Project description:Evaluation of the effect of procedural memory using the double-H maze (DH) on striatal and hippocampal transcriptome in HD R6/1 mice

2022-10-06 | GSE157099 | GEO

Memory-induced 3D chromatin architecture in Huntington's disease (HD) mice [4C-seq]

Project description:Evaluation of the effect of procedural memory using the double-H maze (DH) on striatal 3D chromatin architecture in HD R6/1 mice

2022-10-06 | GSE157076 | GEO

Neurobiological Predictors of Huntington's Disease Onset (Predict-HD)

Project description:Neurobiological Predictors of Huntington's Disease Onset (Predict-HD)

| PRJNA75985 | ENA

Hdac4 interactome in Huntington's Disease

Project description:Hdac4 has been found to modulate symptoms in Huntington's Disease (HD) mouse models through an uknown mechanism unrelated to any enzymatic activity. We investigated the protein-protein interactions to gain insight into the role of Hdac4 in HD.

2019-05-01 | PXD011845 | Pride

Progerin-induced transcriptional changes in Huntington's disease human pluripotent stem cells-derived neurons

Project description:Identification of transcriptional changes in Huntington's disease (HD) and normal (WT) human embryonic stem cells (hESC)- and induced pluripotent stem cells(iPSC)-derived striatal GABAergic neruons.

2020-01-01 | GSE111622 | GEO

Spatiotemporal proteomic profiling of Huntington's disease mice reveals widespread loss of protein function

Project description:Huntington's disease (HD) is characterized by the aggregation of polyglutamine-expanded huntingtin (HTT), proceeding from soluble oligomers to end-stage inclusions. The molecular mechanisms of how protein aggregation leads to neuronal dysfunction are not well understood. We employed mass spectrometry-based quantitative proteomics to dissect spatiotemporal mechanisms of neurodegeneration using the R6/2 mouse model of HD. We show that extensive remodeling of the soluble brain proteome correlates with changes in insoluble aggregate formation during disease progression. In-depth characterization of HTT inclusion bodies uncovered an unprecedented complexity of several hundred proteins. Sequestration to inclusions was dependent on protein expression levels and the presence of aggregation-prone amino acid sequence features, such as low-complexity regions or coiled-coil domains. Overexpression of several sequestered proteins ameliorated HTT toxicity and modified the aggregation behavior in an in vitro model of HD. Our study provides a comprehensive and spatiotemporally-resolved proteome resource of HD progression, indicating that widespread loss of protein function contributes to aggregate-mediated toxicity.

2017-11-24 | PXD004973 | Pride

GENETIC CORRECTION OF HUNTINGTON'S DISEASE PHENOTYPES IN INDUCED PLURIPOTENT STEM CELLS

Project description:Huntington's Disease (HD) is caused by a CAG expansion in the huntingtin gene. Expansion of the polyglutamine tract in the huntingtin protein results in massive cell death in the striatum of HD patients. We report that human induced pluripotent stem cells (iPSCs) derived from HD patient fibroblasts can be corrected by replacing the expanded CAG repeat with a normal repeat using homologous recombination, and that the correction persists in iPSC differentiation into DARPP-32 positive neurons in vitro and vivo. Further, correction of the HD-iPSCs normalized pathogenic HD signaling pathways (cadherin, TGF-?, BNDF, caspase activation), and reversed disease phenotypes such as susceptibility to cell death and altered mitochondrial bioenergetics in neural stem cells. The ability to make patient-specific, genetically corrected iPSCs from HD patients will provide relevant disease models in identical genetic backgrounds and is a critical step for the eventual use of these cells in cell replacement therapy. 16 experimental samples were used overall. There were 8 replicates per group, with one group being the control, and the other being the experimental. Comparison was carried out on the Nimblegen platform.

2012-06-14 | E-GEOD-37547 | biostudies-arrayexpress

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