PC12 cells transfected with a C-terminal fragment of the amyloid precursor protein (APP C-100), exhibit enhanced sensitivity to the calcium ionophore A23187, and diminished sensitivity to hydrogen peroxide

Extracellular neuritic plaques are a hallmark of Alzheimer's disease. The core protein of plaques is Aβ, a 39–43 amino acid peptide derived from the amyloid precursor protein (APP). APP C-100 is a C-terminal fragment of APP, 100 amino acids long, whose sequence includes Aβ. To determine whether...

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Veröffentlicht in:Brain research. Molecular brain research. 1999-09, Vol.72 (1), p.103-107
Hauptverfasser: McKeon-O'Malley, Catherine, Wells, John, Fine, Richard, Ullman, M.David, Volicer, Ladislav
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Sprache:eng
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Zusammenfassung:Extracellular neuritic plaques are a hallmark of Alzheimer's disease. The core protein of plaques is Aβ, a 39–43 amino acid peptide derived from the amyloid precursor protein (APP). APP C-100 is a C-terminal fragment of APP, 100 amino acids long, whose sequence includes Aβ. To determine whether APP C-100 expression alters cellular vulnerability to calcium and H 2O 2, rat PC12 cells were modified to overexpress APP C-100. Cellular survival (as measured in the MTT assay) was determined as a function of concentration for the calcium ionophore, A23187, and for H 2O 2 in APP C-100 transfectants and vector-transfected controls. APP C-100 expression significantly increased cellular vulnerability to A23187, and decreased vulnerability to H 2O 2.
ISSN:0169-328X
1872-6941
DOI:10.1016/S0169-328X(99)00228-4