http://www.cnr.it/ontology/cnr/individuo/prodotto/ID188136
Proteomic characterization of a mouse model of familial Danish dementia. (Articolo in rivista)
- Type
- Label
- Proteomic characterization of a mouse model of familial Danish dementia. (Articolo in rivista) (literal)
- Anno
- 2012-01-01T00:00:00+01:00 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
- 10.1155/2012/728178 (literal)
- Alternative label
Vitale M, Renzone G, Matsuda S, Scaloni A, D'Adamio L, Zambrano N. (2012)
Proteomic characterization of a mouse model of familial Danish dementia.
in Journal of Biomedicine and Biotechnology (Print); Hindawi Publishing Corporation, Cairo (Egitto)
(literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
- Vitale M, Renzone G, Matsuda S, Scaloni A, D'Adamio L, Zambrano N. (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#url
- http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3350990/ (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
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- Note
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- Dipartimento di Biochimica e Biotecnologie Mediche, Universita degli Studi di Napoli Federico II, 80131 Napoli, Italy
CEINGE Biotecnologie Avanzate, 80145 Napoli, Italy
Proteomics and Mass Spectrometry Laboratory, ISPAAM, National Research Council, 80147 Napoli, Italy
Department of Microbiology and Immunology, Albert Einstein College of Medicine, Bronx, NY 10462, USA (literal)
- Titolo
- Proteomic characterization of a mouse model of familial Danish dementia. (literal)
- Abstract
- 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 FDD(KI) 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 FDD(KI) 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 FDD(KI) mice. (literal)
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