Neuronal Apoptosis Induced by β-Amyloid Is Mediated by Caspase-8

Content Provider	Semantic Scholar
Author	Ivins, Kathryn J. Thornton, Phillip L. Rohn, Troy T. Cotman, Carl
Copyright Year	1999
Abstract	Abstract The Alzheimer disease-associated β-amyloid peptide has been shown to induce apoptotic neuronal death. In the present study, we test the hypothesis that the apoptotic pathway activated by β-amyloid is similar to the pathway activated by the Fas/TNFR family of death receptors, which requires caspase-8 activity and adaptor proteins such as FADD. We demonstrate that the selective caspase-8 inhibitor IETD-fmk blocks neuronal death induced by β-amyloid. Furthermore, using viral-mediated gene delivery, we show that neurons expressing dominant-negative FADD are protected from apoptosis induced by β-amyloid. Together these results indicate that the apoptotic pathway activated by β-amyloid requires both caspase-8 activity and FADD. These findings further support the hypothesis that β-amyloid might initiate apoptosis by cross-linking death receptors of the Fas/TNFR family.
Starting Page	440
Ending Page	449
Page Count	10
File Format	PDF HTM / HTML
DOI	10.1006/nbdi.1999.0268
Volume Number	6
Alternate Webpage(s)	https://api.elsevier.com/content/article/pii/S0969996199902681
Alternate Webpage(s)	https://www.sciencedirect.com/science/article/pii/S0969996199902681?dgcid=api_sd_search-api-endpoint
Alternate Webpage(s)	https://doi.org/10.1006/nbdi.1999.0268
Journal	Neurobiology of Disease
Language	English
Access Restriction	Open
Content Type	Text
Resource Type	Article