Estrogen induced synthesis of specific proteins in human breast cancer cells

Edwards, Dean P.; Adams, David J.; Savage, Nerina; McGuire, William

doi:10.1016/0006-291x(80)91148-1

Cited by 105 publications

(32 citation statements)

References 11 publications

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“…The data indicate that E 2 -mediated Hsp22 induction is fairly pronounced (Ͼ3-fold) compared with other proteins. For example, Hsp27, another sHSP induced by E 2 in ER ϩ breast cancer cells, was induced ϳ1.5-fold by E 2 (Edwards et al 1980). The inhibitory effects of the anti-estrogen ICI182780 and the RNA polymerase II inhibitor actinomycin D suggest involvement of ER␣ in the transcriptional regulation of Hsp22.…”

Section: Discussionmentioning

confidence: 99%

“…Hsp27 was also reported to be induced by E 2 , although on a lesser scale (Edwards et al 1980). We therefore included Hsp27 in this analysis.…”

Section: Induction Of Hsp22mentioning

confidence: 99%

“…In studies with MCF-7 breast cancer cells, this protein was found to be induced by E 2 and initially designated ''estrogen-regulated 24K protein'' (Edwards et al 1980;Ciocca et al 1984). This protein was reported to be involved in growth and differentiation of hormonally controlled tissues such as breast and endometrium (Ciocca et al 1989).…”

Section: Introductionmentioning

confidence: 99%

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Induction of Hsp22 (HspB8) by estrogen and the metalloestrogen cadmium in estrogen receptor– positive breast cancer cells

et al. 2007

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Estrogen (E 2 ) plays a critical role in the etiology and progression of human breast cancer. The estrogenic response is complex and not completely understood, including in terms of the involved responsive genes. Here we show that Hsp22 (synonyms: HspB8, E2IG1, H11), a member of the small heat shock protein (sHSP) superfamily, was induced by E 2 in estrogen receptor-positive MCF-7 breast cancer cells, resulting in an elevated Hsp22 protein level, whereas it was not induced in estrogen receptor-negative MDA-MB-231 cells. This induction was prevented by the pure anti-estrogen ICI182780 (faslodex, fulvestrant), whereas tamoxifen, a substance with mixed estrogenic and antiestrogenic properties, had no major inhibitory effect on this induction, nor did it induce Hsp22 on its own. Cadmium (Cd) is an environmental pollutant with estrogenic properties (metalloestrogen) that has been implicated in breast cancer. Treatment of MCF-7 cells with Cd also resulted in induction of Hsp22, and this induction was also inhibited by ICI182780. In live MCF-7 cells, Hsp22 interacted at the level of dimers with Hsp27, a related sHSP, as was shown by quantitative fluorescence resonance energy transfer measurements. In cytosolic extracts of MCF-7 cells, most of the E 2 -and Cd-induced Hsp22 was incorporated into high-molecular mass complexes. In part, Hsp22 and Hsp27 were components of distinct populations of these complexes. Finally, candidate elements in the Hsp22 promoter were identified by sequence analysis that could account for the induction of Hsp22 by E 2 and Cd. Taken together, Hsp22 induction represents a new aspect of the estrogenic response with potential significance for the biology of estrogen receptorpositive breast cancer cells.

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Section: Discussionmentioning

confidence: 99%

“…Hsp27 was also reported to be induced by E 2 , although on a lesser scale (Edwards et al 1980). We therefore included Hsp27 in this analysis.…”

Section: Induction Of Hsp22mentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Induction of Hsp22 (HspB8) by estrogen and the metalloestrogen cadmium in estrogen receptor– positive breast cancer cells

et al. 2007

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“…In mammals, these comprise hsp's-100, -90, -70, -60 and the small molecular weight proteins (Coffer et al, 1985). The oestrogen-regulated protein known as hsp-27 was initially identified in breast epithelial MCF-7 cells (Edwards et al, 1980;Conroy and Latchman, 1996). The gene for this protein is known to produce a number of splice variants from a single gene, encoding at least 13 different protein isoforms.…”

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confidence: 99%

Increased risk of malignant progression in benign proliferating breast lesions defined by expression of heat shock protein 27

et al. 2004

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“…Women patients express fourfold higher levels of Hsp27 mRNA in their oesophagus than men, but comparable differences in the level of Hsp27 protein were not observed. Because Hsp27 was first identified in breast tumours (MCF-7) as an oestrogen-responsive protein (Edwards et al, 1980), we examined the response of adenocarcinoma cell lines and an oesophageal epithelial cell line (HET-1A) to both heat shock and oestradiol treatment. Hsp27 protein was inducible by heat shock in BarrettÕs adenocarcinoma cell lines and in HET-1A, but not by oestradiol.…”

mentioning

confidence: 99%

Differential expression of Hsp27 in normal oesophagus, Barrett’s metaplasia and oesophageal adenocarcinomas

et al. 1999

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SummaryThe protein expression patterns of normal, metaplastic and malignant oesophageal tissues were analysed by two-dimensional polyacrylamide gel electrophoresis (2D-PAGE) to identify changes associated with Barrett's metaplasia and transformation to oesophageal adenocarcinoma. Heat-shock protein 27 (Hsp27), a small heat-shock protein which is protective against cytotoxic stresses, was abundant in normal oesophagus. However, Hsp27 expression was markedly lower in Barrett's metaplasia and oesophageal adenocarcinomas. This was confirmed by immunohistochemical analysis. Hsp27 protein was most highly expressed in the upper layers of squamous epithelium and exhibited a pattern of expression that corresponded with the degree of squamous maturation. Northern and Southern analysis demonstrated Hsp27 to be regulated at the level of mRNA transcription or abundance. Normal oesophageal tissues were examined for gender differences in Hsp27 expression. Women expressed fourfold higher levels of Hsp27 mRNA, however, this difference was not appreciable in protein expression. Hsp27 protein was inducible by heat shock in Barrett's adenocarcinoma cell lines and an immortalized oesophageal epithelial cell line (HET-1A), but not by oestradiol. These results demonstrate abundant constitutive expression of the stress-response protein Hsp27 in the normal oesophagus, and suggest that low-level expression in Barrett's metaplasia may be one factor which may influence susceptibility to oesophageal adenocarcinoma development.

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Estrogen induced synthesis of specific proteins in human breast cancer cells

Cited by 105 publications

References 11 publications

Induction of Hsp22 (HspB8) by estrogen and the metalloestrogen cadmium in estrogen receptor– positive breast cancer cells

Induction of Hsp22 (HspB8) by estrogen and the metalloestrogen cadmium in estrogen receptor– positive breast cancer cells

Increased risk of malignant progression in benign proliferating breast lesions defined by expression of heat shock protein 27

Differential expression of Hsp27 in normal oesophagus, Barrett’s metaplasia and oesophageal adenocarcinomas

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