scholarly journals The Effects of Triazine Herbicides on Critical Peroxide Metabolism Gene Expression in MCF-7 and MCF-10A Cells

2020 ◽  
pp. 71-82
Author(s):  
Stephen J. DeMartini ◽  
Nicole B. DeHart ◽  
Jennifer R. Schroeder
Keyword(s):  
Gene Expression ◽  
Hydrogen Peroxide ◽  
Mammary Epithelial Cells ◽  
Human Mammary Epithelial Cell ◽  
Mammary Epithelial ◽  
Pcr Analysis ◽  
Triazine Herbicides ◽  
Human Mammary Epithelial ◽  
The Stability ◽  
Mcf 7

Aim: To identify the oxidative stress impacts of chloro-s-triazine herbicides on human mammary epithelial cell lines. Study Design: MCF-7 mammary epithelial carcinoma and MCF-10A mammary epithelial cells were treated with levels of three triazine herbicides in concentrations flanking the US FDA safe levels. Place and Duration of Study: Department of Biology, Millikin University, in January 2015 through December 2015 and January 2019 through May 2020. Methodology: We examined the oxidative effects of two triazine herbicides, atrazine and simazine, on estrogen-dependent MCF-7 mammary epithelial carcinoma cells using three different bioluminescent assay techniques. We then utilized real time PCR to analyze gene expression through RT-PCR analysis, in both MCF-7 cells and a non-cancerous cell line, MCF-10A, for both of these triazine herbicides plus the related cyanazine. Results: At all concentrations of atrazine and simazine, no statistical differences were found in the levels of oxidized glutathione or total oxidized and reduced nicotinamide adenine dinucleotides phosphates. In stark contrast, levels of hydrogen peroxide were found to be statistically different from the control at all concentrations of atrazine and simazine tested. Using an Analysis of Variance (ANOVA) we determined that within the enzymatic portion of the hydrogen peroxide pathway there were statistically significant differences in the expression of Peroxiredoxin 1 (PRDX1), Sulfiredoxin (SRXN1), and Thioredoxin (TXN). Conclusion: Exposure to triazines alters the hydrogen peroxide pathway, which in turn can greatly affect the stability of the cell milieu.

scholarly journals Gene Expression Profile in Response to Doxorubicin–Rapamycin Combined Treatment of HER-2–Overexpressing Human Mammary Epithelial Cell Lines

2011 ◽  
Vol 11 (2) ◽  
pp. 464-474 ◽  
Author(s):  
Adriana Priscila Trapé ◽  
Maria Lucia Hirata Katayama ◽  
Rosimeire Aparecida Roela ◽  
Helena Brentani ◽  
Graziela Rosa Ravacci ◽  
...  
Keyword(s):  
Gene Expression ◽  
Epithelial Cell ◽  
Gene Expression Profile ◽  
Mammary Epithelial Cell ◽  
Combined Treatment ◽  
Human Mammary Epithelial Cell ◽  
Mammary Epithelial ◽  
Epithelial Cell Lines ◽  
Human Mammary Epithelial ◽  
Her 2

Effect of the extracellular matrix on plasminogen activator isozyme activities of human mammary epithelial cells in culture

1983 ◽  
Vol 3 (6) ◽  
pp. 982-990
Author(s):  
N S Yang ◽  
C Park ◽  
C Longley ◽  
P Furmanski
Keyword(s):  
Extracellular Matrix ◽  
Epithelial Cells ◽  
Plasminogen Activator ◽  
Mammary Epithelial Cells ◽  
Mammary Epithelial ◽  
Collagen Gels ◽  
Human Mammary Epithelial Cells ◽  
Human Mammary Epithelial ◽  
Normal Human ◽  
Mcf 7

Multiple molecular forms of plasminogen activator were detected in normal human mammary epithelial cells in culture. Cells derived from (normal) breast mammoplasty specimens and grown on the surface of collagen gels exhibited three major classes of plasminogen activator isozymes (Mr = 100,000 [100K], 75,000 [75K], and 55,000 [55K]). The activity of the 100K and 75K isozymes was greatly reduced when the cells were grown on conventional tissue-culture-grade plastic surfaces. MCF-7, a human mammary carcinoma cell line, exhibited predominantly or exclusively the 55K isozyme, irrespective of the cell growth substratum. The activity of the 55K isozyme was more than twofold higher for MCF-7 cells grown on collagen gels than for cells grown on plastic. Progesterone, diethylstilbestrol, and estrogen stimulated the activity of the 55K isozyme of MCF-7 cells, but only when the cells were grown on a plastic surface. The plasminogen activator activities of the normal human mammary epithelial cells were not stimulated by these hormones, irrespective of the growth substratum. These results show that the expression of plasminogen activator isozymes by human mammary epithelial cells is subject to modulation by the extracellular matrix. Normal and malignant cells may differ in their responsiveness to these effects.

Repression of Wnt-5a impairs DDR1 phosphorylation and modifies adhesion and migration of mammary cells

2001 ◽  
Vol 114 (11) ◽  
pp. 2043-2053 ◽  
Author(s):  
Marzieh Jönsson ◽  
Tommy Andersson
Keyword(s):  
Mammary Epithelial Cells ◽  
Human Mammary Epithelial Cell ◽  
Mammary Epithelial ◽  
Epithelial Cell Line ◽  
Collagen Binding ◽  
Collagen Matrices ◽  
Endogenous Expression ◽  
Human Mammary Epithelial ◽  
Antisense Approach ◽  
And Migration

The Wnt-5a gene encodes a secreted protein that controls several normal processes during embryogenesis and development of adult tissues by as yet unknown mechanisms. Endogenous expression of Wnt-5a mRNA is known to occur in both mouse and human mammary cell lines. To investigate the biological role of Wnt-5a in the human mammary epithelial cell line HB2, we used an antisense approach to repress endogenous expression of Wnt-5a protein. We also generated a cell population that constitutively overexpresses this protein. We found that overexpression of Wnt-5a protein enhanced cell-to-collagen binding and abolished hepatocyte growth factor-stimulated migration of HB2 transfectants through collagen matrices. Conversely, repression of Wnt-5a protein led to cell scattering, impaired cell-collagen interaction and enhanced cell motility. As we were searching for modified collagen receptors in antisense cells, we discovered that the collagen-binding discoidin domain receptor 1 (DDR1) failed to undergo phosphorylation. In reciprocal experiments, phosphorylation of DDR1 was consistently enabled by expression of Wnt-5a-HA protein in non-Wnt-5a-producing MCF-7 breast cancer cells. Activation of the Wnt/β-catenin signalling pathway did not influence or mimic the Wnt-5a-mediated effect on DDR1 phosphorylation. These data demonstrate that Wnt-5a protein participates in regulation of adhesion to and migration through collagen and is also a co-factor necessary for collagen-induced activation of DDR1 receptors in mammary epithelial cells.

scholarly journals Review of: Metalloproteinase axes increase β-catenin signaling in primary mouse mammary epithelial cells lacking TIMP3

2007 ◽  
Vol 10 (8) ◽  
Author(s):  
D. S. Salomon
Keyword(s):  
Gene Expression ◽  
Epithelial Cells ◽  
Target Genes ◽  
Mammary Epithelial Cells ◽  
Mammary Epithelial ◽  
Pcr Analysis ◽  
Mrna Levels ◽  
Specific Effects ◽  
Primary Mouse ◽  
Ductal Elongation

Citation of original article:C. V. Hojilla, I. Kim, Z. Kassiri, J. E. Fat, H. Fang, R. Khokha. Journal of Cell Science 2007; 120(6): 1050–1060.Abstract of the original article:Multiple cancers exhibit mutations in β-catenin that lead to increased stability, altered localization or amplified activity. β-Catenin is situated at the junction between the cadherin-mediated cell adhesion and Wnt signaling pathways, and TIMP3 functions to alter β-catenin signaling. Here we demonstrate that primary mouse embryonic fibroblasts (MEFs) and mammary epithelial cells (MECs) deficient in Timp3 have increased β-catenin signaling. Functionally, the loss of TIMP3 exerted cell-type-specific effects, with Timp3−/− MEFs being more sensitive and Timp3−/− MECs more resistant to EGTA-induced cell detachment than the wild type. Timp3−/− MECs had higher dephosphorylated β-catenin levels and increased β-catenin transcriptional activity as measured by TCF/LEF-responsive reporter assays. Real-time PCR analysis of β-catenin target genes in MEFs and MECs showed no alteration in Myc, decreased Ccnd1 (cyclin D1) and increased Mmp7 mRNA levels upon loss of TIMP3, with the latter occurring only in epithelial cells. Recombinant TIMP3 and synthetic metalloproteinase inhibitors reverted the increase in dephosphorylated β-catenin, decrease in Ccnd1 gene expression and increase in Mmp7 gene expression. Physiologically, Timp3−/− mammary glands displayed accelerated mammary ductal elongation during pubertal morphogenesis. Gain-of-function studies using slow-release TIMP-containing pellets revealed distinct effects of individual TIMPs on ductal morphogenesis. Recombinant TIMP1, TIMP3 and TIMP4 inhibited ductal elongation whereas TIMP2 promoted this process.

Breast Cancer Diagnosed by MRI Using Mesoporous TiO2-Coated (Fe3O4) Nanoparticles

2020 ◽  
Vol 20 (10) ◽  
pp. 6561-6567 ◽  
Author(s):  
Bo Zheng ◽  
Minghua Xue ◽  
Xinyi Zhang ◽  
Ning Tian ◽  
Dongmei Wang
Keyword(s):  
Breast Cancer ◽  
Glucose Metabolism ◽  
Cancer Cells ◽  
Mammary Epithelial Cells ◽  
Glucose Consumption ◽  
Mammary Epithelial ◽  
Blue Staining ◽  
Human Mammary Epithelial ◽  
Significant Uptake ◽  
Mcf 7

Objective: This study aimed to determine the effects of dimer captosuccinic acid-coated Fe3O4 (super paramagnetic) nanoparticles (NP) on 2-deoxy-d-glucose in targeted cancer cells with high rates of glucose metabolism. Methods: We prepared Fe3O4@DMSA NP and 2-DG-conjugated Fe3O4@DMSA NP, γ-FE, O, and @DMSA-DG NP. Glucose consumption in MDA-MB-231 and MCF-7 breast cancer cells was determined using γ-Fe2O3@DMSA NP or Fe3O4@DMSA-DG NP, and absorption was tested using Prussian blue staining, ultraviolet colorimetry, and magnetic resonance imaging. Results: Glucose consumption was the highest in MDA-MB-231, and the lowest in human mammary epithelial cells (HMEPiC). The significant uptake of Fe2O3@DMSA-DG NP by MDA-MB-231 and MCF-7 cells within two hours was inhibited by glucose. The uptake of Fe3O4@DMSA-DG NP was significantly higher in MDA-MB-231 than in MCF-7 cells, whereas Fe3O4@DMSA NP was not obviously uptaken by either cell line. Absorption was also not evident in HMEPiC incubated with Fe3O4@DMSA-DG NP and Fe3O4@DMSA NP. Conclusions: The tumor targeting efficacy of 2-DG coated Fe3O4@DMSA NP was improved over Fe3O4,@DMSA NP in cancer cells with high rates of glucose metabolism.

scholarly journals Leptin Expression in Human Mammary Epithelial Cells and Breast Milk

1998 ◽  
Vol 83 (5) ◽  
pp. 1810-1810 ◽  
Author(s):  
Susan M. Smith-Kirwin ◽  
Darlise M. O’Connor ◽  
Jennifer Johnston ◽  
Elizabeth de Lancy ◽  
Sandra G. Hassink ◽  
...  
Keyword(s):  
Mammary Gland ◽  
Breast Milk ◽  
Epithelial Cells ◽  
Milk Fat ◽  
Mammary Epithelial Cells ◽  
Skim Milk ◽  
Mammary Epithelial ◽  
Pcr Analysis ◽  
Human Mammary Epithelial Cells ◽  
Human Mammary Epithelial

Leptin has recently been shown to be produced by the human placenta and potentially plays a role in fetal and neonatal growth. Many functions of the placenta are replaced by the mammary gland in terms of providing critical growth factors for the newborn. In this study, we show that leptin is produced by human mammary epithelial cells as revealed by RT/PCR analysis of total RNA from mammary gland and immunohistochemical staining of breast tissue, cultured mammary epithelial cells, and secretory epithelial cells present in human milk. We also verify that immunoreactive leptin is present in whole milk at 30- to 150-fold higher concentrations than skim milk. We propose that leptin is secreted by mammary epithelial cells in milk fat globules, which partition into the lipid portion of breast milk.

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