Chapter 6 DNA Damage Response and Apoptosis

Plesca, Dragos; Mazumder, Suparna; Almasan, Alexandru

doi:10.1016/s0076-6879(08)01606-6

Cited by 149 publications

(95 citation statements)

References 22 publications

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“…Moreover, a significant accumulation of cells in the sub-G1 phase was observed after TPD52L2 knockdown, which is suggestive of apoptosis. 17 Furthermore, knockdown of TPD52L2 in MGC80-3 cells caused a cleavage of PARP, which is one of the most used diagnostic tools for the detection of apoptosis in many cell types expression. 18 Their study revealed that TPD52L2 is essential for gastric cancer cell proliferation, probably through regulation of cell cycle and apoptosis.…”

Section: Discussionmentioning

confidence: 99%

Retracted: Tumor Protein D52-Like 2 Accelerates Gastric Cancer Cell Proliferation In Vitro

Wang²,

Zhu³

et al. 2015

Cancer Biotherapy and Radiopharmaceuticals

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Tumor protein D52-like 2 (TPD52L2) has been commonly described as a protein involved in tumorigenesis, according to its name. However, its pathological function remains under investigation. In the present study, TPD52L2 was found to be widely expressed in several gastric cancer cell lines. An efficient knockdown of TPD52L2 by a specific short hairpin RNA (shRNA) loaded in lentivirus resulted in a remarkable reduction in cell proliferation in both MGC80-3 and SGC-7901 cell lines with high TPD52L2 expression, but a slight or little reduction in the proliferation of MKN-28 and AGS cells with low TPD52L2 expression. Further analysis by flow cytometry revealed that the cell cycle was primarily blocked in the G0/G1 phase, especially in the sub-G1 phase by TPD52L2 silencing, implying its possible roles in cell cycle control and apoptosis. Knockdown of TPD52L2 caused a cleavage of PARP in MGC80-3 cells. Their study suggests that TPD52L2 might promote gastric carcinogenesis, and could be a promising target with respect to developing new therapeutic strategies to treat gastric cancer.

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Section: Discussionmentioning

confidence: 99%

Retracted: Tumor Protein D52-Like 2 Accelerates Gastric Cancer Cell Proliferation In Vitro

Wang²,

Zhu³

et al. 2015

Cancer Biotherapy and Radiopharmaceuticals

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“…However, since reducing the expression of RBM3 or CIRBP did not induce apoptosis or only partly impeded the cell cycle, it was determined if the effect of knocking down their expression impaired DNA damage repair that results in decreasing cell survival during proliferation and rendering the cells more susceptible to the effects of chemotherapy. Since phosphorylation of H2A.X at serine 139 correlates well with DNA damage [Plesca et al, 2008], we determined the γ-H2A.X content to evaluate the impact of the knockdown on DNA damage and repair response. As shown in Figure 6B, both RBM3 and CIRBP down-regulation significantly enhanced DNA damage triggered by drugs in LNCaP cells as judged by the increase in accumulation of γ-H2A.X.…”

Section: Resultsmentioning

confidence: 99%

Down‐regulating cold shock protein genes impairs cancer cell survival and enhances chemosensitivity

Zeng

Kulkarni

Inoue

et al. 2009

J of Cellular Biochemistry

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The microenvironment of the cancer cell is pivotal to its phenotypic regulation. One of the central components of the microenvironment is temperature. An elevation in environmental temperature has been shown to increase the cancer cell's susceptibility to chemo- and radiation therapy. The goal of the studies described here was to identify some of the pathways that are modified by a mild increase in temperature in cancer cells. Using prostate cancer cells as a model system we found that in addition to the well described and anticipated up-regulation of the heat shock family of proteins, there is a significant down-regulation of certain members of the “cold shock” family of proteins such as, RNA binding motif protein 3 (RBM3) and cold inducible RNA binding protein (CIRBP). siRNA-mediated down-regulation of the cold shock protein (CSP) encoding mRNAs dramatically attenuates cell survival in the absence of any heat application. Furthermore, we also demonstrate that knocking down the CSPs can enhance the therapeutic response of prostate cancer cells to chemotherapy. Our findings suggest that down-regulating CSPs in cancer cells may “mimic” the stress response the cells experience when exposed to heat treatment rendering them more susceptible to therapy. Thus, the pharmacological modulation of RBM3 and CIRBP may represent novel therapeutic approaches for prostate cancer.

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“…When damage is severe and irreversible, the host cell may undergo apoptosis (10,41). In the context of mild damage, it may recruit the repair machinery, through either NHEJ or a mechanism involved in homologous recombination, and cell cycle arrest (14,32).…”

Section: Discussionmentioning

confidence: 99%

Parvovirus B19 Infection of Human Primary Erythroid Progenitor Cells Triggers ATR-Chk1 Signaling, Which Promotes B19 Virus Replication

Luo

Lou

Deng

et al. 2011

J Virol

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Human parvovirus B19 (B19V) infection is restricted to erythroid progenitor cells of the human bone marrow. Although the mechanism by which the B19V genome replicates in these cells has not been studied in great detail, accumulating evidence has implicated involvement of the cellular DNA damage machinery in this process. Here, we report that, in ex vivo-expanded human erythroid progenitor cells, B19V infection induces a broad range of DNA damage responses by triggering phosphorylation of all the upstream kinases of each of three repair pathways: ATM (ataxia-telangiectasi mutated), ATR (ATM and Rad3 related), and DNA-PKcs (DNA-dependent protein kinase catalytic subunit). We found that phosphorylated ATM, ATR, and DNA-PKcs, and also their downstream substrates and components (Chk2, Chk1, and Ku70/Ku80 complex, respectively), localized within the B19V replication center. Notably, inhibition of kinase phosphorylation (through treatment with either kinase-specific inhibitors or kinase-specific shRNAs) revealed requirements for signaling of ATR and DNA-PKcs, but not ATM, in virus replication. Inhibition of the ATR substrate Chk1 led to similar levels of decreased virus replication, indicating that signaling via the ATR-Chk1 pathway is critical to B19V replication. Notably, the cell cycle arrest characteristic of B19V infection was not rescued by interference with the activity of any of the three repair pathway kinases.

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Chapter 6 DNA Damage Response and Apoptosis

Cited by 149 publications

References 22 publications

Retracted: Tumor Protein D52-Like 2 Accelerates Gastric Cancer Cell Proliferation In Vitro

Retracted: Tumor Protein D52-Like 2 Accelerates Gastric Cancer Cell Proliferation In Vitro

Down‐regulating cold shock protein genes impairs cancer cell survival and enhances chemosensitivity

Parvovirus B19 Infection of Human Primary Erythroid Progenitor Cells Triggers ATR-Chk1 Signaling, Which Promotes B19 Virus Replication

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