X11α impairs γ- but not β-cleavage of amyloid precursor protein
dc.contributor.author | King, Gwendalyn D. | en_US |
dc.contributor.author | Cherian, Kay | en_US |
dc.contributor.author | Turner, R. Scott | en_US |
dc.date.accessioned | 2010-04-01T15:32:11Z | |
dc.date.available | 2010-04-01T15:32:11Z | |
dc.date.issued | 2004-02 | en_US |
dc.identifier.citation | King, Gwendalyn D.; Cherian, Kay; Turner, R. Scott (2004). "X11α impairs γ- but not β-cleavage of amyloid precursor protein." Journal of Neurochemistry 88(4): 971-982. <http://hdl.handle.net/2027.42/66020> | en_US |
dc.identifier.issn | 0022-3042 | en_US |
dc.identifier.issn | 1471-4159 | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/66020 | |
dc.identifier.uri | http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=14756819&dopt=citation | en_US |
dc.description.abstract | The phosphotyrosine binding domain of the neuronal protein X11α/mint-1 binds to the C-terminus of amyloid precursor protein (APP) and inhibits catabolism to β-amyloid (Aβ), but the mechanism of this effect is unclear. Coexpression of X11α or its PTB domain with APPswe inhibited secretion of Aβ40 but not APPsβswe, suggesting inhibition of γ- but not β-secretase. To further probe cleavage(s) inhibited by X11α, we coexpressed β-secretase (BACE-1) or a component of the γ-secretase complex (PS-1δ9) with APP, APPswe, or C99, with and without X11α, in HEK293 cells. X11α suppressed the PS-1δ9-induced increase in Aβ42 secretion generated from APPswe or C99. However, X11α did not impair BACE-1-mediated proteolysis of APP or APPswe to C99. In contrast to impaired γ-cleavage of APPswe, X11α or its PTB domain did not inhibit γ-cleavage of NotchδE to NICD (the Notch intracellular domain). The X11α PDZ–PS.1δ9 interaction did not affect γ-cleavage activity. In a cell-free system, X11α did not inhibit the catabolism of APP C-terminal fragments. These data suggest that X11α may inhibit Aβ secretion from APP by impairing its trafficking to sites of active γ-secretase complexes. By specifically targeting substrate instead of enzyme X11α may function as a relatively specific γ-secretase inhibitor. | en_US |
dc.format.extent | 497157 bytes | |
dc.format.extent | 3110 bytes | |
dc.format.mimetype | application/pdf | |
dc.format.mimetype | text/plain | |
dc.publisher | Blackwell Science Ltd | en_US |
dc.rights | 2004 International Society for Neurochemistry | en_US |
dc.subject.other | amyloid precursor protein | en_US |
dc.subject.other | X11α | en_US |
dc.subject.other | BACE | en_US |
dc.subject.other | presenilin | en_US |
dc.subject.other | notch | en_US |
dc.subject.other | γ-secretase | en_US |
dc.title | X11α impairs γ- but not β-cleavage of amyloid precursor protein | en_US |
dc.type | Article | en_US |
dc.rights.robots | IndexNoFollow | en_US |
dc.subject.hlbsecondlevel | Neurosciences | en_US |
dc.subject.hlbtoplevel | Health Sciences | en_US |
dc.description.peerreviewed | Peer Reviewed | en_US |
dc.contributor.affiliationum | * Neuroscience Program, University of Michigan, Ann Arbor, Michigan, USA | en_US |
dc.contributor.affiliationum | † Department of Neurology, University of Michigan, Ann Arbor, Michigan, USA | en_US |
dc.contributor.affiliationum | † Institute of Gerontology, University of Michigan, Ann Arbor, Michigan, USA | en_US |
dc.contributor.affiliationum | § Veterans Affairs Ann Arbor Healthcare System, Geriatric Research Education and Clinical Center, Ann Arbor, Michigan, USA | en_US |
dc.identifier.pmid | 14756819 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/66020/1/j.1471-4159.2003.02234.x.pdf | |
dc.identifier.doi | 10.1046/j.1471-4159.2003.02234.x | en_US |
dc.identifier.source | Journal of Neurochemistry | en_US |
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