Heteromers of amyloid precursor protein in cerebrospinal fluid.


Por: Cuchillo-Ibañez I, Lopez-Font I, Boix-Amorós A, Brinkmalm G, Blennow K, Molinuevo JL and Sáez-Valero J

Publicada: 8 ene 2015
Resumen:
Soluble fragments of the amyloid precursor protein (APP) generated by a- and ß-secretases, sAPPa and sAPPß, have been postulated as promising new cerebrospinal fluid (CSF) biomarkers for the clinical diagnosis of Alzheimer's disease (AD). However, the capacity of these soluble proteins to assemble has not been explored and could be relevant. Our aim is to characterize possible sAPP oligomers that could contribute to the quantification of sAPPa and sAPPß in CSF by ELISA, as well as to characterize the possible presence of soluble full-length APP (sAPPf).

Filiaciones:
:
 Instituto de Neurociencias de Alicante, Universidad Miguel Hernández-CSIC, Av, Ramón y Cajal s/n, Sant Joan d'Alacant, Spain.
ISSN: 17501326





MOL NEURODEGENER
Editorial
BIOMED CENTRAL LTD, 236 GRAYS INN RD, FLOOR 6, LONDON WC1X 8HL, ENGLAND, Reino Unido
Tipo de documento: Article
Volumen: 10 Número:
Páginas: 2-2
WOS Id: 000349127800001
ID de PubMed: 25573162

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