PARP inhibitor BMN-673 induced apoptosis by trapping PARP-1 and inhibiting base excision repair via modulation of Pol-β in chromatin of breast cancer cells

2022 ◽  
pp. 115860
Author(s):  
Chinmayee Sethy ◽  
Chanakya Nath Kundu
Keyword(s):  
Breast Cancer ◽  
Cancer Cells ◽  
Base Excision Repair ◽  
Breast Cancer Cells ◽  
Excision Repair ◽  
Parp Inhibitor ◽  
Base Excision ◽  
Induced Apoptosis ◽  
Parp 1

Chk1 inhibitor synergizes quinacrine mediated apoptosis in breast cancer cells by compromising the base excision repair cascade

2016 ◽  
Vol 105 ◽  
pp. 23-33 ◽  
Author(s):  
Ranjan Preet ◽  
Sumit Siddharth ◽  
Shakti Ranjan Satapathy ◽  
Sarita Das ◽  
Anmada Nayak ◽  
...  
Keyword(s):  
Breast Cancer ◽  
Cancer Cells ◽  
Base Excision Repair ◽  
Breast Cancer Cells ◽  
Excision Repair ◽  
Chk1 Inhibitor ◽  
Base Excision

scholarly journals Author response: Perturbation of base excision repair sensitizes breast cancer cells to APOBEC3 deaminase-mediated mutations

2019 ◽  
Author(s):  
Birong Shen ◽  
Joseph H Chapman ◽  
Michael F Custance ◽  
Gianna M Tricola ◽  
Charles E Jones ◽  
...  
Keyword(s):  
Breast Cancer ◽  
Cancer Cells ◽  
Base Excision Repair ◽  
Breast Cancer Cells ◽  
Excision Repair ◽  
Author Response ◽  
Base Excision

scholarly journals Perturbation of base excision repair sensitizes breast cancer cells to APOBEC3 deaminase-mediated mutations

eLife ◽  
2020 ◽  
Vol 9 ◽  
Author(s):  
Birong Shen ◽  
Joseph H Chapman ◽  
Michael F Custance ◽  
Gianna M Tricola ◽  
Charles E Jones ◽  
...  
Keyword(s):  
Breast Cancer ◽  
Cancer Cells ◽  
Base Excision Repair ◽  
Breast Cancer Cells ◽  
Excision Repair ◽  
Entry Site ◽  
Abasic Sites ◽  
Elevated Expression ◽  
Base Excision

Abundant APOBEC3 (A3) deaminase-mediated mutations can dominate the mutational landscape (‘mutator phenotype’) of some cancers, however, the basis of this sporadic vulnerability is unknown. We show here that elevated expression of the bifunctional DNA glycosylase, NEIL2, sensitizes breast cancer cells to A3B-mediated mutations and double-strand breaks (DSBs) by perturbing canonical base excision repair (BER). NEIL2 usurps the canonical lyase, APE1, at abasic sites in a purified BER system, rendering them poor substrates for polymerase β. However, the nicked NEIL2 product can serve as an entry site for Exo1 in vitro to generate single-stranded DNA, which would be susceptible to both A3B and DSBs. As NEIL2 or Exo1 depletion mitigates the DNA damage caused by A3B expression, we suggest that aberrant NEIL2 expression can explain certain instances of A3B-mediated mutations.

scholarly journals Role of Insulin-Like Growth Factor Binding Protein-3 in 1, 25-Dihydroxyvitamin-D3-Induced Breast Cancer Cell Apoptosis

2013 ◽  
Vol 2013 ◽  
pp. 1-9 ◽  
Author(s):  
C. Brosseau ◽  
G. Pirianov ◽  
K. W. Colston
Keyword(s):  
Breast Cancer ◽  
Growth Factor ◽  
Cancer Cells ◽  
Breast Cancer Cells ◽  
Igf I ◽  
Induced Apoptosis ◽  
Parp 1 ◽  
Mcf 7 ◽  
Igfbp 3

Insulin-like growth factor I (IGF-I) is implicated in breast cancer development and 1, 25-dihydroxyvitamin D3(1, 25-D3) has been shown to attenuate prosurvival effects of IGF-I on breast cancer cells. In this study the role of IGF binding protein-3 (IGFBP-3) in 1, 25-D3-induced apoptosis was investigated using parental MCF-7 breast cancer cells and MCF-7/VDRcells, which are resistant to the growth inhibitory effects of 1, 25-D3. Treatment with 1, 25-D3increased IGFBP-3 mRNA expression in both cell lines but increases in intracellular IGFBP-3 protein and its secretion were observed only in MCF-7. 1, 25-D3-induced apoptosis was not associated with activation of any caspase but PARP-1 cleavage was detected in parental cells. IGFBP-3 treatment alone produced cleavage of caspases 7, 8, and 9 and PARP-1 in MCF-7 cells. IGFBP-3 failed to activate caspases in MCF-7/VDRcells; however PARP-1 cleavage was detected. 1, 25-D3treatment inhibited IGF-I/Akt survival signalling in MCF-7 but not in MCF-7/VDRcells. In contrast, IGFBP-3 treatment was effective in inhibiting IGF-I/Akt pathways in both breast cancer lines. These results suggest a role for IGFBP-3 in 1, 25-D3apoptotic signalling and that impaired secretion of IGFBP-3 may be involved in acquired resistance to vitamin D in breast cancer.

Lobetyolin inhibits the proliferation of breast cancer cells via ASCT2 down-regulation-induced apoptosis

2021 ◽  
pp. 096032712110214
Author(s):  
Yansong Chen ◽  
Ye Tian ◽  
Gongsheng Jin ◽  
Zhen Cui ◽  
Wei Guo ◽  
...  
Keyword(s):  
Breast Cancer ◽  
Mrna Expression ◽  
Cancer Cells ◽  
Breast Cancer Cells ◽  
Glutamine Metabolism ◽  
Down Regulation ◽  
Anti Cancer ◽  
Induced Apoptosis ◽  
Glutamine Uptake

This study aimed to investigate the anti-cancer effect of lobetyolin on breast cancer cells. Lobetyolin was incubated with MDA-MB-231 and MDA-MB-468 breast cancer cells for 24 h. Glucose uptake and the mRNA expression of GLUT4 ( SLC2A4), HK2 and PKM2 were detected to assess the effect of lobetyolin on glucose metabolism. Glutamine uptake and the mRNA expression of ASCT2 ( SLC1A5), GLS1, GDH and GLUL were measured to assess the effect of lobetyolin on glutamine metabolism. Annexin V/PI double staining and Hoechst 33342 staining were used to investigate the effect of lobetyolin on cell apoptosis. Immunoblot was employed to estimate the effect of lobetyolin on the expression of proliferation-related markers and apoptosis-related markers. SLC1A5 knockdown with specific siRNA was performed to study the role of ASCT2 played in the anti-cancer effect of lobetyolin on MDA-MB-231 and MDA-MB-468 breast cancer cells. C-MYC knockdown with specific siRNA was performed to study the role of c-Myc played in lobetyolin-induced ASCT2 down-regulation. Myr-AKT overexpression was performed to investigate the role of AKT/GSK3β signaling played in lobetyolin-induced down-regulation of c-Myc and ASCT2. The results showed that lobetyolin inhibited the proliferation of both MDA-MB-231 and MDA-MB-468 breast cancer cells. Lobetyolin disrupted glutamine uptake via down-regulating ASCT2. SLC1A5 knockdown attenuated the anti-cancer effect of lobetyolin. C-MYC knockdown attenuated lobetyolin-caused down-regulation of ASCT2 and Myr-AKT overexpression reversed lobetyolin-caused down-regulation of both c-Myc and ASCT2. In conclusion, the present work suggested that lobetyolin exerted anti-cancer effect via ASCT2 down-regulation-induced apoptosis in breast cancer cells.

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