scholarly journals Novel insights in the molecular mechanisms of action of retinoids and their potential repercussions on breast cancer cell proliferation

2018 ◽  
Author(s):  
Ignacio Miro Estruch
Keyword(s):  
Breast Cancer ◽  
Cell Proliferation ◽  
Cancer Cell ◽  
Breast Cancer Cell ◽  
Molecular Mechanisms ◽  
Mechanisms Of Action ◽  
Cancer Cell Proliferation ◽  
Breast Cancer Cell Proliferation

Heregulin β1 promotes breast cancer cell proliferation through Rac/ERK-dependent induction of cyclin D1 and p21Cip1

2008 ◽  
Vol 410 (1) ◽  
pp. 167-175 ◽  
Author(s):  
Chengfeng Yang ◽  
Eric A. Klein ◽  
Richard K. Assoian ◽  
Marcelo G. Kazanietz
Keyword(s):  
Breast Cancer ◽  
Cell Proliferation ◽  
Cyclin D1 ◽  
Cancer Cell ◽  
Breast Cancer Cell ◽  
Molecular Mechanisms ◽  
Small Gtpase ◽  
Dominant Negative ◽  
Cancer Cell Proliferation ◽  
Breast Cancer Cell Proliferation

Accumulating evidence indicates that heregulins, EGF (epidermal growth factor)-like ligands, promote breast cancer cell proliferation and are involved in the progression of breast cancer towards an aggressive and invasive phenotype. However, there is limited information regarding the molecular mechanisms that mediate these effects. We have recently established that HRG (heregulin β1) promotes breast cancer cell proliferation and migration via cross-talk with EGFR (EGF receptor) that involves the activation of the small GTPase Rac1. In the present paper we report that Rac1 is an essential player for mediating the induction of cyclin D1 and p21Cip1 by HRG in breast cancer cells. Inhibition of Rac function by expressing either the Rac-GAP (GTPase-activating protein) β2-chimaerin or the dominant-negative Rac mutant N17Rac1, or Rac1 depletion using RNAi (RNA interference), abolished the cyclin D1 and p21Cip1 induction by HRG. Interestingly, the proliferative effect of HRG was impaired not only when the expression of Rac1 or cyclin D1 was inhibited, but also when cells were depleted of p21Cip1 using RNAi. Inhibition of EGFR, PI3K (phosphoinositide 3-kinase; kinases required for Rac activation by HRG) or MEK [MAPK (mitogen-activated protein kinase)/ERK (extracellular-signal-regulated kinase) kinase] also blocked the up-regulation of cyclin D1 and p21Cip1 by HRG. In addition, we found that HRG activates NF-κB (nuclear factor κB) in a Rac1- and MEK-dependent fashion, and inhibition of NF-κB abrogates cyclin D1/p21Cip1 induction and proliferation by HRG. Taken together, these findings establish a central role for Rac1 in the control of HRG-induced breast cancer cell-cycle progression and proliferation through up-regulating the expression of cyclin D1 and p21Cip1.

scholarly journals Emodin and Aloe-Emodin Suppress Breast Cancer Cell Proliferation through ERαInhibition

2013 ◽  
Vol 2013 ◽  
pp. 1-12 ◽  
Author(s):  
Pao-Hsuan Huang ◽  
Chih-Yang Huang ◽  
Mei-Chih Chen ◽  
Yueh-Tsung Lee ◽  
Chia-Herng Yue ◽  
...  
Keyword(s):  
Breast Cancer ◽  
Cell Proliferation ◽  
Cancer Cell ◽  
Breast Cancer Cell ◽  
Transcriptional Activation ◽  
Molecular Mechanisms ◽  
Estrogenic Activity ◽  
Cancer Cell Proliferation ◽  
Breast Cancer Cell Proliferation ◽  
Aloe Emodin

The anthraquinones emodin and aloe-emodin are abundant in rhubarb. Several lines of evidence indicate that emodin and aloe-emodin have estrogenic activity as phytoestrogens. However, their effects on estrogen receptorα(ERα) activation and breast cancer cell growth remain controversial. The goal of this study is to investigate the effects and molecular mechanisms of emodin and aloe-emodin on breast cancer cell proliferation. Our results indicate that both emodin and aloe-emodin are capable of inhibiting breast cancer cell proliferation by downregulating ERαprotein levels, thereby suppressing ERαtranscriptional activation. Furthermore, aloe-emodin treatment led to the dissociation of heat shock protein 90 (HSP90) and ERαand increased ERαubiquitination. Although emodin had similar effects to aloe-emodin, it was not capable of promoting HSP90/ERαdissociation and ERαubiquitination. Protein fractionation results suggest that aloe-emodin tended to induce cytosolic ERαdegradation. Although emodin might induce cytosolic ERαdegradation, it primarily affected nuclear ERαdistribution similar to the action of estrogen when protein degradation was blocked. In conclusion, our data demonstrate that emodin and aloe-emodin specifically suppress breast cancer cell proliferation by targeting ERαprotein stability through distinct mechanisms. These findings suggest a possible application of anthraquinones in preventing or treating breast cancer in the future.

Madhuca indica Inhibits Breast Cancer Cell Proliferation by Modulating COX-2 Expression

2019 ◽  
Vol 18 (7) ◽  
pp. 459-474 ◽  
Author(s):  
Paramita Ghosh ◽  
Debarpan Mitra ◽  
Sreyashi Mitra ◽  
Sudipta Ray ◽  
Samir Banerjee ◽  
...  
Keyword(s):  
Breast Cancer ◽  
Cell Proliferation ◽  
Cancer Cell ◽  
Breast Cancer Cell ◽  
Cancer Cell Proliferation ◽  
Breast Cancer Cell Proliferation ◽  
Cox 2

Characterization of YY1 OPB Peptide for its Anticancer Activity

2019 ◽  
Vol 19 (6) ◽  
pp. 504-511 ◽  
Author(s):  
Yige Qi ◽  
Ting Yan ◽  
Lu Chen ◽  
Qiang Zhang ◽  
Weishu Wang ◽  
...  
Keyword(s):  
Breast Cancer ◽  
Amino Acids ◽  
Cell Proliferation ◽  
Cancer Cell ◽  
Breast Cancer Cell ◽  
Expression Vectors ◽  
Cancer Cell Proliferation ◽  
Breast Cancer Cell Proliferation ◽  
Oncogene Products ◽  
And Migration

Background:The oncoprotein binding (OPB) domain of Yin Yang 1 (YY1) consists of 26 amino acids between G201 and S226, and is involved in YY1 interaction with multiple oncogene products, including MDM2, AKT, EZH2 and E1A. Through the OPB domain, YY1 promotes the oncogenic or proliferative regulation of these oncoproteins in cancer cells. We previously demonstrated that a peptide with the OPB sequence blocked YY1-AKT interaction and inhibited breast cancer cell proliferation.Objective:In the current study, we characterized the OPB domain and determined a minimal region for peptide design to suppress cancer cellMethods:Using alanine-scan method, we identified that the amino acids at OPB C-terminal are essential to YY1 binding to AKT. Further studies suggested that serine and threonine residues, but not lysines, in OPB play a key role in YY1-AKT interaction. We generated GFP fusion expression vectors to express OPB peptides with serially deleted N-terminal and found that OPB1 (i.e. G201-S226) is cytoplasmic, but OPB2 (i.e. E206-S226), OPB3 (i.e. E206-S226) and control peptide were both nuclear and cytoplasmic.Results:Both OPB1 and 2 inhibited breast cancer cell proliferation and migration, but OPB3 exhibited similar effects to control. OPB1 and 2 caused cell cycle arrest at G1 phase, increased p53 and p21 expression, and reduced AKT(S473) phosphorylation in MCF-7 cells, but not in MDA-MB-231 cells.Conclusion:: Overall, the serines and threonines of OPB are essential to YY1 binding to oncoproteins, and OPB peptide can be minimized to E206-S226 that maintain inhibitory activity to YY1- promoted cell proliferation.

The epithelial sodium channel has a role in breast cancer cell proliferation

2021 ◽  
Vol 187 (1) ◽  
pp. 31-43
Author(s):  
Adam W. Ware ◽  
Joshua J. Harris ◽  
Tania L. Slatter ◽  
Heather E. Cunliffe ◽  
Fiona J. McDonald
Keyword(s):  
Breast Cancer ◽  
Cell Proliferation ◽  
Sodium Channel ◽  
Cancer Cell ◽  
Breast Cancer Cell ◽  
Epithelial Sodium Channel ◽  
Cancer Cell Proliferation ◽  
Breast Cancer Cell Proliferation
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