Cell surface nucleolin is a novel ADAMTS5 receptor mediating endothelial cell apoptosis
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PROVIDER: PRJNA789689 | ENA |
REPOSITORIES: ENA
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Project description:This study demonstrates that TS5-p45 induces endothelial cell (EC) apoptosis in a caspase-dependent manner via its cell surface receptor Nucleolin (NCL). To unravel how this apoptosis mechanism is induced in ECs, we performed RNA-seq using TS5-p45-treated ECs. Transcriptional changes under TS5-p45 treatment was further evaluated to highlight some of the caspase-dependent apoptosis-inducing and -suppressing genes which are altered in favor of apoptosis.
2022-03-02 | GSE191049 | GEO
Project description:C1QTNF4 is a secreted protein that is structurally unique within the C1QTNF family, a family of proteins that have structural homology with both complement C1q and the tumor necrosis factor superfamily. The role of C1QTNF4 in immunity and inflammation remains poorly defined and a cell surface receptor has yet to be identified. Here we performed co-immunoprecipitation with subsequent mass spectrometric analysis in order to identify a cell surface receptor of C1QTNF4. We report identification of nucleolin as a cell surface binding partner of C1QTNF4. Nucleolin may serve as a docking molecule for C1QTNF4 and act in a context-dependent manner through co-receptors. Having identified nucleolin as a cell surface receptor is a further step to understanding C1QTNF4’s function in the healthy immune system.
2021-03-21 | PXD023088 | Pride
Project description:Retinoblastoma (RB) is an intraocular childhood tumor which, if left untreated, leads to blindness and mortality. Nucleolin (NCL) protein which is differentially expressed on the tumor cell surface, binds ligands and regulates carcinogenesis and angiogenesis. We found that NCL is over expressed in RB tumor tissues and cell lines compared to normal retina. We studied the effect of nucleolin-aptamer (NCL-APT) to reduce proliferation in RB tumor cells. Aptamer treatment on the RB cell lines (Y79 and WERI-Rb1) led to significant inhibition of cell proliferation. Locked nucleic acid (LNA) modified NCL-APT administered subcutaneously (s.c.) near tumor or intraperitoneally (i.p.) in Y79 xenografted nude mice resulted in 26 and 65% of tumor growth inhibition, respectively. Downregulation of inhibitor of apoptosis proteins, tumor miRNA-18a, altered serum cytokines, and serum miRNA-18a levels were observed upon NCL-APT treatment. Desorption electrospray ionization mass spectrometry (DESI MS)-based imaging of cell lines and tumor tissues revealed changes in phosphatidylcholines levels upon treatment. Thus, our study provides proof of concept illustrating NCL-APT-based targeted therapeutic strategy and use of DESI MS-based lipid imaging in monitoring therapeutic responses in RB.
2016-11-15 | GSE89818 | GEO
Project description:TRA2β4 is transcribed from the human transformer 2β(TRA2B) gene and overexpressed in colon cancer cells. Nucleolin is one of RNA-binding proteins to regulate cell survival and proliferation. In this study, TRA2β4 and Nucleolin levels were reduced in colon cancer HCT116 cells and gene expression levels were measured using microarray analysis.
2018-04-06 | GSE112758 | GEO
Project description:To further explore the function and underlying mechanism of nucleolin in embryonic stem cells (ESCs), we compared the transcription profile of tetracycline (Tc)-inducible EGFP (as a control) or nucleolin siRNA expression-stable ESCs cultured with or without Tc for 3 days, and identified distinct classes of up- and down-regulated genes by nucleolin in mouse ESCs. Total RNA obtained from CGR8 ES cells stably integrated with Tc-inducible siRNA EGFP, nucleoin-1 or nucleolin-2 cultured with or without Tc for 3 days, and then hybridized to Illumina Sentrix Mouse-6 v2.0 BeadChips. Three replicates each condition.
2011-10-19 | E-GEOD-23993 | biostudies-arrayexpress
Project description:Although Rrp6 contains a helicase and RNase D domain at the C-terminus, it is not involved in stable RNA interactions. We thus hypothesized that mRrp6-mediated nucleolar inflammatory RNA degradation may depend on the pre-mRNA substrate that is delivered to the mRrp6-exosome complex by nucleolin as a guide factor. To demonstrate this possibility, we examined nucleoplasmic RNAs which were bound to nucleolin through RNA-IP-sequencing at the late time points of LPS stimulation.
2021-02-28 | GSE95528 | GEO
Project description:To further explore the function and underlying mechanism of nucleolin in embryonic stem cells (ESCs), we compared the transcription profile of tetracycline (Tc)-inducible EGFP (as a control) or nucleolin siRNA expression-stable ESCs cultured with or without Tc for 3 days, and identified distinct classes of up- and down-regulated genes by nucleolin in mouse ESCs.
2011-10-20 | GSE23993 | GEO
Project description:We previously showed that the RNA binding protein Nucleolin is localized to axons of DRG sensory neurons by interaction with the molecular motor Kinesin-1 (Kif5A) and subsequently localizes importin beta1 mRNA there (Perry et al., 2016). In this work, we created a mouse with a heterozygous deletion of the domain in nucleolin responsible for the Kif5A interaction and showed that nucelolin protein levels are reduced in the axons of dorsal root ganglia neurons in this mouse model. The goal of this study was to identify RNAs who's axonal localization is affected by this perturbation.
2021-07-23 | GSE142096 | GEO
Project description:Reducing sugars can covalently react with proteins to generate a heterogeneous and complex group of compounds called advanced glycation end products (AGEs). AGEs are generally considered as pathogenic molecules, mediating a pro-inflammatory response and contributing to the development of a number of human diseases. However, the intrinsic function of AGEs remains to be elucidated. We now provide multiple lines of evidence showing that AGEs can specifically bind a cell-surface protein and regulate its functions. To identify cellular binding partners for AGEs, we used dehydroascorbic acid (DHA)-modified serum albumins as one of the AGEs to screen for binding proteins in the lipid raft fraction prepared from mouse splenocytes and identified histone localized on the cell-surface as an AGE-binding protein. Histone ubiquitously recognized AGEs, including proteins modified with glucose and its metabolites. AGEs inhibited the binding of plasminogen to the histone component H2B which functions as a cell-surface plasminogen receptor on monocytes/macrophages. Moreover, AGEs regulated the recruitment of monocytes/macrophage to the site of inflammation. Our discovery of histone as a cell-surface receptor for AGEs suggests that, beside our common concept of AGEs as danger-associated molecular patterns mediating a pro-inflammatory response, they may also be involved in the homeostatic response via binding to histone.
2022-03-31 | GSE195558 | GEO
Project description:Binding of Nucleolin to HBV cccDNA
| PRJNA509631 | ENA