About: Proteomics reveal energy metabolism and mitogen-activated protein kinase signal transduction perturbation in human Borna disease virus Hu-H1-infected oligodendroglial cells

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About: Proteomics reveal energy metabolism and mitogen-activated protein kinase signal transduction perturbation in human Borna disease virus Hu-H1-infected oligodendroglial cells Goto Sponge NotDistinct Permalink

An Entity of Type : schema:ScholarlyArticle, within Data Space : covidontheweb.inria.fr associated with source document(s)

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	Proteomics reveal energy metabolism and mitogen-activated protein kinase signal transduction perturbation in human Borna disease virus Hu-H1-infected oligodendroglial cells
Creator	Wang, X Yang, Y Zhang, L Zhou, J Bode, L Huang, R Liu, S Liu, X Lv, L Pan, J Xie, P Zhan, Y Zhao, M
Source	Elsevier; Medline; PMC
abstract	Abstract Borna disease virus (BDV) is a neurotropic, non-cytolytic RNA virus which replicates in the cell nucleus targeting mainly hippocampal neurons, but also astroglial and oligodendroglial cells in the brain. BDV is associated with a large spectrum of neuropsychiatric pathologies in animals. Its relationship to human neuropsychiatric illness still remains controversial. We could recently demonstrate that human BDV strain Hu-H1 promoted apoptosis and inhibited cell proliferation in a human oligodendroglial cell line (OL cells) whereas laboratory BDV strain V acted contrariwise. Here, differential protein expression between BDV Hu-H1-infected OL cells and non-infected OL cells was assessed through a proteomics approach, using two-dimensional electrophoresis followed by matrix-assisted laser desorption ionization-time of flight tandem mass spectrometry. A total of 63 differential host proteins were identified in BDV Hu-H1-infected OL cells compared to non-infected OL cells. We found that most changes referred to alterations related to the pentose phosphate pathway, glyoxylate and dicarboxylate metabolism, the tricarboxylic acid (TCA) cycle, and glycolysis /gluconeogenesis. By manual querying, two differential proteins were found to be associated with mitogen-activated protein kinase (MAPK) signal transduction. Five key signaling proteins of this pathway (i.e., p-Raf, p-MEK, p-ERK1/2, p-RSK, and p-MSK) were selected for Western blotting validation. p-ERK1/2 and p-RSK were found to be significantly up-regulated, and p-MSK was found to be significantly down-regulated in BDV Hu-H1-infected OL cells compared to non-infected OL cell. Although BDV Hu-H1 constitutively activated the ERK–RSK pathway, host cell proliferation and nuclear translocation of activated pERK in BDV Hu-H1-infected OL cells were impaired. These findings indicate that BDV Hu-H1 infection of human oligodendroglial cells significantly perturbs host energy metabolism, activates the downstream ERK–RSK complex of the Raf/MEK/ERK signaling cascade, and disturbs host cell proliferation possibly through impaired nuclear translocation of pERK, a finding which warrants further research.
has issue date	2014-05-30(xsd:dateTime)
bibo:doi	10.1016/j.neuroscience.2014.03.009
bibo:pmid	24637096
has license	els-covid
sha1sum (hex)	52a89d91ec1861a7a366272f18e7825426bc41f4
schema:url	https://doi.org/10.1016/j.neuroscience.2014.03.009
resource representing a document's title	Proteomics reveal energy metabolism and mitogen-activated protein kinase signal transduction perturbation in human Borna disease virus Hu-H1-infected oligodendroglial cells
has PubMed Central identifier	PMC7116963
has PubMed identifier	24637096
schema:publication	Neuroscience
resource representing a document's body	covid:52a89d91ec1861a7a366272f18e7825426bc41f4#body_text
is schema:about of	named entity 'human' named entity 'demonstrate' named entity 'astroglial' named entity 'MAPK' named entity 'replicates' named entity 'pathologies' named entity 'mitogen-activated protein kinase' named entity 'cells' named entity 'protein' named entity 'cells' named entity 'MITOGEN-ACTIVATED' covid:arg/52a89d91ec1861a7a366272f18e7825426bc41f4 named entity 'Borna' named entity 'hippocampal' named entity 'cells' named entity 'cells' named entity 'large' named entity 'animals' named entity 'cell proliferation' named entity 'astroglial' named entity 'neurotropic' named entity 'cell nucleus' named entity 'BDV' named entity 'BDV' named entity 'neuropsychiatric' named entity 'mitogen-activated protein kinase' named entity 'glycolysis' named entity 'pathologies' named entity 'MAPK' named entity 'oligodendroglial' named entity 'proteomics' named entity 'astroglia' named entity '1:200' named entity 'apoptosis' named entity 'neuropsychiatric disorders' named entity 'ketose' named entity 'PVY' named entity 'MEK/ERK' named entity 'pentose phosphate pathway' named entity 'mitochondrial' named entity 'MAPK' named entity 'antibodies' named entity 'autolysis' named entity 'BDV' named entity 'signaling proteins' named entity 'metabolic' named entity 'down-regulation' named entity 'protein' named entity 'infection' named entity 'up-regulated' named entity 'aldose' named entity 'oligodendrocytes' named entity 'glyoxylate and dicarboxylate metabolism' named entity 'Beverly, MA' named entity 'catalyzes' named entity 'phosphate' named entity 'serum' named entity 'pentose phosphate pathway' named entity 'Raf' named entity 'aconitate hydratase' named entity 'fetal' named entity 'Bio-Rad' named entity 'metabolic pathways' named entity 'enolase 1' named entity 'xylulose-5-phosphate' named entity 'BDV' named entity 'phosphoglucomutase' named entity 'Immunofluorescence' named entity 'MSK'

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