Examine how the absence of prion protein expression could affect the cellular glycosylation enzymes during development
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ABSTRACT:
ORGANISM(S): Mus musculus
PROVIDER: GSE28935 | GEO | 2011/04/29
SECONDARY ACCESSION(S): PRJNA139889
REPOSITORIES: GEO
Similar Datasets
Project description:Dr. Wong's laboratory is interested in examining if and how the absence of prion protein expression could affect the cellular glycosylation enzymes during development. Prion protein is a glycoprotein and changes in glycosylation on the protein have been implicated in the pathogenic process. Our objective is to examine if and how the absence of prion protein expression could affect the cellular glycosylation enzymes during development. To do this, we proposed to compare and contrast the expression profile of the glycosylation enzymes in control and prion protein knockout mouse brain at the age of 2 and 82 weeks (n=3). RNA preparations from control and prion protein knockout mice brain of age ~2 and 82 weeks were sent to the Microarray Core (E). The RNA was amplified, labeled, and hybridized to GLYCOv3 microarrays.
2011-04-29 | E-GEOD-28935 | biostudies-arrayexpress
Project description:Dr. Jameson's research focus is on development and regulation of lymphocytes, especially T cells. Recent work has suggested that differential glycosylation effects the sensitivity of the T cell receptors and its coreceptors, suggesting that regulation of glycosylation may be a critical element in controlling T cell development, survival and functional activity.
2010-12-11 | GSE26012 | GEO
Project description:Bone remodeling is a tightly regulated process that engages degradation and biogenesis of the bone matrix. The process is controlled by two major cell types, bone forming cells-osteoblasts and bone-degrading cells-osteoclasts. We are interested in the bone-resorption mechanism mediated by osteoclasts and wish to identify glycosylation genes that are regulated during the formation of osteoclast cells and determine the function of glycosylation and glycan-binding proteins in the osteoclastogenesis.
2011-04-29 | GSE28937 | GEO
Project description:Prion diseases are fatal transmissible neurodegenerative conditions of humans and animals that arise through neurotoxicity induced by PrP misfolding. The cellular and molecular mechanisms of prion-induced neurotoxicity remain undefined. Understanding these processes will underpin therapeutic and control strategies for human and animal prion diseases, respectively. Prion diseases are difficult to study in their natural hosts and require the use of tractable animal models. Here we used RNA-Seq-based transcriptome analysis of prion-exposed Drosophila to probe the mechanism of prion-induced neurotoxicity. Adult Drosophila transgenic for pan neuronal expression of ovine PrP targeted to the plasma membrane exhibit a neurotoxic phenotype evidenced by decreased locomotor activity after exposure to ovine prions at the larval stage. Pathway analysis and quantitative PCR of genes differentially expressed in prion-infected Drosophila revealed up-regulation of cell cycle activity and DNA damage response, followed by down-regulation of eIF2 and mTOR signalling. Mitochondrial dysfunction was identified as the principal toxicity pathway in prion-exposed PrP transgenic Drosophila. The transcriptomic changes we observed were specific to PrP targeted to the plasma membrane since these prion-induced gene expression changes were not evident in similarly-treated Drosophila transgenic for cytosolic pan neuronal PrP expression, or in non-transgenic control flies. Collectively, our data indicate that aberrant cell cycle activity, repression of protein synthesis and altered mitochondrial function are key events involved in prion-induced neurotoxicity, and correlate with those identified in mammalian hosts undergoing prion disease. These studies highlight the use of PrP transgenic Drosophila as a genetically well-defined tractable host to study mammalian prion biology.
2020-01-31 | GSE144028 | GEO
Project description:Dr. van Kooyk's laboratory is interested in investigating the expression of glycosyltransferases in dendritic cells and the changes in expression associated with maturation. Dr. van Kooyk's laboratory is exploring the function of antigen presenting cells, such as dendritic cells (DC), that regulate viral-antigen recognition, DC trafficking and T cell binding--all processes that initiate immunity or tolerance. Essential in this is the recognition of ligands by C-type lectins and the functional consequences of differential terminal glycosylation that may regulate DC function.
2011-04-29 | GSE28933 | GEO
Project description:Prions consist of aggregates of abnormal conformers of cellular prion protein (PrPC). They propagate by recruiting host-encoded PrPC although the critical interacting proteins and the reasons for the differences in susceptibility of distinct cell lines and populations are unknown. We derived a lineage of cell lines with markedly differing susceptibilities, unexplained by PrPC expression differences, to identify such factors. We examined the transcriptomes of prion-resistant revertants, isolated from highly susceptible cells, and identified a gene expression signature associated with susceptibility. Several of these genes encode proteins with a role in extracellular matrix (ECM) remodelling, a compartment in which disease-related PrP deposits. Loss-of-function of nine of these genes significantly increased susceptibility. Remarkably, inhibition of fibronectin 1 binding to integrin α8 by RGD peptide inhibited metalloproteinases (MMP)-2/9 whilst increasing prion propagation rates. This indicates that prion replication may be controlled by MMPs at the ECM in an integrin-dependent manner.
2014-07-31 | GSE56275 | GEO
Project description:Dr. Stanley's laboratory is interested in 1) understanding the biological roles of specific classes of N-glycan in development and immunity through studies of glycosyltransferase mutant mice, 2) identifying complex binding specificities of galectins using a panel of CHO glycosylation mutants, and 3) determining how O-fucose glycans function in Notch receptor signaling and in modulating the interaction of Notch receptors with their ligands.
2011-02-04 | GSE27055 | GEO
Project description:This report describes our study of the efficacy and the potential mechanism underlying the anti-prion action of a new anti-prion compound having a glycoside structure in prion-infected cells. The study revealed involvements of two factors in the mechanism of the compound action: interferon and a microtubule nucleation activator, phosphodiesterase 4D interacting protein. In particular, phosphodiesterase 4D interacting protein was suggested to be important in regulating the trafficking or fusion of prion protein-containing vesicles or structures in cells. The findings of the study are expected to be useful not only for the elucidation of cellular regulatory mechanisms of prion protein, but also for the implication of new targets for therapeutic development. Prion-infected N167 cells were treated with either anti-prion glycoside compound (Gly-9) or control glycoside compound (Gly-14) at a dose of 5 M-NM-<g/mL for three days. Then, gene expression profiles were analyzed by DNA microarray analysis. Experiments were performed in quadruplicate.
2014-02-22 | E-GEOD-55241 | biostudies-arrayexpress
Project description:This report describes our study of the efficacy and the potential mechanism underlying the anti-prion action of a new anti-prion compound having a glycoside structure in prion-infected cells. The study revealed involvements of two factors in the mechanism of the compound action: interferon and a microtubule nucleation activator, phosphodiesterase 4D interacting protein. In particular, phosphodiesterase 4D interacting protein was suggested to be important in regulating the trafficking or fusion of prion protein-containing vesicles or structures in cells. The findings of the study are expected to be useful not only for the elucidation of cellular regulatory mechanisms of prion protein, but also for the implication of new targets for therapeutic development.
2014-02-22 | GSE55241 | GEO
Project description:A comparison of prion infected and non-infected samples from neuroblastoma cells (N2a), and a comparison of prion infected and non-infected samples from hypothalmus cells (GT1). 11 dual-color DNA-chip hybridizations of cDNAs were made. Keywords: other
2005-08-24 | GSE1803 | GEO