scholarly journals Exogenous FABP4 increases breast cancer cell proliferation and activates the expression of fatty acid transport proteins

2016 ◽  
Vol 56 (1) ◽  
pp. 208-217 ◽  
Author(s):  
Sandra Guaita-Esteruelas ◽  
Alba Bosquet ◽  
Paula Saavedra ◽  
Josep Gumà ◽  
Josefa Girona ◽  
...  
Keyword(s):  
Breast Cancer ◽  
Cell Proliferation ◽  
Fatty Acid ◽  
Breast Cancer Cell ◽  
Transport Proteins ◽  
Fatty Acid Transport ◽  
Cancer Cell Proliferation ◽  
Acid Transport ◽  
Breast Cancer Cell Proliferation ◽  
Fatty Acid Transport Proteins

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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