Apoptosis is induced by β-amyloid in cultured central nervous system neurons. Alzheimer's disease (AD) is characterized by neurodegeneration, and β-amyloid peptide (AβP) is implicated in this process. This study shows that synthetic AβP triggers neuronal degeneration through an apoptotic pathway. Cultured neurons exposed to AβP exhibit morphological and biochemical features of apoptosis, including membrane blebbing, nuclear chromatin condensation, and internucleosomal DNA fragmentation. An inhibitor of nucleases, aurintricarboxylic acid, prevents DNA fragmentation and delays cell death, suggesting that apoptosis may contribute to neuronal loss in AD. β-amyloid accumulation in senile plaques is a key feature of AD pathology. AβP deposits are associated with dystrophic neurites and neuronal loss in affected brain regions. Mutations in the AβP precursor protein (AβPP) are linked to familial AD, and these mutations may promote AβP production. In vitro and in vivo studies support the hypothesis that AβP directly contributes to neurodegeneration in AD. In primary neuronal cultures, AβP aggregates induce dystrophic neurite morphology and neuronal loss. In vivo studies show that intracerebral injection of AβP induces neuronal degeneration in adult rats and aged primates. Cell death can occur through necrosis or apoptosis. Apoptosis is a regulated form of cell death that functions in development and tissue homeostasis. Neurons undergoing apoptosis exhibit characteristic features such as membrane blebbing, nuclear condensation, and DNA fragmentation. In this study, AβP-treated neurons showed these features, indicating apoptosis. Electron microscopy and DNA fragmentation analysis confirmed ultrastructural and biochemical changes consistent with apoptosis. The study demonstrates that AβP induces apoptosis in cultured neurons, suggesting a role for apoptosis in neuronal loss in AD. The findings indicate that AβP may contribute to neurodegeneration through an apoptotic pathway, and that this process may be influenced by factors such as calcium homeostasis and protein synthesis. The results suggest that apoptosis may play a role in the progression of AD, and that understanding the apoptotic pathway may lead to strategies for delaying neurodegeneration.Apoptosis is induced by β-amyloid in cultured central nervous system neurons. Alzheimer's disease (AD) is characterized by neurodegeneration, and β-amyloid peptide (AβP) is implicated in this process. This study shows that synthetic AβP triggers neuronal degeneration through an apoptotic pathway. Cultured neurons exposed to AβP exhibit morphological and biochemical features of apoptosis, including membrane blebbing, nuclear chromatin condensation, and internucleosomal DNA fragmentation. An inhibitor of nucleases, aurintricarboxylic acid, prevents DNA fragmentation and delays cell death, suggesting that apoptosis may contribute to neuronal loss in AD. β-amyloid accumulation in senile plaques is a key feature of AD pathology. AβP deposits are associated with dystrophic neurites and neuronal loss in affected brain regions. Mutations in the AβP precursor protein (AβPP) are linked to familial AD, and these mutations may promote AβP production. In vitro and in vivo studies support the hypothesis that AβP directly contributes to neurodegeneration in AD. In primary neuronal cultures, AβP aggregates induce dystrophic neurite morphology and neuronal loss. In vivo studies show that intracerebral injection of AβP induces neuronal degeneration in adult rats and aged primates. Cell death can occur through necrosis or apoptosis. Apoptosis is a regulated form of cell death that functions in development and tissue homeostasis. Neurons undergoing apoptosis exhibit characteristic features such as membrane blebbing, nuclear condensation, and DNA fragmentation. In this study, AβP-treated neurons showed these features, indicating apoptosis. Electron microscopy and DNA fragmentation analysis confirmed ultrastructural and biochemical changes consistent with apoptosis. The study demonstrates that AβP induces apoptosis in cultured neurons, suggesting a role for apoptosis in neuronal loss in AD. The findings indicate that AβP may contribute to neurodegeneration through an apoptotic pathway, and that this process may be influenced by factors such as calcium homeostasis and protein synthesis. The results suggest that apoptosis may play a role in the progression of AD, and that understanding the apoptotic pathway may lead to strategies for delaying neurodegeneration.