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http://hdl.handle.net/2445/196240
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DC Field | Value | Language |
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dc.contributor.author | Ferrer, Isidro (Ferrer Abizanda) | - |
dc.contributor.author | Andrés Benito, Pol | - |
dc.contributor.author | Ausín, Karina | - |
dc.contributor.author | Cartas Cejudo, Paz | - |
dc.contributor.author | Lachén Montes, Mercedes | - |
dc.contributor.author | Río Fernández, José Antonio del | - |
dc.contributor.author | Fernández Irigoyen, Joaquín | - |
dc.contributor.author | Santamaría, Enrique | - |
dc.date.accessioned | 2023-03-30T07:22:58Z | - |
dc.date.available | 2023-07-15T05:10:26Z | - |
dc.date.issued | 2022-07-15 | - |
dc.identifier.issn | 0022-3069 | - |
dc.identifier.uri | http://hdl.handle.net/2445/196240 | - |
dc.description.abstract | The neocortex of P301S mice, used as a model of fronto-temporal lobar degeneration linked to tau mutation (FTLD-tau), and wild-type mice, both aged 9 months, were analyzed with conventional label-free phosphoproteomics and SWATH-MS (sequential window acquisition of all theoretical fragment ion spectra mass spectrometry) to assess the (phospho)proteomes. The total number of identified dysregulated phosphoproteins was 328 corresponding to 524 phosphorylation sites. The majority of dysregulated phosphoproteins, most of them hyperphosphorylated, were proteins of the membranes, synapses, membrane trafficking, membrane vesicles linked to endo- and exocytosis, cytoplasmic vesicles, and cytoskeleton. Another group was composed of kinases. In contrast, proteins linked to DNA, RNA metabolism, RNA splicing, and protein synthesis were hypophosphorylated. Other pathways modulating energy metabolism, cell signaling, Golgi apparatus, carbohydrates, and lipids are also targets of dysregulated protein phosphorylation in P301S mice. The present results, together with accompanying immunohistochemical and Western-blotting studies, show widespread abnormal phosphorylation of proteins, in addition to protein tau, in P301S mice. These observations point to dysregulated protein phosphorylation as a relevant contributory pathogenic component of tauopathies. | - |
dc.format.extent | 18 p. | - |
dc.format.mimetype | application/pdf | - |
dc.language.iso | eng | - |
dc.publisher | Lippincott, Williams & Wilkins. Wolters Kluwer Health | - |
dc.relation.isformatof | Versió postprint del document publicat a: https://doi.org/10.1093/jnen/nlac062 | - |
dc.relation.ispartof | Journal of Neuropathology and Experimental Neurology, 2022, vol. 81, num. 9, p. 696-706 | - |
dc.relation.uri | https://doi.org/10.1093/jnen/nlac062 | - |
dc.rights | (c) American Association of Neuropathologists, 2022 | - |
dc.source | Articles publicats en revistes (Biologia Cel·lular, Fisiologia i Immunologia) | - |
dc.subject.classification | Proteòmica | - |
dc.subject.classification | Citosquelet | - |
dc.subject.classification | Proteïnes quinases | - |
dc.subject.other | Proteomics | - |
dc.subject.other | Cytoskeleton | - |
dc.subject.other | Protein kinases | - |
dc.title | Dysregulated Protein Phosphorylation in a Mouse Model of FTLD-Tau | - |
dc.type | info:eu-repo/semantics/article | - |
dc.type | info:eu-repo/semantics/acceptedVersion | - |
dc.identifier.idgrec | 729257 | - |
dc.date.updated | 2023-03-30T07:22:58Z | - |
dc.rights.accessRights | info:eu-repo/semantics/openAccess | - |
Appears in Collections: | Articles publicats en revistes (Biologia Cel·lular, Fisiologia i Immunologia) Articles publicats en revistes (Institut de Bioenginyeria de Catalunya (IBEC)) Articles publicats en revistes (Institut d'lnvestigació Biomèdica de Bellvitge (IDIBELL)) |
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File | Description | Size | Format | |
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729257.pdf | 252.25 kB | Adobe PDF | View/Open |
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