Author: ["Marianna Armogida","Agnès Petit","Bruno Vincent","Sabine Scarzello","Cristine Alves da Costa","Frédéric Checler"]
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Abstract
Genetic and biochemical evidence have led to the suggestion that presenilins could be the long-searched-for γ-secretase, the proteolytic activity that generates the carboxy terminus of amyloid β-peptides. This activity is also thought to be responsible for the release of the Notch intracellular domain (NICD) from Notch. Here, we report the production of endogenous secreted and intracellular 40- and 42-amino-acid Aβ peptides in mouse fibroblasts deficient in presenilin 1, presenilin 2 or both. We show that the endogenous production of Aβ40 and Aβ42 was not altered by presenilin deficiency. By contrast, inactivating presenilin genes fully abolished NICD production. These data indicate that Aβ and NICD production are distinct catabolic events. Also, even though NICD formation is indeed presenilin dependent, endogenous secreted and intracellular β-amyloid peptides are still generated in absence of presenilins, indicating that there is a γ-secretase activity distinct from presenilins, at least in murine fibroblasts.Cite this article
Armogida, M., Petit, A., Vincent, B. et al. Endogenous β-amyloid production in presenilin-deficient embryonic mouse fibroblasts. Nat Cell Biol 3, 1030–1033 (2001). https://doi.org/10.1038/ncb1101-1030 