Breast cancer markers: Comparison between sialyltransferase and human mammary epithelial antigens (HME-Ags) for the detection of human breast tumors grafted in nude mice

1985 ◽  
Vol 5 (1) ◽  
pp. 51-56 ◽  
Author(s):  
Masao Sasaki ◽  
Shirley Barber ◽  
Roberto L. Ceriani
Keyword(s):  
Breast Cancer ◽  
Nude Mice ◽  
Breast Tumors ◽  
Mammary Epithelial ◽  
Human Breast ◽  
Cancer Markers ◽  
Human Mammary Epithelial ◽  
Epithelial Antigens

scholarly journals The ETS Transcription Factor ESE-1 Transforms MCF-12A Human Mammary Epithelial Cells via a Novel Cytoplasmic Mechanism

2004 ◽  
Vol 24 (12) ◽  
pp. 5548-5564 ◽  
Author(s):  
Jason D. Prescott ◽  
Karen S. N. Koto ◽  
Meenakshi Singh ◽  
Arthur Gutierrez-Hartmann
Keyword(s):  
Breast Cancer ◽  
Transcription Factor ◽  
Epithelial Cells ◽  
Nuclear Localization ◽  
Human Breast Cancer ◽  
Mammary Epithelial Cells ◽  
Cell Transformation ◽  
Mammary Epithelial ◽  
Human Breast ◽  
Human Mammary Epithelial

ABSTRACT Several different transcription factors, including estrogen receptor, progesterone receptor, and ETS family members, have been implicated in human breast cancer, indicating that transcription factor-induced alterations in gene expression underlie mammary cell transformation. ESE-1 is an epithelium-specific ETS transcription factor that contains two distinguishing domains, a serine- and aspartic acid-rich (SAR) domain and an AT hook domain. ESE-1 is abundantly expressed in human breast cancer and trans-activates epithelium-specific gene promoters in transient transfection assays. While it has been presumed that ETS factors transform mammary epithelial cells via their nuclear transcriptional functions, here we show (i) that ESE-1 protein is cytoplasmic in human breast cancer cells; (ii) that stably expressed green fluorescent protein-ESE-1 transforms MCF-12A human mammary epithelial cells; and (iii) that the ESE-1 SAR domain, acting in the cytoplasm, is necessary and sufficient to mediate this transformation. Deletion of transcriptional regulatory or nuclear localization domains does not impair ESE-1-mediated transformation, whereas fusing the simian virus 40 T-antigen nuclear localization signal to various ESE-1 constructs, including the SAR domain alone, inhibits their transforming capacity. Finally, we show that the nuclear localization of ESE-1 protein induces apoptosis in nontransformed mammary epithelial cells via a transcription-dependent mechanism. Together, our studies reveal two distinct ESE-1 functions, apoptosis and transformation, where the ESE-1 transcription activation domain contributes to apoptosis and the SAR domain mediates transformation via a novel nonnuclear, nontranscriptional mechanism. These studies not only describe a unique ETS factor transformation mechanism but also establish a new paradigm for cell transformation in general.

scholarly journals Revealing Glycoproteins in the Secretome of MCF-7 Human Breast Cancer Cells

2015 ◽  
Vol 2015 ◽  
pp. 1-8 ◽  
Author(s):  
Aik-Aun Tan ◽  
Wai-Mei Phang ◽  
Subash C. B. Gopinath ◽  
Onn H. Hashim ◽  
Lik Voon Kiew ◽  
...  
Keyword(s):  
Breast Cancer ◽  
Breast Cancer Cells ◽  
Mammary Epithelial Cells ◽  
Cancer Cell Line ◽  
Negative Control ◽  
Mammary Epithelial ◽  
Human Breast ◽  
Human Mammary Epithelial ◽  
Alpha 1 Antitrypsin ◽  
Mcf 7

Breast cancer is one of the major issues in the field of oncology, reported with a higher prevalence rate in women worldwide. In attempt to reveal the potential biomarkers for breast cancer, the findings of differentially glycosylated haptoglobin and osteonectin in previous study have drawn our attention towards glycoproteins of secretome from the MCF-7 cancer cell line. In the present study, further analyses were performed on the medium of MCF-7 cells by subjecting it to two-dimensional analyses followed by image analysis in contrast to the medium of human mammary epithelial cells (HMEpC) as a negative control. Carboxypeptidase A4 (CPA4), alpha-1-antitrypsin (AAT), haptoglobin (HP), and HSC70 were detected in the medium of MCF-7, while only CPA4 and osteonectin (ON) were detected in HMEpC medium. In addition, CPA4 was detected as upregulated in the MCF-7 medium. Further analysis by lectin showed that CPA4, AAT, HP, and HSC70 were secreted as N-glycan in the medium of MCF-7, with HP also showing differentially N-glycosylated isoforms. For the HMEpC, only CPA4 was detected as N-glycan. No O-glycan was detected in the medium of HMEpC but MCF-7 expressed O-glycosylated CPA4 and HSC70. All these revealed that glycoproteins could be used as glycan-based biomarkers for the prognosis of breast cancer.

scholarly journals Circulating human mammary epithelial antigens in breast cancer.

1982 ◽  
Vol 79 (17) ◽  
pp. 5420-5424 ◽  
Author(s):  
R. L. Ceriani ◽  
M. Sasaki ◽  
H. Sussman ◽  
W. M. Wara ◽  
E. W. Blank
Keyword(s):  
Breast Cancer ◽  
Mammary Epithelial ◽  
Human Mammary Epithelial ◽  
Epithelial Antigens

Role of polyamines in the growth of hormone-responsive and - resistant human breast cancer cells in nude mice

1992 ◽  
Vol 66 (1) ◽  
pp. 1-9 ◽  
Author(s):  
Andrea Manni ◽  
Betty Badger ◽  
Juliann Martel ◽  
Laurence Demers
Keyword(s):  
Breast Cancer ◽  
Cancer Cells ◽  
Nude Mice ◽  
Human Breast Cancer ◽  
Breast Cancer Cells ◽  
Human Breast Cancer Cells ◽  
Human Breast

scholarly journals MEK inhibition leads to lysosome-mediated Na+/I− symporter protein degradation in human breast cancer cells

2013 ◽  
Vol 20 (2) ◽  
pp. 241-250 ◽  
Author(s):  
Zhaoxia Zhang ◽  
Sasha Beyer ◽  
Sissy M Jhiang
Keyword(s):  
Breast Cancer ◽  
Cell Surface ◽  
Human Breast Cancer ◽  
Breast Cancer Cells ◽  
Breast Tumors ◽  
Human Breast Cancer Cells ◽  
Human Breast ◽  
Iodide Uptake ◽  
Mek Inhibition ◽  
Protein Levels

The Na+/I−symporter (NIS (SLC5A5)) is a transmembrane glycoprotein that mediates active iodide uptake into thyroid follicular cells. NIS-mediated iodide uptake in thyroid cells is the basis for targeted radionuclide imaging and treatment of differentiated thyroid carcinomas and their metastases. Furthermore, NIS is expressed in many human breast tumors but not in normal non-lactating breast tissue, suggesting that NIS-mediated radionuclide uptake may also allow the imaging and targeted therapy of breast cancer. However, functional cell surface NIS expression is often low in breast cancer, making it important to uncover signaling pathways that modulate NIS expression at multiple levels, from gene transcription to posttranslational processing and cell surface trafficking. In this study, we investigated NIS regulation in breast cancer by MAPK/extracellular signal-regulated kinase (ERK) kinase (MEK) signaling, an important cell signaling pathway involved in oncogenic transformation. We found that MEK inhibition decreased NIS protein levels in all-trans retinoic acid/hydrocortisone-treated MCF-7 cells as well as human breast cancer cells expressing exogenous NIS. The decrease in NIS protein levels by MEK inhibition was not accompanied by a decrease inNISmRNA or a decrease inNISmRNA export from the nucleus to the cytoplasm. NIS protein degradation upon MEK inhibition was prevented by lysosome inhibitors but not by proteasome inhibitors. Interestingly, NIS protein level was correlated with MEK/ERK activation in human breast tumors from a tissue microarray. Taken together, MEK activation appears to play an important role in maintaining NIS protein stability in human breast cancers.

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