Poly(ADP‐ribose) polymerase‐1 promotes recruitment of meiotic recombination‐11 to chromatin and DNA double‐strand break repair in Ku70‐deficient breast cancer cells

Huang, Yujing; Shao, Qing; Luo, Xinrong; Yang, Dejuan; Zeng, Beilei; Xiang, Tingxiu; Ren, Guosheng; Cheng, Qiao

doi:10.1096/fj.201800092r

Cited by 6 publications

(3 citation statements)

References 38 publications

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“…Therefore, we used the concentrations below 5.0 μM for tubeimoside II and 10.0 μM for olaparib and tubeimoside I for the following experiments. PARP 1 is a key factor in DNA repair and is considered as a crucial therapeutic target for the treatment of breast cancer . It can bind DNA double-strand breaks, modulates the recruitment of meiotic recombination 11 (MRE-11), and regulates the process of alternative end-joining (A-EJ) .…”

Section: Resultsmentioning

confidence: 99%

“…PARP 1 is a key factor in DNA repair and is considered as a crucial therapeutic target for the treatment of breast cancer. 43 It can bind DNA double-strand breaks, modulates the recruitment of meiotic recombination 11 (MRE-11), and regulates the process of alternative end-joining (A-EJ). 44 Therefore, we evaluated the expression of PARP 1 and MRE-11 affected by tubeimoside I and tubeimoside II on MDA-MB-231 cells.…”

Section: E Coli System Enabled Expression Of Parp 1 At Amentioning

confidence: 99%

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Affinity Chromatographic Method for Determining Drug–Protein Interaction with Enhanced Speed Than Typical Frontal Analysis

Ou,

Qiao,

et al. 2023

Langmuir

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Revealing drug−protein interaction is highly important to select a drug candidate with improved drug-like properties in the early stages of drug discovery. This highlights the urgent need to develop assays that enable the analysis of drug−protein interaction with high speed. Herein, this purpose was realized by the development of an affinity chromatographic method with a two-fold higher speed than typical assays like frontal analysis and zonal elution. The method involved synthesis of a stationary phase by immobilizing poly(ADPribose) polymerase-1 (PARP 1 ) onto macroporous silica gel through a one-step bioorthogonal reaction, characterization of mutual displacement interaction of two canonical drugs to the immobilized PARP 1 , determination of the interaction between three (iniparib, rucaparib, and olaparib) drugs and the protein, and validation of these parameters by typical frontal analysis. The numbers of binding sites on the column were (2.85 ± 0.05) × 10 −7 , (1.89 ± 0.71) × 10 −6 , and (1.49 ± 0.06) × 10 −7 M for iniparib, rucaparib, and olaparib, respectively. On these sites, the association constants of the three drugs to the protein were (9.85 ± 0.56) × 10 4 , (2.85 ± 0.34) × 10 4 , and (1.07 ± 0.35) × 10 5 M −1 . The determined parameters presented a good agreement with the calculation by typical frontal analyses, which indicated that the current continuous competitive frontal analysis method was reliable for determining drug−protein interaction. Application of the methods was achieved by screening tubeimosides I and II as the bioactive compounds against breast cancer in Bolbostemma paniculatum. Their mechanism may be the interference of DNA repair via down-regulating PARP 1 and meiotic recombination 11 expressions, thus leading to oncogene mutations and death of cancer cells. The method was high speed since it allowed simultaneous determination of binding parameters between two drugs and a protein with a smaller number of experiments to be performed. Such a feature made the method an attractive alternative for high-speed analysis of drug−protein interaction or the other bindings in a binary system.

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Section: Resultsmentioning

confidence: 99%

Section: E Coli System Enabled Expression Of Parp 1 At Amentioning

confidence: 99%

Affinity Chromatographic Method for Determining Drug–Protein Interaction with Enhanced Speed Than Typical Frontal Analysis

Ou,

Qiao,

et al. 2023

Langmuir

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“…92 In the absence of KU complex, DSBs bound to MRN complex with the help of PARP-1, which results in end processing of DSBs. 93 Now sequence microhomology between two DNA ends take place, then Pol θ (may be PARP-1 recruited) synthesizes nucleotides to the damage site, and finally, DNA ligase-3 ligates the ends through aNHEJ, an error-prone DNA repair mechanism due to insertion or deletion at the point of microhomology. 89…”

Section: Role Of Parp-1 In Dna Repairmentioning

confidence: 99%

An assessment of poly (ADP‐ribose) polymerase‐1 role in normal and cancer cells

et al. 2020

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Poly (ADP-ribose) polymerase (PARP) is a superfamily of 18 proteins characterized by the PARP homology domain, the catalytic domain. This catalytic domain helps in the ADP-ribosylation of various acceptor proteins using nicotinamide adenine dinucleotide (NAD+) as a donor for ADP-ribose. PARP-1 and PARP-2 carry out 80% of poly-ADP-ribosylation of cellular protein. Hence, their combined knockout results in embryonic lethality of mice. PARP-1 consists of three major domains, namely, DNA binding domain, automodification domain, and a catalytic domain. These domains further consist of subdomains and motifs, which helps PARP-1 in a diverse function. PARP-1 is mainly involved in DNA damage detection and repair, but emerging evidence suggests its role in many other functions such as DNA synthesis, replication, apoptosis, necrosis, and cancer progression. Herein, we review the current state of the PARP-1 role in DNA damage repair and other biological processes including epithelial to mesenchymal transition (EMT). We have also observed the role of PARP-1 in modulating EMT regulators like E-cadherin, Vimentin, Claudin-1, Snail, Smad-4, Twist-1, and β-catenin. Here, we have also attempted to relate the role of PARP-1 in EMT of cancer cells.

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The effect of vitamin E and selenium combination in repairing fluoride-induced DNA damage to NRK-52E cells

2020

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Poly(ADP‐ribose) polymerase‐1 promotes recruitment of meiotic recombination‐11 to chromatin and DNA double‐strand break repair in Ku70‐deficient breast cancer cells

Cited by 6 publications

References 38 publications

Affinity Chromatographic Method for Determining Drug–Protein Interaction with Enhanced Speed Than Typical Frontal Analysis

Affinity Chromatographic Method for Determining Drug–Protein Interaction with Enhanced Speed Than Typical Frontal Analysis

An assessment of poly (ADP‐ribose) polymerase‐1 role in normal and cancer cells

The effect of vitamin E and selenium combination in repairing fluoride-induced DNA damage to NRK-52E cells

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