Beta-amyloid-induced activation of caspase-3 in primary cultures of rat neurons |
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Authors: | Marín N Romero B Bosch-Morell F Llansola M Felipo V Romá J Romero F J |
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Affiliation: | Neurophysiology and Neurotoxicology Unit, Department of Physiology, School of Medicine and Dentistry, University of Valencia, Av. Blasco Iba?ez 17, E-46010, Valencia, Spain. |
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Abstract: | It is known that beta-amyloid peptide (Abeta) contributes to the neurodegeneration in Alzheimer's disease (AD) and operates through activation of an apoptotic pathway. Apoptotic signal is driven by a family of cysteine proteases called caspases. The beta-amyloid precursor protein (APP) is directly and efficiently cleaved by caspases during apoptosis, resulting in elevated beta-amyloid peptide formation. Cerebellar neurons from rat pups were treated with the aged Abeta(25-35) at 1 and 5 microM and fluorescence assays of caspase activity performed over 4 days. We observed an increase in caspase activity after 48 h treatment in both 1 and 5 microM treated cells, then (72-96 h) caspase activity decreased to control values. The data presented support the hypothesis that Abeta(25-35)-induced apoptosis is mediated by the activation of Caspase-3 and that this is a transient effect. |
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