Downregulation of ANP32B, a novel substrate of caspase-3, enhances caspase-3 activation and apoptosis induction in myeloid leukemic cells

Shen, Shao‐Ming; Yu, Yun; Wu, Yingli; Cheng, Jinke; Wang, Li‐Shun; Chen, Guoqiang

doi:10.1093/carcin/bgp320

Cited by 55 publications

(57 citation statements)

References 51 publications

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“…Caspase Inhibition-ANP32B (acidic leucine-rich nuclear phosphoprotein 32 B) is involved in gene regulation, acting as a histone chaperone (47) or modulating mRNA trafficking as a HuR ligand (82). In addition, ANP32B can act as a caspase-3 inhibitor (Fig.…”

Section: Exploring Novel CC Protein Interaction Partners Using Amentioning

confidence: 99%

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Structural and Functional Analysis of Novel Human Cytochrome c Targets in Apoptosis

Martínez-Fábregas

Dı́az-Moreno

González‐Arzola

et al. 2014

Molecular & Cellular Proteomics

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Since the first description of apoptosis four decades ago, great efforts have been made to elucidate, both in vivo and in vitro, the molecular mechanisms involved in its regulation. Although the role of cytochrome c during apoptosis is well established, relatively little is known about its participation in signaling pathways in vivo due to its essential role during respiration. To obtain a better understanding of the role of cytochrome c in the onset of apoptosis, we used a proteomic approach based on affinity chromatography with cytochrome c as bait in this study. In this approach, novel cytochrome c interaction partners were identified whose in vivo interaction and cellular localization were facilitated through bimolecular fluorescence complementation. Modeling of the complex interface between cytochrome c and its counterparts indicated the involvement of the surface surrounding the heme crevice of cytochrome c, in agreement with the vast majority of known redox adducts of cytochrome c. However, in contrast to the high turnover rate of the mitochondrial cytochrome c redox adducts, those occurring under apoptosis led to the formation of stable nucleo-cytoplasmic ensembles, as inferred mainly from surface plasmon resonance and nuclear magnetic resonance measurements, which permitted us to corroborate the formation of such complexes in vitro. The results obtained suggest that human cytochrome c interacts with pro-survival, anti-apoptotic proteins following its release into the cytoplasm. Thus, cytochrome c may interfere with cell survival pathways and unlock apoptosis in order to prevent the spatial and temporal coexistence of antagonist signals. Molecular & Cellular

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Section: Exploring Novel CC Protein Interaction Partners Using Amentioning

confidence: 99%

“…In addition, ANP32B can act as a caspase-3 inhibitor (Fig. 9B), as the expression of endogenous ANP32B blocked by a specific siRNA enhances caspase-3 activation and promotes apoptosis (82). In contrast, ANP32B overexpression results in the rescue of Rat1 cells from induced apoptosis (83).…”

Section: Exploring Novel CC Protein Interaction Partners Using Amentioning

confidence: 99%

Structural and Functional Analysis of Novel Human Cytochrome c Targets in Apoptosis

Martínez-Fábregas

Dı́az-Moreno

González‐Arzola

et al. 2014

Molecular & Cellular Proteomics

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“…In most cases caspase activation is indispensable for complete cell apoptosis (37). Over 400 caspase substrates have been identified, including proteins involved in apoptosis, DNA metabolism and repair, and regulation of the cell cycle and proliferation (15), and the number is still increasing with the addition of tumor suppressor proteins (29,41).…”

mentioning

confidence: 99%

Prostate Apoptosis Response 4 (Par-4), a Novel Substrate of Caspase-3 during Apoptosis Activation

Chaudhry

Singh

Parent

et al. 2012

Molecular and Cellular Biology

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“…Retrovirus packaging and infection were carried out as previously described. 21 Virally infected cells were cultured in medium containing 2 lg/ml puromycin for 7 days and drug-resistant clones were collected and expanded. SGC-7901 cells infected with negative control sequence and shRNAs targeting MPS-1 were named NC and P1, 2, 4 cells, respectively.…”

Section: Cell Culture and Treatmentmentioning

confidence: 99%

Knockdown of metallopanstimulin‐1 inhibits NF‐κB signaling at different levels: The role of apoptosis induction of gastric cancer cells

Yang

Zhang

et al. 2011

Intl Journal of Cancer

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The ribosomal protein S27 (metallopanstimulin-1, MPS-1) has been reported to be a multifunctional protein, with increased expression in a number of cancers. We reported previously that MPS-1 was highly expressed in human gastric cancer. Knockdown of MPS-1 led to spontaneous apoptosis and repressed proliferation of human gastric cancer cells in vitro and in vivo. However, how does MPS-1 regulate these processes is unclear. Here we performed microarray and pathway analyses to investigate possible pathways involved in MPS-1 knockdown-induced apoptosis in gastric cancer cells. Our results showed that knockdown of MPS-1 inhibited NF-jB activity by reducing phosphorylation of p65 at Ser536 and IjBa at Ser32, inhibiting NF-jB nuclear translocation, and down-regulating its DNA binding activity. Furthermore, data-mining the Gene-RegulatoryNetwork revealed that growth arrest DNA damage inducible gene 45b (Gadd45b), a direct NF-jB target gene, played a critical role in MPS-1 knockdown-induced apoptosis. Over-expression of Gadd45b inhibited MPS-1 knockdown-induced apoptosis via inhibition of JNK phosphorylation. Taken together, these data revealed a novel pathway, the MPS-1/NF-jB/Gadd45b signal pathway, played an important role in MPS-1 knockdown-induced apoptosis of gastric cancer cells. This study sheds new light on the role of MPS-1/NF-jB in apoptosis and the possible use of MPS-1 targeting strategy in the treatment of gastric cancer.Gastric cancer is one of the most common cancers worldwide and it has the second highest mortality rate among all cancers.1 Although combination therapies are commonly used, the outcome of gastric cancer remains poor as the precise molecular events responsible for its generation and progression are still unknown. 2 In our previous studies, we used serological analysis of recombinant cDNA expression libraries (SEREX) to define new gastric cancer-related antigens and we successfully identified an array of relevant proteins, including metallopanstimulin-1 (MPS-1), 3 plant homeodomain finger 10 (PHF10) 4 and frizzled-related protein (FRZB). 5The MPS-1 protein, also known as ribosomal protein S27 (RPS27), is a component of the 40S subunit of the ribosome and belongs to the S27E family of ribosomal proteins.6 Being a zinc finger protein of C4 type, MPS-1 locates both in the cytoplasm and the nucleus. Previous studies demonstrated that MPS-1 is highly expressed in many types of malignant tumors and might be involved in the malignant progression. [7][8][9][10] In addition, the level of MPS-1 protein was found to be elevated in the sera of patients with various types of cancers and it was studied as a tumor marker or tumor-associated antigen;11,12 yet, the role of MPS-1 in tumorigenesis is unclear. We reported previously that the expression of MPS-1 was significantly higher in gastric cancer cells than their normal counterparts. Down-regulation of MPS-1 by shRNAs in gastric cancer cell line SGC-7901 increased spontaneous apoptosis and inhibited the tumor growth in vitro and in vivo.13 However, how do...

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Downregulation of ANP32B, a novel substrate of caspase-3, enhances caspase-3 activation and apoptosis induction in myeloid leukemic cells

Cited by 55 publications

References 51 publications

Structural and Functional Analysis of Novel Human Cytochrome c Targets in Apoptosis

Structural and Functional Analysis of Novel Human Cytochrome c Targets in Apoptosis

Prostate Apoptosis Response 4 (Par-4), a Novel Substrate of Caspase-3 during Apoptosis Activation

Knockdown of metallopanstimulin‐1 inhibits NF‐κB signaling at different levels: The role of apoptosis induction of gastric cancer cells

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