Knockdown of p54nrb inhibits migration, invasion and TNF-α release of human acute monocytic leukemia THP1 cells

Zhang, Xiujuan; Wu, Changli; Wang, Xiong; Chen, Chunling; Li, Rong; Zhou, Guangji

doi:10.3892/or.2016.4756

Cited by 10 publications

(4 citation statements)

References 34 publications

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“…In some breast cancers, lower NONO is associated with increased proliferation . The THP1 cell knock downed NONO shows a decrease of G0/G1 phase cells and an increase of S and G2/M phase cells compared with wild‐type or negative control cells, which indicates the knock‐down of NONO can accelerate THP1 cell cycle . Thus, NONO plays dual roles as either a promoter or inhibitor of cell proliferation.…”

Section: Physiological Functions Of Nonomentioning

confidence: 95%

NONO and tumorigenesis: More than splicing

Feng

Deng

et al. 2020

J Cellular Molecular Medi

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The NONO (non-POU domain-containing octamer-binding protein) protein, also known as 54 kD nuclear RNA-and DNA-binding protein (p54nrb), belongs to the multifunctional DBHS (Drosophila behaviour/human splicing) family of proteins which can bind DNA, RNA and protein. 1 NONO has a nuclear localization signal (NLS) at its C-terminal, so it is located in the nucleus of most mammalian cells and is primarily distributed in the subnuclear domain named paraspeckles. 2 Emerging evidence strongly indicates new roles for NONO in tumorigenesis, including but not limited to regulating proliferation, apoptosis, cell migration and DNA damage repair. Here, we provide a comprehensive review of the NONO and its functions in tumorigenesis. AbstractThe non-POU domain-containing octamer-binding protein NONO/p54 nrb , which belongs to the Drosophila behaviour/human splicing (DBHS) family, is a multifunctional nuclear protein rarely functioning alone. Emerging solid evidences showed that NONO engages in almost every step of gene regulation, including but not limited to mRNA splicing, DNA unwinding, transcriptional regulation, nuclear retention of defective RNA and DNA repair. NONO is involved in many biological processes including cell proliferation, apoptosis, migration and DNA damage repair. Dysregulation of NONO has been found in many types of cancer. In this review, we summarize the current and fast-growing knowledge about the regulation of NONO, its biological function and implications in tumorigenesis and cancer progression. Overall, significant findings about the roles of NONO have been made, which might make NONO to be a new biomarker or/and a possible therapeutic target for cancers. K E Y W O R D S DBHS, NONO, splicing, tumorigenesis | 4369 FENG Et al.

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Section: Physiological Functions Of Nonomentioning

confidence: 95%

NONO and tumorigenesis: More than splicing

Feng

Deng

et al. 2020

J Cellular Molecular Medi

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“…Numerous studies have certified that miR-141-3p regulates cell proliferation and apoptosis in multiple cancers (42,43). Moreover, MNX1 has been testified to expedite insulinoma cell proliferation via interaction with NONO protein (44). In the course of inflammation, the capacity of cell viability and apoptosis tend to change naturally (45).…”

Section: Discussionmentioning

confidence: 99%

Increased Expression of microRNA-141-3p Improves Necrotizing Enterocolitis of Neonates Through Targeting MNX1

et al. 2020

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Objective: MicroRNA-141-3p (miR-141-3p) has been investigated in various kinds of cancers. This research delves into the functions and regulatory mechanisms of miR-141-3p in necrotizing enterocolitis (NEC) of neonates. Methods: NEC tissues were obtained from neonatal mice, and subsequently, expression of miR-141-3p and motor neuron and pancreas homeobox 1 (MNX1) was assayed via RT-qPCR. Moreover, the intestinal histopathological changes and histiocytic apoptosis were observed via hematoxylin and eosin (H&E) and TUNEL staining. The correlative inflammatory factors and oxidative stress markers were evaluated to uncover the influence of miR-141-3p in NEC tissue damage. Further, the relation between MNX1 and miR-141-3p was predicated, and the functions of MNX1 in inflammatory response and cell growth of IEC-6 cells were investigated. Results: Downregulated miR-141-3p and upregulated MNX1 were discovered in NEC tissues. Moreover, miR-141-3p clearly alleviated inflammation response and oxidative stress damage in NEC, which was achieved through regulating inflammatory cytokines (IL-1β, IL-6, and TNF-α) and oxidative stress markers (MPO, MDA, and SOD) expression. MNX1 was forecasted as a target gene of miR-141-3p; meanwhile, MNX1 overexpression overturned the influence of miR-141-3p in the inflammatory response and cell growth process of IEC-6 cells. Conclusion: These explorations reveal that increased expression of miR-141-3p could improve the damage to intestinal tissues in NEC through targeting MNX1. The research might exhibit a neoteric therapeutic strategy for NEC.

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“…According to the final score, the expression levels of TWIST, MDR1, E-cadherin and Vimentin were categorized as low (<6) or high (≥6). TWIST-silenced HepG2 and R-HepG2, and negative control (NC) HepG2 and R-HepG2 cell lines were established as previously described (18). Packaged lentiviruses containing TWIST-specific short hairpin RNA (shRNA), which were labeled with green fluorescent protein as a transfection marker were provided by Shanghai GenePharma Co., Ltd. (Shanghai, China).…”

Section: Immunohistochemistry (Ihc)mentioning

confidence: 99%

“…Western blot analysis. Western blotting was performed as previously described (18). Cells were collected and lysed with radioimmunoprecipitation assay lysis buffer [50 mM Tris-HCl (pH 8.0), 150 mM sodium chloride, 1.0% Igepal CA-630 (NP-40), 0.5% sodium deoxycholate).…”

Section: Immunohistochemistry (Ihc)mentioning

confidence: 99%

Knockdown of TWIST enhances the cytotoxicity of chemotherapeutic drugs in doxorubicin-resistant HepG2 cells by suppressing MDR1 and EMT

Liang

et al. 2018

Int J Oncol

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The transcription factor twist family bHLH transcription factor 1 (TWIST), which is a member of the basic helix-loop-helix class of proteins, is known to induce epithelial-mesenchymal transition (EMT) and promote cancer metastasis. TWIST has previously been reported to be associated with multidrug resistance (MDR), since its depletion increases drug sensitivity. Although these previous studies have established a strong association between EMT and MDR, the molecular mechanism remains obscure. The present study demonstrated that TWIST protein expression was elevated in liver cancer, and was positively correlated with multidrug resistance protein 1 (MDR1) expression. Conversely, MDR1 was negatively correlated with E‑cadherin expression in liver cancer samples. In addition, the present study indicated that doxorubicin-resistant HepG2 (R‑HepG2) cells acquired an EMT phenotype. TWIST was also more highly expressed in R‑HepG2 cells compared with in parental HepG2 cells. Knockdown of TWIST increased the sensitivity of R‑HepG2 cells to 5-fluroracil, cisplatin and doxorubicin through a reduction in MDR1 expression and drug efflux ability. Furthermore, knockdown of TWIST in R‑HepG2 cells inhibited the migratory ability of cells and suppressed the EMT phenotype. These findings demonstrated that targeting TWIST may be considered a novel strategy to overcome drug resistance in liver cancer.

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Knockdown of p54nrb inhibits migration, invasion and TNF-α release of human acute monocytic leukemia THP1 cells

Cited by 10 publications

References 34 publications

NONO and tumorigenesis: More than splicing

NONO and tumorigenesis: More than splicing

Increased Expression of microRNA-141-3p Improves Necrotizing Enterocolitis of Neonates Through Targeting MNX1

Knockdown of TWIST enhances the cytotoxicity of chemotherapeutic drugs in doxorubicin-resistant HepG2 cells by suppressing MDR1 and EMT

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