Isolation and properties of cell lines from the metastasising rat mammary tumour SMT-2A

Ps, Rudland; Dj, Dunnington; Kim, U; Gusterson, B A; O'Hare, MJ; Monaghan, Paul

doi:10.1038/bjc.1989.182

Cited by 10 publications

(11 citation statements)

References 21 publications

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“…However, MCF-7 cells when exposed to high levels of oestrogens which induce increased levels of AGR2 (Liu et al, 2005) assume a more aggressive phenotype in vitro and can form tumours and metastases in nu nu mice in vivo (Clarke et al, 1994;Kern et al, 1994). Moreover, the immunodeficient rodent is a poor model for breast cancer metastasis, since T-celldepleted rats fail to allow the formation of tumours and metastases from a rat cell line that is highly metastatic in the same immunecompetent intact rats (Rudland et al, 1989).…”

Section: Discussionmentioning

confidence: 99%

Significance of the metastasis-inducing protein AGR2 for outcome in hormonally treated breast cancer patients

et al. 2006

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The anterior gradient protein-2 (AGR2) is inducible by oestrogen and itself can induce metastasis in a rat model for breast cancer. Here, a rabbit antibody to recombinant human AGR2 was used to assess its prognostic significance in a retrospective cohort of 351 breast cancer patients treated by adjuvant hormonal therapy. The antibody stains 66% of breast carcinomas to varying degrees. The percentage of positive carcinoma cells in tumours directly correlates with the level of AGR2 mRNA (Spearman's rank correlation, P ¼ 0.0007) and protein (linear regression analysis r 2 ¼ 0.95, P ¼ 0.0002). There is a significant association of staining of carcinomas for AGR2 with oestrogen receptor a (ERa) staining and with low histological grade (both Fisher's Exact test Po0.0001). In the ERapositive cases, but not the ERa-negative cases, when subdivided into the separate staining classes for AGR2, there is a significantly progressive decrease in patient survival with increased staining (log rank test, P ¼ 0.006). The significant association of staining for AGR2 with patient death over a 10-year period (log rank test P ¼ 0.007, hazard ratio ¼ 3) only becomes significant at 6 years of follow-up. This may be due to the cessation of adjuvant hormonal therapy at an earlier time, resulting in adverse re-expression of the metastasis-inducing protein AGR2.

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Section: Discussionmentioning

confidence: 99%

Significance of the metastasis-inducing protein AGR2 for outcome in hormonally treated breast cancer patients

et al. 2006

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“…Normal host muscle cell proliferation, including the proliferation of smaller myoblast-like cells which were identified by staining for myoglobin (Rudland et al, 1984), was found around the Rama 37-S100A1-and KP1-S100A1-derived tumours, but not around Rama 37V-and KP1-Rama 37-derived tumours (Figure 8). The incidence of muscle proliferation in the tumours derived from the two clones of KP1-S100A1 cells (40 and 45%) was significantly higher than in tumours derived from KP1-Rama 37 cells (0%) (P ¼ 0.02 and 0.009, respectively, Fisher Exact test).…”

Section: A4/-mentioning

confidence: 99%

“…Animals that contained no visible muscle blocks bordering the primary tumours were eliminated from the analysis of muscle invasion and muscle proliferation. For analysis of muscle proliferation, the sections containing visible muscle blocks bordering the primary tumours were immunohistochemically stained with antimyoglobin antibody (Sigma, Dorset, UK) as described previously (Rudland et al, 1984 …”

Section: Tumorigenicity and Metastasismentioning

confidence: 99%

Mutually antagonistic actions of S100A4 and S100A1 on normal and metastatic phenotypes

et al. 2004

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Increased levels of the homodimeric calcium-binding protein, S100A4, have been shown to cause a metastatic phenotype in at least three independent model systems of breast cancer and its presence in carcinoma cells has been shown to be associated with a reduction in the survival of patients suffering from a range of different cancers. S100A4 has been shown to interact in vitro with another member of the S100 family of proteins, S100A1. The purpose of the present study was to find out whether S100A1 could affect S100A4 function. Fluorescence resonance energy transfer was used to show the interaction of S100A4 and S100A1 in living cells and the binding affinities between S100A4 and S100A1 were determined using a biosensor. S100A1 reduced the S100A4 inhibition of nonmuscle myosin A self-association and phosphorylation in vitro. S100A1 reduced S100A4 induced motility and growth in soft agar and metastasis in vivo. The results show for the first time that interactions between different S100 proteins can affect cancer-related activity, and that the presence of S100A1 protein in carcinoma cells might modulate the effect of S100A4 on their metastatic abilities.

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“…Unfortunately, it is not possible to identify the transfected DNA sequences that cause metastasis, since the transfected rat sequences cannot be readily identified within the recipient rat cells. However, this approach was chosen initially so that a completely syngeneic system could be tested for genetic transferance of metastatic properties, since human and rat mammary cells and cell lines that are metastatic in their syngeneic hosts largely fail to metastasize in allo geneic, immunodeficient rodents [45], Now that the syn geneic system has been validated, we are transfecting into Rama 37 cells fragmented DNA from human mam mary cell lines isolated from metastatic primary tumors [46] and from pleural effusions [47], with similar results [B. Davies and P.S.R., unpubl. results].…”

Section: Discussionmentioning

confidence: 99%

Generation of Metastatic Variants by Transfection of a Nonmetastatic Rat Mammary Epithelial Cell Line with DNA from a Metastatic Rat Mammary Cell Line

Jamieson

Barraclough²,

Rudland³

1990

Pathobiology

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Transfection of rat mammary (Rama) 37 epithelial cells, which yield nonmetastasizing adenomas in syngeneic Wistar-Furth rats, with HindlΠ-fragmented cellular DNA and the drug-resistance plasmids pSV2, gpí or pSV2neo yields drug-resistant transformants with a frequency of 10^-4–10^-5. Transformant cell lines transfected with the following, pSV2gpt alone, pSV2gpt and Rama 37 DNA, pSV2gpt and DNA from a metastasizing cell line Rama 800 (CT set), pSVlneo and salmon sperm DNA, pSV2neø and Rama 800 DNA (C set), all yield tumors when injected subcutaneously into syngeneic rats. A few transformants obtained by cotransfection with DNA from Rama 800 cells produce metastases in lungs and/or lymph nodes. The incidence of such metastases for two transfectants, termed CT4–41 and C18P, is significant at 20 and 24%, respectively, but only half (48%) that achieved with Rama 800 cells. Reintroduction into rats of cells cultured from a metastatic tumor of CT4–41 and of C18P, and from their lung or lymph node metastases, produces either a similar incidence (20–24%) or a significantly higher (48–52%) incidence of metastasis than that of the original transfectants. Cells cultured from nonmetastatic tumors fail to produce any metastatic lesions. When [³²P]-labeled gpt or neo DNAs are hybridized to EcoRI-digested cellular DNA of the CT4–41 or C18P series of cell lines, tumors or metastases, gpt binds to one major fragment of 3,800 basepairs, and neo to two major fragments of 5,700 and 4,200 basepairs. The same cell lines produce hybridizing mRNAs of 1,500 and 1,900 bases for the CT4–41 series and 2,000–2,400 bases for the C18P series. It is suggested that transfection of DNA from the metastatic cells causes the nonmetastatic cells to become metastatic, in a genetically dominant manner, but additional steps are required for this process to become established and expressed at a level equivalent to that of the original, metastasizing donor cells.

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Isolation and properties of cell lines from the metastasising rat mammary tumour SMT-2A

Cited by 10 publications

References 21 publications

Significance of the metastasis-inducing protein AGR2 for outcome in hormonally treated breast cancer patients

Significance of the metastasis-inducing protein AGR2 for outcome in hormonally treated breast cancer patients

Mutually antagonistic actions of S100A4 and S100A1 on normal and metastatic phenotypes

Generation of Metastatic Variants by Transfection of a Nonmetastatic Rat Mammary Epithelial Cell Line with DNA from a Metastatic Rat Mammary Cell Line

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