Presenilin 1 is actively degraded by the 26S proteasome

P E Fraser; G Levesque; G Yu; L R Mills; J Thirlwell; M Frantseva; S E Gandy; M Seeger; P L Carlen; P St George-Hyslop

doi:10.1016/s0197-4580(98)00029-3

Presenilin 1 is actively degraded by the 26S proteasome

Neurobiol Aging. 1998 Jan-Feb;19(1 Suppl):S19-21. doi: 10.1016/s0197-4580(98)00029-3.

Authors

P E Fraser¹, G Levesque, G Yu, L R Mills, J Thirlwell, M Frantseva, S E Gandy, M Seeger, P L Carlen, P St George-Hyslop

Affiliation

¹ Centre for Research in Neurodegenerative Diseases, Department of Medicine, The Toronto Hospital, University of Toronto, Ontario, Canada.

PMID: 9562462
DOI: 10.1016/s0197-4580(98)00029-3

Abstract

The metabolic pathways governing the turnover of presenilin 1 (PS1) have been incompletely worked out. The PS1 holoprotein has low abundance in many cells and appears to undergo endoproteolytic cleavage near residue 298. We provide evidence that one mechanism by which the PS1 holoprotein is degraded is through the action of the 26S proteasome. We also show that the proteasome does not participate in the endoproteolytic cleavage.

Publication types

Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, P.H.S.

MeSH terms

Alzheimer Disease / metabolism*
Animals
Blotting, Western
Caco-2 Cells
Hippocampus / metabolism
Humans
In Vitro Techniques
Membrane Proteins / metabolism*
Mice
NF-kappa B / metabolism
Peptide Hydrolases / metabolism*
Presenilin-1
Proteasome Endopeptidase Complex*
Rats
Rats, Wistar

Substances

Membrane Proteins
NF-kappa B
PSEN1 protein, human
Presenilin-1
Peptide Hydrolases
Proteasome Endopeptidase Complex
ATP dependent 26S protease