Effects of Daidzein or Genistein on Proliferation and Antioxidation of Mammary Epithelial Cell of Dairy Cow In Vitro

2011 ◽  
Vol 343-344 ◽  
pp. 649-654
Author(s):  
Chun Long Liu ◽  
Zhong Qiu Li ◽  
Xing Jun Feng
Keyword(s):  
Epithelial Cell ◽  
Epithelial Cells ◽  
Dairy Cow ◽  
Mammary Epithelial Cell ◽  
Mammary Epithelial Cells ◽  
Mammary Epithelial ◽  
Logarithmic Growth Phase ◽  
Mda Content ◽  
Mammary Epithelial Cell Proliferation

Effects of Daidzein or Genistein on the proliferation and antioxidation of mammary epithelial cells of dairy cow were investigated in vitro. 10 groups were assigned including blank control, estradiol (E2) group(10 ng/mL), different concentrations of Daidzein (1, 10, 100, 1 000 ng/mL) and Genistein (1, 10, 100, 1 000 ng/mL) groups. The MMT method was used to determine the proliferation effect of Genistein or Daidzein, and the results showed that Genistein at the concentration of 10 and 100 ng/mL, and Daidzein at the concentration of 100 and 1000 ng/mL significantly improved dairy cow mammary epithelial cell proliferation (P<0.05) , while significantly weaker than E2 group(P<0.05). In the antioxidation experiment, the T-SOD and GSH-PX activity, MDA and NO content of the mammary epithelial cells at the logarithmic growth phase treated with Daidzein or Genistein for 24 h were measured and the results showed that 100, 1000 ng/mL Daidzein, and 100, 1000 ng/ mL Genistein significantly increased the T-SOD activities and decreased MDA content (P<0.05).1 000 ng/ mL Daidzein and 100, 1 000 ng/mL Genistein significantly increased the GSH-PX activites (P<0.05). The results showed that proper levels of daidzein and genistein can improv the proliferation and antioxidation function of mammary epithelial cell of dairy cows.

scholarly journals A Dual Role for Oncostatin M Signaling in the Differentiation and Death of Mammary Epithelial Cells in Vivo

2008 ◽  
Vol 22 (12) ◽  
pp. 2677-2688 ◽  
Author(s):  
Paul G. Tiffen ◽  
Nader Omidvar ◽  
Nuria Marquez-Almuina ◽  
Dawn Croston ◽  
Christine J. Watson ◽  
...  
Keyword(s):  
Gene Expression ◽  
Epithelial Cell ◽  
Epithelial Cells ◽  
Mammary Epithelial Cells ◽  
Mammary Epithelial ◽  
Oncostatin M ◽  
Specific Gene ◽  
Mammary Involution

Abstract Recent studies in breast cancer cell lines have shown that oncostatin M (OSM) not only inhibits proliferation but also promotes cell detachment and enhances cell motility. In this study, we have looked at the role of OSM signaling in nontransformed mouse mammary epithelial cells in vitro using the KIM-2 mammary epithelial cell line and in vivo using OSM receptor (OSMR)-deficient mice. OSM and its receptor were up-regulated approximately 2 d after the onset of postlactational mammary regression, in response to leukemia inhibitory factor (LIF)-induced signal transducer and activator of transcription-3 (STAT3). This resulted in sustained STAT3 activity, increased epithelial apoptosis, and enhanced clearance of epithelial structures during the remodeling phase of mammary involution. Concurrently, OSM signaling precipitated the dephosphorylation of STAT5 and repressed expression of the milk protein genes β-casein and whey acidic protein (WAP). Similarly, during pregnancy, OSM signaling suppressed β-casein and WAP gene expression. In vitro, OSM but not LIF persistently down-regulated phosphorylated (p)-STAT5, even in the continued presence of prolactin. OSM also promoted the expression of metalloproteinases MMP3, MMP12, and MMP14, which, in vitro, were responsible for OSM-specific apoptosis. Thus, the sequential activation of IL-6-related cytokines during mammary involution culminates in an OSM-dependent repression of epithelial-specific gene expression and the potentiation of epithelial cell extinction mediated, at least in part, by the reciprocal regulation of p-STAT5 and p-STAT3.

Vaccaria segetalisactivates cellular lactogenesis signaling pathway of dairy cow mammary epithelial cells in vitro

2015 ◽  
Vol 49 (2) ◽  
pp. 199
Author(s):  
L.I. Nan ◽  
Wei Cheng-jie ◽  
Meng Hai-yang ◽  
Sun Xiao-xu ◽  
Wang Li-na ◽  
...  
Keyword(s):  
Epithelial Cells ◽  
Signaling Pathway ◽  
Dairy Cow ◽  
Mammary Epithelial Cells ◽  
Mammary Epithelial

Overexpression of Mos, Ras, Src, and Fos inhibits mouse mammary epithelial cell differentiation

1992 ◽  
Vol 12 (9) ◽  
pp. 3890-3902
Author(s):  
B Jehn ◽  
E Costello ◽  
A Marti ◽  
N Keon ◽  
R Deane ◽  
...  
Keyword(s):  
Estrogen Receptor ◽  
Epithelial Cell ◽  
Epithelial Cells ◽  
Mammary Epithelial Cell ◽  
Mammary Epithelial Cells ◽  
Binding Activity ◽  
Mammary Epithelial ◽  
Dna Binding Activity ◽  
Beta Casein ◽  
Lactogenic Hormones

Mammary epithelial cells terminally differentiate in response to lactogenic hormones. We present evidence that oncoprotein overexpression is incompatible with this hormone-inducible differentiation and results in striking cellular morphological changes. In mammary epithelial cells in culture, lactogenic hormones (glucocorticoid and prolactin) activated a transfected beta-casein promoter and endogenous beta-casein gene expression. This response to lactogenic hormone treatment was paralleled by a decrease in cellular AP-1 DNA-binding activity. Expression of the mos, ras, or src (but not myc) oncogene blocked the activation of the beta-casein promoter induced by the lactogenic hormones and was associated with the maintenance of high levels of AP-1. Mos expression also increased c-fos and c-jun mRNA levels. Overexpression of Fos and Jun from transiently transfected constructs resulted in a functional inhibition of the glucocorticoid receptor in these mouse mammary epithelial cells. This finding clearly suggests that glucocorticoid receptor inhibition arising from oncogene expression will contribute to the block in hormonally induced mammary epithelial cell differentiation. Expression of Src resulted in the loss of the normal organization and morphological phenotype of mammary epithelial cells in the epithelial/fibroblastic line IM-2. Activation of a conditional c-fos/estrogen receptor gene encoding an estrogen-dependent Fos/estrogen receptor fusion protein also morphologically transformed mammary epithelial cells and inhibited initiation of mammary epithelial differentiation-associated expression of the beta-casein and WDNM 1 genes. In response to estrogen treatment, the cells displayed a high level of AP-1 DNA-binding activity. Our results demonstrate that high cellular AP-1 levels contribute to blocking the ability of mammary epithelial cells in culture to respond to lactogenic hormones. This and other studies indicate that the oncogene products Mos, Ras, and Src exert their effects, at least in part, by stimulating cellular Fos and probably cellular Jun activity.

Overexpression of the integrin-linked kinase mesenchymally transforms mammary epithelial cells

2001 ◽  
Vol 114 (6) ◽  
pp. 1125-1136 ◽  
Author(s):  
A. Somasiri ◽  
A. Howarth ◽  
D. Goswami ◽  
S. Dedhar ◽  
C.D. Roskelley
Keyword(s):  
Epithelial Cell ◽  
Epithelial Cells ◽  
Mammary Epithelial Cell ◽  
Mammary Epithelial Cells ◽  
Mammary Epithelial ◽  
Cell Morphogenesis ◽  
Wild Type ◽  
Integrin Linked Kinase ◽  
E Cadherin ◽  
Cell Cell

Signals generated by the interaction of (β)1 integrins with laminin in the basement membrane contribute to mammary epithelial cell morphogenesis and differentiation. The integrin-linked kinase (ILK) is one of the signaling moieties that associates with the cytoplasmic domain of (β)1 integrin subunits with some specificity. Forced expression of a dominant negative, kinase-dead form of ILK subtly altered mouse mammary epithelial cell morphogenesis but it did not prevent differentiative milk protein expression. In contrast, forced overexpression of wild-type ILK strongly inhibited both morphogenesis and differentiation. Overexpression of wild-type ILK also caused the cells to lose the cell-cell adhesion molecule E-cadherin, become invasive, reorganize cortical actin into cytoplasmic stress fibers, and switch from an epithelial cytokeratin to a mesenchymal vimentin intermediate filament phenotype. Forced expression of E-cadherin in the latter mesenchymal cells rescued epithelial cytokeratin expression and it partially restored the ability of the cells to differentiate and undergo morphogenesis. These data demonstrate that ILK, which responds to interactions between cells and the extracellular matrix, induces a mesenchymal transformation in mammary epithelial cells, at least in part, by disrupting cell-cell junctions.

scholarly journals Endocytosis and intracellular transport of transferrin across the lactating rabbit mammary epithelial cell.

1992 ◽  
Vol 40 (10) ◽  
pp. 1501-1510 ◽  
Author(s):  
T Seddiki ◽  
S Delpal ◽  
M Ollivier-Bousquet
Keyword(s):  
Epithelial Cell ◽  
Epithelial Cells ◽  
Mammary Epithelial Cell ◽  
Intracellular Transport ◽  
Mammary Epithelial Cells ◽  
Basal Membrane ◽  
Mammary Epithelial ◽  
Casein Micelles ◽  
Human Transferrin ◽  
Rabbit Milk

To study the transcytosis and segregation of ligand in the mammary epithelial cell, endocytosis and intracellular transit of human blood transferrin were followed in lactating rabbit mammary epithelial cells. Human transferrin labeled with biotin added to an incubation medium was bound to the basal membrane of mammary epithelial cells and carried across the cell to the lumen of the acini within 5-60 min. At the same time, biotinylated human transferrin accumulated at the apex of the cell. After incubation with human transferrin labeled with colloidal gold, label was detected inside endosome-like structures, vesicles and saccules of the Golgi apparatus, and inside the lumen within 2-5 min. A significant label accumulated at the apex of the cell after 30-60 min. Biotin labeling did not modify the time of transit of human transferrin, as attested by comparison with the time of transit of native transferrin. Human transferrin was never detected inside vesicles containing casein micelles. In contrast, rabbit milk transferrin was immunocytochemically detected inside vesicles containing casein micelles. These results indicate that transcytosis of human transferrin follows a pathway different from vesicles that carry casein micelles.

scholarly journals In Vitro Culture and Characterization of a Mammary Epithelial Cell Line from Chinese Holstein Dairy Cow

PLoS ONE ◽  
2009 ◽  
Vol 4 (11) ◽  
pp. e7636 ◽  
Author(s):  
Han Hu ◽  
Jiaqi Wang ◽  
Dengpan Bu ◽  
Hongyang Wei ◽  
Linyun Zhou ◽  
...  
Keyword(s):  
Epithelial Cell ◽  
In Vitro Culture ◽  
Dairy Cow ◽  
Mammary Epithelial Cell ◽  
Mammary Epithelial ◽  
Epithelial Cell Line ◽  
Mammary Epithelial Cell Line ◽  
Holstein Dairy Cow

Zip3 plays a major role in zinc uptake into mammary epithelial cells and is regulated by prolactin

2005 ◽  
Vol 288 (5) ◽  
pp. C1042-C1047 ◽  
Author(s):  
Shannon L. Kelleher ◽  
Bo Lönnerdal
Keyword(s):  
Mammary Gland ◽  
Epithelial Cell ◽  
Epithelial Cells ◽  
Mammary Epithelial Cell ◽  
Mammary Epithelial Cells ◽  
Cell Model ◽  
Mammary Epithelial ◽  
Maternal Circulation ◽  
Physiological Explanation ◽  
Secretory Phenotype

During lactation, a substantial amount of Zn2+ is transferred by the mammary gland from the maternal circulation into milk; thus secretory mammary epithelial cells must tightly regulate Zn2+ transport to ensure optimal Zn2+ transfer to the suckling neonate. To date, six Zn2+ import proteins (Zip1–6) have been identified; however, Zip3 expression is restricted to tissues with unique requirements for Zn2+, such as the mammary gland, which suggests that it may play a specialized role in this tissue. In the present study, we have used a unique mammary epithelial cell model (HC11) to characterize the role of Zip3 in mammary epithelial cell Zn2+ transport. Confocal microscopy demonstrated that Zip3 is localized to the cell surface in mammary epithelial cells and transiently relocalized to an intracellular compartment in cells with a secretory phenotype. Total 65Zn transport was higher in secreting cells, while gene silencing of Zip3 decreased 65Zn uptake into mammary epithelial cells, particularly in those with a secretory phenotype. Finally, reduced expression of Zip3 ultimately resulted in cell death, indicating that mammary epithelial cells have a unique requirement for Zip3-mediated Zn2+ import, which may reflect the unique requirement for Zn2+ of this highly specialized cell type and thus provides a physiological explanation for the restricted tissue distribution of this Zn2+ importer.

scholarly journals Repression of p63 and induction of EMT by mutant Ras in mammary epithelial cells

2016 ◽  
Vol 113 (41) ◽  
pp. E6107-E6116 ◽  
Author(s):  
Kathryn E. Yoh ◽  
Kausik Regunath ◽  
Asja Guzman ◽  
Seung-Min Lee ◽  
Neil T. Pfister ◽  
...  
Keyword(s):  
Epithelial Cell ◽  
Epithelial Cells ◽  
Epithelial To Mesenchymal Transition ◽  
Mammary Epithelial Cells ◽  
Collagen Gel ◽  
Mammary Epithelial ◽  
Transcriptional Level ◽  
Mesenchymal Transition ◽  
Related Transcription Factor

The p53-related transcription factor p63 is required for maintenance of epithelial cell differentiation. We found that activated forms of the Harvey Rat Sarcoma Virus GTPase (H-RAS) and phosphatidylinositol-4,5-bisphosphate 3-kinase catalytic subunit alpha (PIK3CA) oncogenes strongly repress expression of ∆Np63α, the predominant p63 isoform in basal mammary epithelial cells. This regulation occurs at the transcriptional level, and a short region of the ∆Np63 promoter is sufficient for repression induced by H-RasV12. The suppression of ∆Np63α expression by these oncogenes concomitantly leads to an epithelial-to-mesenchymal transition (EMT). In addition, the depletion of ∆Np63α alone is sufficient to induce EMT. Both H-RasV12 expression and ∆Np63α depletion induce individual cell invasion in a 3D collagen gel in vitro system, thereby demonstrating how Ras can drive the mammary epithelial cell state toward greater invasive ability. Together, these results suggest a pathway by which RAS and PIK3CA oncogenes induce EMT through regulation of ∆Np63α.

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