Glycosilated nucleolin as marker for human gliomas

Galzio, Renato; Rosati, Floriana; Benedetti, Elisabetta; Cristiano, Loredana; Aldi, Silvia; Mei, Stefania; D’Angelo, Barbara; Gentile, Roberta; Laurenti, Giulio; Cifone, Maria Grazia; Giordano, Antonio; Cimini, Annamaria

doi:10.1002/jcb.23381

Cited by 50 publications

(55 citation statements)

References 36 publications

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“…Recently, nucleolin was also found to be present on the cell surface in a wide range of cells (Galzio et al, 2012) and serve as receptors for HIV-1, ECM, adhesion molecules and growth factors Wang et al, 2011). Consistent with these reports, our results showed that nucleolin exists in the membrane fraction of A375 cells (Fig.…”

Section: Discussionsupporting

confidence: 92%

Identification of Nucleolin as a Lipid-Raft-Dependent β1-Integrin-Interacting Protein in A375 Cell Migration

Wang

Zhang

et al. 2013

Molecules and Cells

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Lipid rafts are related to cell surface receptor function. Integrin is a major surface receptor protein in cell adhesion and migration on the extracellular matrix (ECM). Here, we showed that lipid rafts played a critical role in human melanoma A375 cell spreading and migration on fibronectin; an important component of the ECM that interacts with β1 integrin. We found that the disruption of lipid rafts did not markedly inhibit the expression and activation of β1 integrin. By coimmunoprecipitation and mass spectrometry, we investigated the influence of lipid rafts on the β1 integrin complex and identified nucleolin as a potential lipid-raft-dependent β1-integrin-interacting protein. Upon confirmation of the interaction between β1 integrin and nucleolin, further studies revealed that nucleolin colocalized with β1 integrin in lipid rafts and raft disruption interrupted their association. In addition, knockdown of nucleolin markedly attenuated A375 cell spreading and migration on fibronectin. Taken together, we demonstrated that nucleolin is a critical lipid-raft-dependent β1-integrin-interacting protein in A375 cell spreading and migration on fibronectin.

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Section: Discussionsupporting

confidence: 92%

Identification of Nucleolin as a Lipid-Raft-Dependent β1-Integrin-Interacting Protein in A375 Cell Migration

Wang

Zhang

et al. 2013

Molecules and Cells

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“…Nucleolin over expression is related with increased cell proliferation. Cell surface nucleolin is found in a wide range of tumor cells, and it is used as a marker for cancer diagnosis [15, 16]. Increased levels of cytoplasmic and cell-surface nucleolin have been demonstrated to correlate with malignancy grade and proliferation rate in glioblastoma [15].…”

Section: Introductionmentioning

confidence: 99%

Interfering with the interaction between ErbB1, nucleolin and Ras as a potential treatment for glioblastoma

et al. 2014

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The three oncogenes, ErbB receptors, Ras proteins and nucleolin may contribute to malignant transformation. Previously, we demonstrated that nucleolin could bind both Ras protein and ErbB receptors. We also showed that the crosstalk between the three proteins facilitates anchorage independent growth and tumor growth in nude mice, and that inhibition of this interaction in prostate and colon cancer cells reduces tumorigenicity. In the present study, we show that treatment with Ras and nucleolin inhibitors reduces the oncogenic effect induced by ErbB1 receptor in U87-MG cells. This combined treatment enhances cell death, reduces cell proliferation and cell migration. Moreover, we demonstrate a pivotal role of nucleolin in ErbB1 activation by its ligand. Nucleolin inhibitor prevents EGF-induced receptor activation and its downstream signaling followed by reduced proliferation. Furthermore, inhibition of Ras by Salirasib (FTS), mainly reduces cell viability and motility. The combined treatment, which targets both Ras and nucleolin, additively reduces tumorigenicity both in vitro and in vivo. These results suggest that targeting both nucleolin and Ras may represent an additional opportunity for inhibiting cancers, including glioblastoma, that are driven by these oncogenes.

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“…Subsequently, the phosphorylated Smad complex is linked into Smad4 and then shuttled into the cell nucleus, where the complex initiates the corresponding gene transcription and protein expression [6][7][8]. At the same time, C23 protein is reported to express in the different subcellular structures of cancer cell [9][10][11], such as colorectal cancer [12] and gliomas [14]. Notably, C23 is demonstrated to influence some receptor-mediated signaling pathways [15].…”

Section: Introductionmentioning

confidence: 96%

C23 protein meditates bone morphogenetic protein-2-mediated EMT via up-regulation of Erk1/2 and Akt in gastric cancer

2015

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In our previous study, the epithelial-to-mesenchymal transition (EMT) has been identified to be involved in gastric cancer progression. Notably, nuclear protein C23 and bone morphogenetic protein-2 (BMP2) have been linked into EMT. However, the specific mechanisms underlying BMP2 pathway-mediated EMT are not still unraveled. In this study, we adopted immunohistochemistry and immunoblotting to determine the expression of C23 and BMP2 receptor II (BMPR-II) in 90 gastric cancer samples and cell lines. Subsequently, relevant cell lines were selected to be treated with si-C23 or si-BMPRII and the detection of in vitro assay. Our results revealed that both C23 and BMPRII were aberrantly and constitutively expressed in gastric cancer specimens and cell lines, whose expression was positively associated with metastasis, stage and differentiation, and portended poor survival outcome of gastric cancer patients. In vitro assay validated the increased expression of p-Erk1/2, p-Akt, vimentin, N-cadherin, and MMP2 in BMP2-stimulated MGC803 cells, which was in a dose-dependent manner. By contrast, si-C23 treatment attenuated the BMP2-stimulated expression of p-Erk1/2, p-Akt, vimentin, N-cadherin, and MMP2. Also, the treatment of either si-C23 or si-BMPRII decreased the ability of migration and invasion of MGC803 cells. In conclusion, C23 mediates BMP2-induced EMT progression via the up-regulation of Erk1/2 and Akt signaling pathway in gastric cancer, which indicated both C23 and BMPRII pathway could be recommended as prospective targets or biomarkers to antagonize the progression of gastric cancer.

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Glycosilated nucleolin as marker for human gliomas

Cited by 50 publications

References 36 publications

Identification of Nucleolin as a Lipid-Raft-Dependent β1-Integrin-Interacting Protein in A375 Cell Migration

Identification of Nucleolin as a Lipid-Raft-Dependent β1-Integrin-Interacting Protein in A375 Cell Migration

Interfering with the interaction between ErbB1, nucleolin and Ras as a potential treatment for glioblastoma

C23 protein meditates bone morphogenetic protein-2-mediated EMT via up-regulation of Erk1/2 and Akt in gastric cancer

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