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http://hdl.handle.net/2445/187446
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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 | Rio, José Antonio del | - |
dc.contributor.author | Fernández Irigoyen, Joaquín | - |
dc.contributor.author | Santamaría, Enrique | - |
dc.date.accessioned | 2022-07-07T12:55:32Z | - |
dc.date.available | 2022-07-07T12:55:32Z | - |
dc.date.issued | 2022-06-08 | - |
dc.identifier.issn | 1422-0067 | - |
dc.identifier.uri | http://hdl.handle.net/2445/187446 | - |
dc.description.abstract | Altered protein phosphorylation is a major pathologic modification in tauopathies and Alzheimer's disease (AD) linked to abnormal tau fibrillar deposits in neurofibrillary tangles (NFTs) and pre-tangles and beta-amyloid deposits in AD. hTau transgenic mice, which express 3R and less 4R human tau with no mutations in a murine knock-out background, show increased tau deposition in neurons but not NFTs and pre-tangles at the age of nine months. Label-free (phospho)proteomics and SWATH-MS identified 2065 proteins in hTau and wild-type (WT) mice. Only six proteins showed increased levels in hTau; no proteins were down-regulated. Increased tau phosphorylation in hTau was detected at Ser199, Ser202, Ser214, Ser396, Ser400, Thr403, Ser404, Ser413, Ser416, Ser422, Ser491, and Ser494, in addition to Thr181, Thr231, Ser396/Ser404, but not at Ser202/Thr205. In addition, 4578 phosphopeptides (corresponding to 1622 phosphoproteins) were identified in hTau and WT mice; 64 proteins were differentially phosphorylated in hTau. Sixty proteins were grouped into components of membranes, membrane signaling, synapses, vesicles, cytoskeleton, DNA/RNA/protein metabolism, ubiquitin/proteasome system, cholesterol and lipid metabolism, and cell signaling. These results showed that over-expression of human tau without pre-tangle and NFT formation preferentially triggers an imbalance in the phosphorylation profile of specific proteins involved in the cytoskeletal-membrane-signaling axis. | - |
dc.format.extent | 15 p. | - |
dc.format.mimetype | application/pdf | - |
dc.language.iso | eng | - |
dc.publisher | MDPI AG | - |
dc.relation.isformatof | Reproducció del document publicat a: https://doi.org/10.3390/ijms23126427 | - |
dc.relation.ispartof | International Journal of Molecular Sciences, 2022, vol. 23, num. 12 | - |
dc.relation.uri | https://doi.org/10.3390/ijms23126427 | - |
dc.rights | cc by (c) Ferrer, Isidro (Ferrer Abizanda) et al, 2022 | - |
dc.rights.uri | http://creativecommons.org/licenses/by/3.0/es/ | * |
dc.source | Articles publicats en revistes (Institut d'lnvestigació Biomèdica de Bellvitge (IDIBELL)) | - |
dc.subject.classification | Malaltia d'Alzheimer | - |
dc.subject.classification | Proteïnes | - |
dc.subject.other | Alzheimer's disease | - |
dc.subject.other | Proteins | - |
dc.title | Dysregulated Brain Protein Phosphorylation Linked to Increased Human Tau Expression in the hTau Transgenic Mouse Model | - |
dc.type | info:eu-repo/semantics/article | - |
dc.type | info:eu-repo/semantics/publishedVersion | - |
dc.date.updated | 2022-07-07T10:52:15Z | - |
dc.rights.accessRights | info:eu-repo/semantics/openAccess | - |
dc.identifier.pmid | 35742871 | - |
Appears in Collections: | Articles publicats en revistes (Institut d'lnvestigació Biomèdica de Bellvitge (IDIBELL)) Articles publicats en revistes (Institut de Bioenginyeria de Catalunya (IBEC)) |
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File | Description | Size | Format | |
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ijms-23-06427-v2.pdf | 1.09 MB | Adobe PDF | View/Open |
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