Selective increase in cellular A beta 42 is related to apoptosis but not necrosis

• Published in: Neuroreport Vol. 11; no. 1; pp. 167 - 171
• Main Authors: Ohyagi, Y, Yamada, T, Nishioka, K, Clarke, N J, Tomlinson, A J, Naylor, S, Nakabeppu, Y, Kira, J, Younkin, S G
• Format: Journal Article
• Language: English
• Published: England 17-01-2000
• Subjects: Amyloid beta-Peptides - biosynthesis; Animals; Antineoplastic Agents, Alkylating - pharmacology; Antineoplastic Agents, Phytogenic - pharmacology; Apoptosis - physiology; Cells, Cultured; Enzyme-Linked Immunosorbent Assay; Etoposide - pharmacology; Guinea Pigs; Humans; Hydrogen Peroxide - pharmacology; Immunohistochemistry; In Situ Nick-End Labeling; L-Lactate Dehydrogenase - metabolism; Melphalan - pharmacology; Necrosis; Peptide Fragments - biosynthesis; Reactive Oxygen Species - metabolism; Sodium Azide - toxicity
• ISSN: 0959-4965
• DOI: 10.1097/00001756-200001170-00033

Amyloid beta protein ending at 42 (A beta 42) plays an important role in the pathology of Alzheimer's disease (AD). Here we show an increase in cellular A beta 42 in damaged neurons, with both ELISA and immunocytochemistry. The cellular A beta 42 increase was caused by 3-day treatments with H2O2, etoposide or melphalan, all of which induce genotoxic apoptosis, but not by treatment with sodium azide, which causes necrosis. Secreted A beta was similarly decreased with all these treatments. The cellular A beta 42 increase appeared even with minimal damage (ELISA) and A beta 42-positive cells were TUNEL negative (double staining), indicating that any early apoptosis mechanism may induce the cellular A beta 42 increase. Thus, neuronal apoptosis and cellular A beta 42 increase may be linked in a way that contributes importantly to AD pathology.