Sequence of the pS2 mRNA induced by estrogen in the human breast cancer cell line MCF-7

Jakowlew, Sonia B.; Breathnach, Richard; Jeltsch, Jean‐Marc; Masiakowski, Piotr; Chambon, Pierre

doi:10.1093/nar/12.6.2861

Cited by 275 publications

(144 citation statements)

References 49 publications

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“…crosslinked. Membranes were prehybridized and hybridized in aqueous bu er (56SSC, 56Denhardt's solution, 20 mM sodium phosphate pH 7, 1 mg/ml torula RNA (Sigma) and 1% sodium dodecyl sulphate (SDS) and probed with the following labelled cDNA fragments: EGFR (Ullrich et al, 1984), ERBB2 , ERBB3 (Plowman et al, 1990), ERBB4 (Plowman et al, 1993a), pS2 (Jakowlew et al, 1984) and rat glyceraldehyde phosphate dehydrogenase (GAPDH) (Tso et al, 1985). Membranes were washed to 0.56SSC+0.1% SDS at 658C and autoradiographed at 7758C.…”

Section: Northern Blotsmentioning

confidence: 99%

An intron 1 enhancer element mediates oestrogen-induced suppression of ERBB2 expression

Bates

Hurst

1997

Oncogene

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Overexpression of the ERBB2 gene in human breast cancer is associated with a poor prognosis and resistance to hormonal treatment and chemotherapy. Oestrogen receptor (ER) positive tumour-derived cell lines are known to express relatively low levels of ERBB2 protein under oestrogenic conditions, but markedly higher levels following withdrawal of oestrogens or administration of tamoxifen. Expression of the closely related ERBB3 gene, which co-operates with ERBB2 in cellular transformation, is now shown to respond to oestrogenic manipulation in a similar way, both responses being mediated largely by transcriptional changes. Six previously undescribed DNase I hypersensitive sites occur within the ®rst intron of ERBB2 in cells that overexpress the gene. A 409 base pair DNA fragment containing one of these sites conferred ER dependent oestrogen inhibition on the ERBB2 promoter in two types of transient transfection assay. DNase I footprinting revealed four separate transcription factor binding sites within this fragment consistent with a role as a transcriptional enhancer. These ®ndings implicate intron 1 sequences in the control of ERBB2 expression for the ®rst time and demonstrate that one site within this region is involved in mediating the transcriptional response to oestrogens. Additionally, there is likely to be synergism between ERBB2 and ERBB3 signalling when both are overexpressed in response to oestrogen inhibition, thereby driving transformed cell behaviour.

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Section: Northern Blotsmentioning

confidence: 99%

An intron 1 enhancer element mediates oestrogen-induced suppression of ERBB2 expression

Bates

Hurst

1997

Oncogene

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Section: The Ps2 Peptidementioning

confidence: 99%

“…The pS2 gene has been cloned by two groups [ 15,161. The nucleotide sequence of a pS2 full-length cDNA encoded a peptide of 84 amino acid residues out of which 26 or 21 residues represented a putative signal peptide corresponding to a mature pS2 peptide of 58 or 63 residues [15]. By the use of an antibody raised against a synthetic peptide corresponding to a 3 1 amino acid residue sequence from the C-terminal end of the predicted pS2 peptide, it has been possible to immuno-precipitate the pS2 peptide from the culture media of MCF-7 cells [ 171.…”

Section: The Ps2 Peptidementioning

confidence: 99%

“…1. Alignment of the amino acid sequences for the human breast cancer associated pS2 peptide [15,16,18,19], porcine pancreatic spasmolytic polypeptide domain I and II [25,26], and the frog skin peptides spasmolysin I and II [35]. It should be noted that Gln-1 1 of PSP-domain I has been deleted in order to obtain exact alignment of cysteine residues.…”

Section: Pancreatic Spasmolytic Polypeptidementioning

confidence: 99%

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A new family of growth factor‐like peptides ‘Trefoil’ disulphide loop structures as a common feature in breast cancer associated peptide (pS2), pancreatic spasmolytic polypeptide (PSP), and frog skin peptides (spasmolysins)

1989

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A new family of growth factor-like peptides 'Trefoil' disulphide loop structures as a common feature in breast cancer associated peptide (pS2), pancreatic spasmolytic polypeptide (PSP), and frog skin peptides (spasmolysins) Four peptides present in completely different biological sources have been shown to exhibit a large degree of structural similarity. The peptides include: (i) a 60 amino acid residue breast cancer associated pS2 peptide isolated from human gastric juice and the culture media of the human breast cancer cell line MCF-7; (ii) a 106 amino acid residue pancreatic spasmolytic polypeptide (PSP) isolated from porcine pancreas and pancreatic juice; and (iii) a 49 and 50 amino acid residue peptide predicted from a cDNA isolated from the skin of the frog, Xenopus luevis. These peptides are characterized by having one (pS2 and the frog peptides) or two (PSP) domains of a highly conserved 38-39 amino acid residue consensus sequence not found in any other known peptides or proteins. The domain sequences contain 6 cysteine residues in nearly the same positions and it is suggested that these 6 residues are linked by 3 disulphide bonds to form a characteristic 'trefoil' disulphide loop structure common in all four peptides. From the sources of which the peptides have been isolated and from experiments showing that PSP has a growth factor stimulatory effect on MCF-7 cells, it is further suggested that these peptides may represent members of a new family of growth factors.Amino acid sequence comparison; Domain structure; Disuhide bond; Receptor binding

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“…Plasmids containing inserts of ER and pS2 coding sequences were kindly provided by P. Chambon [16,17]. The plasmid recombinant for the erbB2 gene was constructed by T. Yamamoto [IS] and kindly provided by Y. Shilo.…”

Section: Plasmidsmentioning

confidence: 99%

Expression of genes coding for pS2, c‐erbB2, estrogen receptor and the H23 breast tumor‐associated antigen

et al. 1990

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Expression of the gene coding for a new breast tumor-associated antigen, H23, was compared to expression of genes coding for pS2, c-erbB2 and estrogen receptor (ER). Comparison involved mRNA expression in normal and malignant breast tissues as well as in non-breast tumors. Results obtained by RNA dot blot and Northern hybridizations showed that expression of the H23 antigen coding gene is a discriminatory marker in human breast cancer. It is expressed in 92% of breast tumors whereas 69%, 62% and 56% of breast tumors demonstrate significant mRNA levels of c-erbB2, ER and pS2, respectively. Non-malignant or normal breast tissue expresses much lower levels of the H23 antigen mRNA. From the comparative analysis presented here it is concluded that the gene coding for H23 antigen furnishes a most useful marker for human breast cancer.Gene expression; Breast tumor antigen H23; Breast tumor antigen pS2; Oncogene erbB2; Estrogen receptor; Breast cancer

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Sequence of the pS2 mRNA induced by estrogen in the human breast cancer cell line MCF-7

Cited by 275 publications

References 49 publications

An intron 1 enhancer element mediates oestrogen-induced suppression of ERBB2 expression

An intron 1 enhancer element mediates oestrogen-induced suppression of ERBB2 expression

A new family of growth factor‐like peptides ‘Trefoil’ disulphide loop structures as a common feature in breast cancer associated peptide (pS2), pancreatic spasmolytic polypeptide (PSP), and frog skin peptides (spasmolysins)

Expression of genes coding for pS2, c‐erbB2, estrogen receptor and the H23 breast tumor‐associated antigen

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