Small-molecule aggregation inhibitors reduce excess amyloid in a trisomy 16 mouse cortical cell line

• ANDRÉA C PAULA LIMA ^[1] ; CHRISTIAN ARRIAGADA ^[2] ; RODRIGO TORO ^[3] ; ANA MARÍA CÁRDENAS ^[3] ; RAÚL CAVIEDES ^[2] ; SERGIO T FERREIRA ^[1] ; PABLO CAVIEDES ^[2]
  1. [1] Universidade Federal do Rio de Janeiro

     Universidade Federal do Rio de Janeiro

     Brasil

     
  2. [2] Universidad de Chile

     Universidad de Chile

     Santiago, Chile

     
  3. [3] Universidad de Valparaíso

     Universidad de Valparaíso

     Valparaíso, Chile

     

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• Localización: Biological Research, ISSN-e 0717-6287, ISSN 0716-9760, Vol. 41, Nº. 2, 2008, págs. 129-136
• Idioma: inglés
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• Resumen

  • We have previously characterized a number of small molecule organic compounds that prevent the aggregation of the β-amyloid peptide and its neurotoxicity in hippocampal neuronal cultures. We have now evaluated the effects of such compounds on amyloid precursor protein (APP) accumulation in the CTb immortalized cell line derived from the cerebral cortex of a trisomy 16 mouse, an animal model of Down's syndrome. Compared to a non-trisomic cortical cell line (CNh), CTb cells overexpress APP and exhibit slightly elevated resting intracellular Ca2+ levéis ([Ca2+]¡). Here, we show that the compounds 2,4-dinitrophenol, 3-nitrophenol and 4-anisidine decreased intracellular accumulation of APP in CTb cells. Those compounds were non-toxic to the cells, and slightly increased the basal [Ca2+]¡. Results indícate that the compounds tested can be leads for the development of drugs to decrease intracellular vesicular accumulation of APP in trisomic cells.