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Neuroreport ; 11(15): 3357-60, 2000 Oct 20.
Article in English | MEDLINE | ID: mdl-11059902

ABSTRACT

There is evidence to suggest that certain metabolic fragments of the beta-amyloid precursor protein (betaAPP) containing the whole of the beta-amyloid (Abeta) sequence are toxic to cells. We showed previously that the 105-amino acid C-terminal peptide (CT105) fragment, incorporating Abeta, is particularly toxic to Xenopus oocytes as well as to mammalian neurons. Here, we investigated the contributions of Na+ and Ca2+ gradients to intracellular CT105-induced toxicity in oocytes, monitored by measuring the membrane resting potential. The concentration gradients of Na+ and Ca2+ were manipulated to determine the involvement of the trans-membrane concentration gradients of these ions in the mode of action of CT105. The results suggested that Na+ influx and intracellular events are mainly responsible for the observed CT105-induced toxicity.


Subject(s)
Amyloid beta-Protein Precursor/poisoning , Calcium/metabolism , Sodium/metabolism , Animals , Female , Isotonic Solutions , Magnesium/pharmacology , Membrane Potentials/drug effects , Oocytes/drug effects , Oocytes/physiology , Osmolar Concentration , Peptide Fragments/poisoning , Ringer's Solution , Xenopus
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