PARPBP is a prognostic marker and confers anthracycline resistance to breast cancer

Background: PARPBP (PARP1 binding protein) is an important suppressor of homologous recombination during DNA repair, but the expression and function of PARPBP in breast cancer remain unclear. Methods: PARPBP expression was analyzed in breast cancer patient samples and public datasets for its correlation with clinical outcome. The function of PARPBP in breast cancer cell proliferation and anthracycline treatment response were studied both in vitro and in vivo. Results: PARPBP was upregulated significantly at both mRNA and protein levels in breast cancer tissues compared with normal breast tissues. PARPBP high expression group had poorer overall survival (OS) than the PARPBP low expression group. Knockdown of PARPBP suppressed breast cancer cell proliferation and colony formation while overexpression of PARPBP did the opposite. We found that transcription factor forkhead box M1 (FOXM1) could activate PARPBP expression by directly binding to the promoter of PARPBP. In addition, high expression of PARPBP related with anthracycline resistance in breast cancer. Depletion of PARPBP increased breast cancer cell apoptosis and DNA damage caused by epirubicin. Moreover, tumor xenograft experiments further demonstrated that PARPBP was involved in breast cancer anthracycline resistance. Conclusion: Taken together, our results highlight that PARPBP is a prognostic marker and confers anthracycline resistance on breast cancer.

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The role of StarD13 in breast cancer cell proliferation and motility. (c2012)

10.26756/th.2012.36 ◽

2012 ◽

Author(s):

Samer J. Hanna

Keyword(s):

Breast Cancer ◽

Cell Proliferation ◽

Cancer Cell ◽

Breast Cancer Cell ◽

Cancer Cell Proliferation ◽

Breast Cancer Cell Proliferation

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TIG3-A Novel Inhibitor of Breast Cancer Cell Proliferation

10.21236/ada420065 ◽

2003 ◽

Author(s):

Richard L. Eckert

Keyword(s):

Breast Cancer ◽

Cell Proliferation ◽

Cancer Cell ◽

Breast Cancer Cell ◽

Cancer Cell Proliferation ◽

Breast Cancer Cell Proliferation

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

Current Molecular Medicine ◽

10.2174/1566524019666181212100808 ◽

2019 ◽

Vol 18 (7) ◽

pp. 459-474 ◽

Cited By ~ 3

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

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Characterization of YY1 OPB Peptide for its Anticancer Activity

Current Cancer Drug Targets ◽

10.2174/1568009618666181031153151 ◽

2019 ◽

Vol 19 (6) ◽

pp. 504-511 ◽

Cited By ~ 3

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.

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