production by aromatase conversion from androgens plays an important role in breast tumor promotion. Here, we show that 17beta-estradiol (E2) can rapidly enhance aromatase enzymatic activity through an increase of aromatase protein phosphorylation in breast cancer cell lines. In vivo labeling experiments and site-directed mutagenesis studies demonstrated that phosphorylation of the 361-tyrosine residue is crucial in the up-regulation of aromatase activity under E2 exposure. Our results demonstrated a direct involvement of nonreceptor tyrosine-kinase c-Src in E2-stimulated aromatase activity because inhibition of its signaling abrogated the up-regulatory effects induced by E2 on aromatase activity as well as phosphorylation of aromatase protein. In addition, from our data it emerges that aromatase is a target of cross talk between growth factor receptors and estrogen receptor alpha signaling. These findings show, for the first time, that tyrosine phosphorylation processes play a key role in the rapid changes induced by E2 in aromatase enzymatic activity, revealing the existence of a short nongenomic autocrine loop between E2 and aromatase in breast cancer cells.

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Section: Discussioncontrasting

confidence: 99%

Rapid Estradiol/ERα Signaling Enhances Aromatase Enzymatic Activity in Breast Cancer Cells

Catalano¹,

Barone²,

Giordano

et al. 2009

Molecular Endocrinology

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“…Furthermore, estrogenmetabolizing enzymes such as aromatase, sulfatase, sulfotransferase, and 17b-hydroxysteroid dehydrogenases (17b-HSDs) exist in stromal cells adjacent to the tumor. These convert androgens and inactive estrogens (estrone (E1), estrone sulfate) into active estrogen (17b-estradiol, E 2 ; Pasqualini & Chetrite 2006, Takase et al 2006.…”

Section: Introductionmentioning

confidence: 99%

“…Aromatase is a key enzyme that catalyses the conversion of androgens to estrogen (Pasqualini & Chetrite 2006, Takase et al 2006. Aromatase mRNA is expressed in various tissues, such as adipose tissue, bone, brain, skin, and breast cancer (Bulun et al 2005).…”

Section: Introductionmentioning

confidence: 99%

Estrogen signaling ability in human endometrial cancer through the cancer-stromal interaction

Matsumoto

Yamaguchi

Seino

et al. 2008

Endocrine Related Cancer

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The estrogen pathway plays an important role in the etiology of human endometrial carcinoma (EC). We examined whether estrogen biosynthesis in the tumor microenvironment promotes endometrial cancer. To examine the contribution of stromal cells to estrogen signaling in EC, we used reporter cells stably transfected with the estrogen response element (ERE) fused to the destabilized green fluorescent protein (GFP) gene. In this system, the endometrial cancer stromal cells from several patients activated the ERE of cancer cells to a variable extent. The GFP expression level increased when testosterone, a substrate for aromatase, was added. The effect was variably inhibited by aromatase inhibitors (AIs), although the response to AIs varied among patients. These results suggest that GFP expression is driven by estrogen synthesized by aromatase in the endometrial cancer stromal cells. In a second experiment, we constructed an adenovirus reporter vector containing the same construct as the reporter cells described above, and visualized endogenous ERE activity in primary culture cancer cells from 15 EC specimens. The GFP expression levels varied among the cases, and in most primary tissues, ERE activities were strongly inhibited by a pure anti-estrogen, fulvestrant. Interestingly, a minority of primary tissues in endometrial cancer showed ERE activity independent of the estrogen-ER pathway. These results suggest that AI may have some therapeutic value in EC; however, the hormonal microenvironment must be assessed prior to initiating therapy.

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“…In previous studies in this laboratory it was found that E 2 is also an anti-aromatase agent in breast cancer cells [10]. This dual effect of E 2 in controlling its own bioformation is intriguing but it is interesting to mention that in recent studies it was observed that E 2 can also stimulate the formation of the biologically inactive glucuronides in breast cancer cells [11].…”

Section: Discussionmentioning

confidence: 94%

Estradiol inhibits the estrone sulfatase activity in normal and cancerous human breast tissues

Chétrite¹,

Cortés-Prieto

Philippe³

et al. 2007

The Journal of Steroid Biochemistry and Molecular Biology

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Estradiol as an anti-aromatase agent in human breast cancer cells

Cited by 17 publications

References 39 publications

Rapid Estradiol/ERα Signaling Enhances Aromatase Enzymatic Activity in Breast Cancer Cells

Rapid Estradiol/ERα Signaling Enhances Aromatase Enzymatic Activity in Breast Cancer Cells

Estrogen signaling ability in human endometrial cancer through the cancer-stromal interaction

Estradiol inhibits the estrone sulfatase activity in normal and cancerous human breast tissues

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