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Expression data from rat organotypic hippocampal slices lentivirally infected with shRNF10 or scramble construct

ABSTRACT: RNF10 is a synapse-to-nucleus protein messsenger regulating NMDAR-dependent gene trascription. We have charaterized the impact of the absence of RNF10 on structural synaptic plasticity. In this dataset we included expression data from homogenates of DIV14 rat organotypic hippocampal slices lentivirally infected with shRNF10 or scramble construct

ORGANISM(S): Rattus norvegicus

PROVIDER: GSE69267 | GEO | 2015/06/20

SECONDARY ACCESSION(S): PRJNA285054

REPOSITORIES: GEO

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Expression data from rat organotypic hippocampal slices lentivirally infected with shRNF10 or scramble construct

Project description:RNF10 is a synapse-to-nucleus protein messsenger regulating NMDAR-dependent gene trascription. We have charaterized the impact of the absence of RNF10 on structural synaptic plasticity. In this dataset we included expression data from homogenates of DIV14 rat organotypic hippocampal slices lentivirally infected with shRNF10 or scramble construct 8 total samples were analyzed (4 shRNF10 and 4 scramble).

2015-06-20 | E-GEOD-69267 | biostudies-arrayexpress

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NMDA glutamate receptor antagonist MK-801 induces proteome changes in adult human brain slices which are partially counteracted by haloperidol and clozapine

Project description:Deciphering the molecular pathways associated with N-methyl-D-aspartate receptor (NMDAr) hypofunction and its interaction with antipsychotics is necessary to advance our understanding of the basis of schizophrenia, as well as our capacity to treat this disease. In this regard, the development of human brain-derived models amenable for studying the neurobiology of schizophrenia may contribute to fill the gaps led by the widely employed animal models. Here we assessed the proteomic changes induced by the NMDA glutamate receptor antagonist MK-801 on human brain slice cultures obtained from adult donors submitted to resective neurosurgery. Initially, we demonstrated that MK-801 diminishes NMDA glutamate receptor signaling in human brain slices in culture. Next, using mass- spectrometry-based proteomics and systems biology in silico analyses, we found that MK-801 led to alterations in proteins related to several pathways previously associated with schizophrenia pathophysiology including ephrin, opioid, melatonin, sirtuin signaling, interleukin 8, endocannabinoid and synaptic vesicle cycle. We also evaluated the impact of both typical and atypical antipsychotics on MK-801-induced proteome changes. Interestingly, the atypical antipsychotic clozapine showed a more significant capacity to counteract the protein alterations induced by NMDAr hypofunction than haloperidol. Finally, using our dataset we identified potential modulators of the MK-801-induced proteome changes, which may be considered promising targets to treat NMDAr hypofunction in schizophrenia.

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Neocortical Slices of Human Tissue

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Project description:Cultured organotypic cerebellar slices were exposed for different time points with either prions (RML) versus non-infectious brain homogenate (NBH) or ligands to the globular domain of the prion protein (POM1) vs IgG We used microarrays to characterize the temporal response of two inducers prion protein dependent cell death: COCS were exposed to RML prions or Non-infectious brain homogenate (NBH) and harvested after 14d, 25d, 38d and 45d (4 replicates each condition). COCS were exposed to POM1 or IgG and harvested after 8h, 1d, 3d, 7d, 10d (4 replicates each condition).

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Neocortical Slices of Human Tissue

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Project description:Methods enabling prion replication ex vivo are important for advancing prion studies. However, few such technologies exist, and many prion strains are not amenable to them. Here we describe a prion organotypic slice culture assay (POSCA) that allows prion amplification and titration ex vivo under conditions that closely resemble intracerebral infection. Thirty-five days after contact with prions, mouse cerebellar slices had amplified the abnormal isoform of prion protein, PrP(Sc), >10(5)-fold. This is quantitatively similar to amplification in vivo, but fivefold faster. PrP(Sc) accumulated predominantly in the molecular layer, as in infected mice. The POSCA detected replication of prion strains from disparate sources, including bovines and ovines, with variable detection efficiency. Pharmacogenetic ablation of microglia from POSCA slices led to a 15-fold increase in prion titers and PrP(Sc) concentrations over those in microglia-containing slices, as well as an increase in susceptibility to infection. This suggests that the extensive microglial activation accompanying prion diseases represents an efficacious defensive reaction.

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