scholarly journals Coexpression of EphA10 and Gli3 promotes breast cancer cell proliferation, invasion and migration

2021 ◽  
pp. jim-2021-001836
Author(s):  
Jing Peng ◽  
Danhua Zhang
Keyword(s):  
Breast Cancer ◽  
Cell Proliferation ◽  
Mammary Epithelial Cells ◽  
Clinicopathological Characteristics ◽  
Normal Breast ◽  
Mammary Epithelial ◽  
Invasion And Migration ◽  
Human Mammary Epithelial ◽  
And Migration ◽  
Invasive Carcinomas

This study investigated the influences of EphA10 and Gli3 on breast cancer (BC) cell proliferation, invasion and migration. Immunohistochemistry was used to reveal the expressions of EphA10 and Gli3 in 18 intraductal carcinomas, 124 invasive carcinomas, 50 paracancerous tissues (2 cm away from the tumor, when possible or available), 50 lobular hyperplastic tissues and 30 normal breast tissues. qRT-PCR and Western blotting were applied to detect the expressions of EphA10 and Gli3 in invasive BC cells (MDA-MB-231, BT20 and Hs578T) and normal human mammary epithelial cells (MCF10A). MDA-MB-231 and BT20 cells were transfected with sh-EphA10, sh-Gli3 or sh-EphA10+sh-Gli3. CCK-8 was used to test the proliferation of transfected MDA-MB-231 and BT20 cells. Transwell and scratch assays were used for evaluation of invasion and migration of the transfected cells. EphA10 and Gli3 were highly expressed in invasive carcinomas and invasive BC cells. The expressions of EphA10 and Gli3 were associated with the clinicopathological characteristics and poor prognosis of patients with invasive BC. Knockdown of EphA10 or Gli3 suppressed activities of BC cells. Knockdown of both EphA10 and Gli3 was more effective than knockdown of Gli3 alone. Taken together, coexpression of EphA10 and Gli3 promotes BC cell proliferation, invasion and migration.

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.

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.

Matrix-fibrinogen enhances wound closure by increasing both cell proliferation and migration

Blood ◽  
2003 ◽  
Vol 102 (12) ◽  
pp. 4035-4043 ◽  
Author(s):  
Brian J. Rybarczyk ◽  
Sarah O. Lawrence ◽  
Patricia J. Simpson-Haidaris
Keyword(s):  
Cell Proliferation ◽  
Growth Factor ◽  
Wound Repair ◽  
Wound Closure ◽  
Mammary Epithelial Cells ◽  
Dermal Fibroblasts ◽  
Mammary Epithelial ◽  
Cell Phenotype ◽  
Matrix Assembly ◽  
And Migration

AbstractFibrinogen (FBG) assembles into matrix fibrils of fibroblasts, lung and mammary epithelial cells, but not endothelial cells. Furthermore, cryptic β15-21 residues are exposed in FBG fibrils with no evidence of thrombin or plasmin proteolysis. Herein, the effects of FBG on migration and proliferation of wounded dermal fibroblasts were investigated. FBG preassembled into matrix prior to scrape-wounding induced 3H-thymidine incorporation 8-fold and shortened the time to wound closure 1.6-fold ± 0.1-fold. FBG added immediately after wounding did not enhance either response. Fibroblast growth factor-2/platelet-derived growth factor (FGF-2/PDGF) stimulated cell proliferation 2.2-fold for FGF-2 and 3.2-fold for PDGF and wound closure 1.5-fold ± 0.1-fold in the absence of matrix-FBG. Surprisingly, exogenous growth factors had negligible effect on wound closure and cell proliferation already enhanced by matrix-FBG. Matrix-FBG-enhanced wound closure required active assembly of an FBG-fibronectin matrix, engagement of αvβ3, and FBG Aα-RGDS572-575 integrin recognition sites; Aα-RGDF95-98 sites were not sufficient for matrix-FBG assembly, enhanced wound closure, or cell proliferation. Although Bβ1-42 was not necessary for matrix assembly, it was required for matrix-FBG-enhanced cell migration. These data indicate that FBG serves as an important matrix constituent in the absence of fibrin formation to enhance wound repair and implicate Bβ1-42 as a physiologic inducer of signal transduction to promote an intermediate state of cell adhesion and a migratory cell phenotype. (Blood. 2003;102:4035-4043)

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.

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