Interaction of Vault Particles with Estrogen Receptor in the MCF-7 Breast Cancer Cell

Abbondanza, Ciro; Rossi, Valentina; Roscigno, Annarita; Gallo, Luigi; Belsito, Angela; Piluso, Giulio; Medici, Nicola; Nigro, Vincenzo; Molinari, Anna Maria; Moncharmont, Bruno; Puca, Giovanni Alfredo

doi:10.1083/jcb.141.6.1301

Cited by 99 publications

(100 citation statements)

References 55 publications

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“…This suggests a possible cause and effect relationship between the resistance to apoptosis exhibited by senescent cells and their high content of MVP. In contrast to previous studies that showed that the majority of MVP resides in the cytoplasm and that no more than 5% of MVP is localized to the nucleus, 15,16 we observed that the MVP is equally localized in both the cytoplasm and nucleus (Figures 1f and g). Moreover, in the case of 253J cells, it was reported that more MVP was detected in the nucleus than in cytosol.…”

Section: Discussioncontrasting

confidence: 55%

“…10 MVP expression has also been shown to be induced by histone deacetylase inhibitors such as sodium butyrate, 11 phorbol 12-myristate 13-acetate (PMA) and cytarabine 12 as well as by cytotoxic drugs. [12][13][14] MVP/vaults have been proposed to be important in intracellular transport, [15][16][17] innate immunity 18 and virus infection. 19 Several studies demonstrated that MVP is important in cell signaling [20][21][22] and in cell survival.…”

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confidence: 99%

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On the role of major vault protein in the resistance of senescent human diploid fibroblasts to apoptosis

Ryu

et al. 2008

Cell Death Differ

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Major vault protein (MVP), the main component of vault complex, is overexpressed in many multidrug-resistant cancer cell lines, suggesting a possible role for MVP in cell signaling and survival. In this study, we have found that MVP is markedly increased in senescent human diploid fibroblasts (HDFs) as well as in aged organs. We examined whether MVP expression might be affected by apoptotic stress in an aging-dependent manner. We treated young and senescent HDFs with apoptosis-inducing agents such as H 2 O 2 , staurosporine and thapsigargin, and monitored MVP expression. We found that MVP expression is markedly reduced in young HDFs but not in senescent HDFs, in response to apoptotic stresses. Downregulation of MVP increased the sensitivity of senescent HDFs to apoptosis. Also, the level of antiapoptotic B-cell lymphoma protein-2 (Bcl-2) was significantly reduced and the accumulation of c-Jun increased in MVP knocked-down senescent HDFs. Moreover, treatment of MVP knocked-down senescent HDFs with SP600125, a specific c-Jun NH (2) Vaults are large ribonucleoprotein particles found in a great portion of eukaryotic cells. The vault particle is a multimeric structure composed of three proteins -the major vault protein (MVP), two minor vault proteins, vault poly (ADP-ribose) polymerase (VPARP) and telomerase-associated protein-1 (TP-1), and four small untranslated vault RNAs (vRNAs). 1 MVP is the main component of the vault complex accounting for 75% of the total particle mass. 2 The vault particle has been so named because it has a barrel-shaped structure, reminiscent of the vaulted ceilings in cathedrals. 3 The interaction of MVP by its coiled coil domain is involved in the formation of the basic vault complex. 4 MVP expression is upregulated in cancers such as melanoma, 5 colon cancer 6 and gliomas 7 during acquisition of multidrug resistance 8,9 and during differentiation of dendritic cells. 10 MVP expression has also been shown to be induced by histone deacetylase inhibitors such as sodium butyrate, 11 phorbol 12-myristate 13-acetate (PMA) and cytarabine 12 as well as by cytotoxic drugs. 12-14 MVP/vaults have been proposed to be important in intracellular transport, 15-17 innate immunity 18 and virus infection. 19 Several studies demonstrated that MVP is important in cell signaling [20][21][22] and in cell survival. 10,20,23 For example, serumdeprived MVP-deficient mouse embryonic fibroblasts (MEFs) exhibit significantly increased cell death when compared with wild-type MEFs. 20 Therefore, the role of MVP as a scaffolding protein for signaling proteins, especially for cell survival, has received more attention than as a transport vehicle. However, the exact role of MVP in cell survival is not well understood. In this study, we found that apoptotic resistance of senescent human diploid fibroblasts (HDFs) correlates with the increased content of MVP in the senescent cells. This is the first report implicating MVP in apoptosis resistance of senescent HDFs. ResultsIncreased expression of MVP in aged cells and organs...

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Section: Discussioncontrasting

confidence: 55%

mentioning

confidence: 99%

On the role of major vault protein in the resistance of senescent human diploid fibroblasts to apoptosis

Ryu

et al. 2008

Cell Death Differ

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“…Multidrug-resistant cell lines have been shown to use these routes to gain resistance to various drugs. The expected role of vaults in MDR is supported by the following evidence: (a) vaults and their components are upregulated in cells treated with cytotoxic compounds (6), (b) vaults are involved in nucleocytoplasmic transport (2,17), and (c) compounds that interact with the vaults (17). Despite these findings, until recently (18), the vault components were not shown to interact directly with chemotherapeutic compounds.…”

Section: Introductionmentioning

confidence: 80%

“…These particles represent the largest ribonucleoprotein complex identified thus far in eukaryotic cells. They seem to shuttle between the cytoplasm and the nucleus (2), and hence have been implicated in intracellular (3) and nucleocytoplasmic transport (2,3). They are widely distributed in eukaryotic species, including mammals, avians, and amphibians.…”

Section: Introductionmentioning

confidence: 99%

Expression of Noncoding Vault RNA in Human Malignant Cells and Its Importance in Mitoxantrone Resistance

Gopinath

Wadhwa

Kumar

2010

Molecular Cancer Research

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Several noncoding RNAs do vital cellular functions, including gene regulation and cell differentiation. Previously, we reported that vault RNA (vRNA) has the ability to recognize chemotherapeutic compounds, such as mitoxantrone, based on biophysical and biochemical analyses. In the present study, we show that human glioblastoma-, leukemia-, and osteocarcinoma-derived cell lines overexpress vRNA and exhibit higher resistance toward mitoxantrone. Interestingly, when vRNA expression was suppressed by RNA interference in these cells, the resistance progressively decreased. In agreement with these findings, overexpression of vRNA-1 caused resistance to mitoxantrone. These results suggest a role of vRNA in mitoxantrone resistance in malignant cells and justify further studies on the importance and application of noncoding RNAs in cancer chemotherapeutics. Mol Cancer Res; 8(11); 1536-46. ©2010 AACR.

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“…0200-0559; diluted 1/100 for immunofluorescence and 1/1000 for Western blotting), was raised against affinity-purified nuclear extracts of human breast cancer cells of the MCF-7 cell line (Abbondanza et al 1998). Rabbit anti-ubiquitin serum Ab1690, raised against purified ubiquitin, covalently linked to keyhole-limpet hemocyanin, was purchased from Chemicon (Temecula, CA, USA).…”

Section: Antibodies and Inhibitorsmentioning

confidence: 99%

Expression and proteasomal degradation of the major vault protein (MVP) in mammalian oocytes and zygotes

Šutovský¹,

Manandhar²,

Laurinčík³

et al. 2005

Reproduction

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Major vault protein (MVP), also called lung resistance-related protein is a ribonucleoprotein comprising a major part (>70%) of the vault particle. The function of vault particle is not known, although it appears to be involved in multi-drug resistance and cellular signaling. Here we show that MVP is expressed in mammalian, porcine, and human ova and in the porcine preimplantation embryo. MVP was identified by matrix-assisted laser-desorption ionization-time-of-flight (MALDI-TOF) peptide sequencing and Western blotting as a protein accumulating in porcine zygotes cultured in the presence of specific proteasomal inhibitor MG132. MVP also accumulated in poor-quality human oocytes donated by infertile couples and porcine embryos that failed to develop normally after in vitro fertilization or somatic cell nuclear transfer. Normal porcine oocytes and embryos at various stages of preimplantation development showed mostly cytoplasmic labeling, with increased accumulation of vault particles around large cytoplasmic lipid inclusions and membrane vesicles. Occasionally, MVP was associated with the nuclear envelope and nucleolus precursor bodies. Nucleotide sequences with a high degree of homology to human MVP gene sequence were identified in porcine oocyte and endometrial cell cDNA libraries. We interpret these data as the evidence for the expression and ubiquitin-proteasome-dependent turnover of MVP in the mammalian ovum. Similar to carcinoma cells, MVP could fulfill a cell-protecting function during early embryonic development.

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Interaction of Vault Particles with Estrogen Receptor in the MCF-7 Breast Cancer Cell

Cited by 99 publications

References 55 publications

On the role of major vault protein in the resistance of senescent human diploid fibroblasts to apoptosis

On the role of major vault protein in the resistance of senescent human diploid fibroblasts to apoptosis

Expression of Noncoding Vault RNA in Human Malignant Cells and Its Importance in Mitoxantrone Resistance

Expression and proteasomal degradation of the major vault protein (MVP) in mammalian oocytes and zygotes

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