期刊
JOURNAL OF BIOMEDICINE AND BIOTECHNOLOGY
卷 -, 期 -, 页码 -出版社
HINDAWI PUBLISHING CORPORATION
DOI: 10.1155/2012/728178
关键词
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资金
- Ministero dell'Universita e della Ricerca Scientifica [PS 126-Ind]
- Regione Campania (L.R.)
- Alzheimer's Association [IIRG-09-129984, ZEN-11-201425]
- Edward N. & Della L. Thome Memorial Foundation
- National Institutes of Health (NIH) [R01AG033007]
- NATIONAL INSTITUTE ON AGING [R01AG033007] Funding Source: NIH RePORTER
A dominant mutation in the ITM2B/BRI2 gene causes familial Danish dementia (FDD) in humans. To model FDD in animal systems, a knock-in approach was recently implemented in mice expressing a wild-type and mutant allele, which bears the FDD-associated mutation. Since these FDDKI mice show behavioural alterations and impaired synaptic function, we characterized their synaptosomal proteome via two-dimensional differential in-gel electrophoresis. After identification by nanoliquid chromatography coupled to electrospray-linear ion trap tandem mass spectrometry, the differentially expressed proteins were classified according to their gene ontology descriptions and their predicted functional interactions. The Dlg4/Psd95 scaffold protein and additional signalling proteins, including protein phosphatases, were revealed by STRING analysis as potential players in the altered synaptic function of FDDKI mice. Immunoblotting analysis finally demonstrated the actual downregulation of the synaptosomal scaffold protein Dlg4/Psd95 and of the dual-specificity phosphatase Dusp3 in the synaptosomes of FDDKI mice.
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