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rdf:type |
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lifeskim:mentions |
umls-concept:C0002395,
umls-concept:C0007635,
umls-concept:C0021467,
umls-concept:C0021469,
umls-concept:C0208355,
umls-concept:C0301625,
umls-concept:C0441655,
umls-concept:C1413809,
umls-concept:C1707520,
umls-concept:C1743100,
umls-concept:C1819802
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pubmed:issue |
1
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pubmed:dateCreated |
1999-7-8
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pubmed:abstractText |
Peptide aldehyde inhibitors of the chymotrypsin-like activity of the proteasome (CLIP) such as N-acetyl-Leu-Leu-Nle-H (or ALLN) have been shown previously to inhibit the secretion of beta-amyloid peptide (A beta) from cells. To evaluate more fully the role of the proteasome in this process, we have tested the effects on A beta formation of a much wider range of peptide-based inhibitors of CLIP than published previously. The inhibitors tested included several peptide boronates, some of which proved to be the most potent peptide-based inhibitors of beta-amyloid production reported so far. We found that the ability of the peptide aldehyde and boronate inhibitors to suppress A beta formation from cells correlated extremely well with their potency as CLIP inhibitors. Thus, we conclude that the proteasome may be involved either directly or indirectly in A beta formation.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0022-3042
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pubmed:author |
pubmed-author:AllsopDD,
pubmed-author:BeyreutherKK,
pubmed-author:CappaiRR,
pubmed-author:ChristieGG,
pubmed-author:CooperD GDG,
pubmed-author:GardnerR LRL,
pubmed-author:GodfreyFF,
pubmed-author:GrayC WCW,
pubmed-author:GribbleS KSK,
pubmed-author:HartmannTT,
pubmed-author:HowlettD RDR,
pubmed-author:KarranE HEH,
pubmed-author:KingRR,
pubmed-author:LichtenthalerS FSF,
pubmed-author:MansfieldFF,
pubmed-author:MarkwellR ERE,
pubmed-author:MastersC LCL,
pubmed-author:McLaughlinMM,
pubmed-author:RivettA JAJ,
pubmed-author:SmithLL,
pubmed-author:TamaokaAA,
pubmed-author:UnderwoodJJ,
pubmed-author:WadsworthHH,
pubmed-author:WardR VRV
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pubmed:issnType |
Print
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pubmed:volume |
73
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
195-204
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:10386971-Aldehydes,
pubmed-meshheading:10386971-Alzheimer Disease,
pubmed-meshheading:10386971-Amyloid beta-Peptides,
pubmed-meshheading:10386971-Amyloid beta-Protein Precursor,
pubmed-meshheading:10386971-Boronic Acids,
pubmed-meshheading:10386971-Cell Line,
pubmed-meshheading:10386971-Chymotrypsin,
pubmed-meshheading:10386971-Cysteine Endopeptidases,
pubmed-meshheading:10386971-Multienzyme Complexes,
pubmed-meshheading:10386971-Peptide Fragments,
pubmed-meshheading:10386971-Proteasome Endopeptidase Complex,
pubmed-meshheading:10386971-Transfection
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pubmed:year |
1999
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pubmed:articleTitle |
Alzheimer's disease: correlation of the suppression of beta-amyloid peptide secretion from cultured cells with inhibition of the chymotrypsin-like activity of the proteasome.
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pubmed:affiliation |
SmithKline Beecham Pharmaceuticals, Harlow, Essex, England, UK.
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pubmed:publicationType |
Journal Article
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