Alzheimer's disease : Correlation of the suppression of β-amyloid Peptide secretion from cultured cells with inhibition of the chymotrypsin-like activity of the proteasome
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...
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| Veröffentlicht in: | Journal of neurochemistry 1999-07, Vol.73 (1), p.195-204 |
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| creator | CHRISTIE, G MARKWELL, R. E WARD, R. V HOWLETT, D. R HARTMANN, T LICHTENTHALER, S. F BEYREUTHER, K UNDERWOOD, J GRIBBLE, S. K CAPPAI, R MASTERS, C. L TAMAOKA, A GRAY, C. W GARDNER, R. L RIVETT, A. J KARRAN, E. H ALLSOP, D SMITH, L GODFREY, F MANSFIELD, F WADSWORTH, H KING, R MCLAUGHLIN, M COOPER, D. G |
| description | 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. |
| doi_str_mv | 10.1046/j.1471-4159.1999.0730195.x |
| format | Article |
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E ; WARD, R. V ; HOWLETT, D. R ; HARTMANN, T ; LICHTENTHALER, S. F ; BEYREUTHER, K ; UNDERWOOD, J ; GRIBBLE, S. K ; CAPPAI, R ; MASTERS, C. L ; TAMAOKA, A ; GRAY, C. W ; GARDNER, R. L ; RIVETT, A. J ; KARRAN, E. H ; ALLSOP, D ; SMITH, L ; GODFREY, F ; MANSFIELD, F ; WADSWORTH, H ; KING, R ; MCLAUGHLIN, M ; COOPER, D. G</creator><creatorcontrib>CHRISTIE, G ; MARKWELL, R. E ; WARD, R. V ; HOWLETT, D. R ; HARTMANN, T ; LICHTENTHALER, S. F ; BEYREUTHER, K ; UNDERWOOD, J ; GRIBBLE, S. K ; CAPPAI, R ; MASTERS, C. L ; TAMAOKA, A ; GRAY, C. W ; GARDNER, R. L ; RIVETT, A. J ; KARRAN, E. H ; ALLSOP, D ; SMITH, L ; GODFREY, F ; MANSFIELD, F ; WADSWORTH, H ; KING, R ; MCLAUGHLIN, M ; COOPER, D. G</creatorcontrib><description>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.</description><identifier>ISSN: 0022-3042</identifier><identifier>EISSN: 1471-4159</identifier><identifier>DOI: 10.1046/j.1471-4159.1999.0730195.x</identifier><identifier>PMID: 10386971</identifier><identifier>CODEN: JONRA9</identifier><language>eng</language><publisher>Oxford: Blackwell</publisher><subject>Aldehydes - pharmacology ; Alzheimer Disease - metabolism ; Amyloid beta-Peptides - analysis ; Amyloid beta-Peptides - metabolism ; Amyloid beta-Protein Precursor - genetics ; Biological and medical sciences ; Boronic Acids - pharmacology ; Cell Line ; Chymotrypsin - antagonists & inhibitors ; Chymotrypsin - metabolism ; Cysteine Endopeptidases - metabolism ; Degenerative and inherited degenerative diseases of the nervous system. Leukodystrophies. Prion diseases ; Medical sciences ; Multienzyme Complexes - metabolism ; Neurology ; Peptide Fragments - analysis ; Peptide Fragments - metabolism ; Proteasome Endopeptidase Complex ; proteasomes ; Transfection</subject><ispartof>Journal of neurochemistry, 1999-07, Vol.73 (1), p.195-204</ispartof><rights>1999 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><cites>FETCH-LOGICAL-c318t-9558e7b3201b93c90c6e3f2fb6f4078f2c86ddf68317671f5994aadb39bf4f883</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=1887833$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/10386971$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>CHRISTIE, G</creatorcontrib><creatorcontrib>MARKWELL, R. E</creatorcontrib><creatorcontrib>WARD, R. V</creatorcontrib><creatorcontrib>HOWLETT, D. R</creatorcontrib><creatorcontrib>HARTMANN, T</creatorcontrib><creatorcontrib>LICHTENTHALER, S. F</creatorcontrib><creatorcontrib>BEYREUTHER, K</creatorcontrib><creatorcontrib>UNDERWOOD, J</creatorcontrib><creatorcontrib>GRIBBLE, S. K</creatorcontrib><creatorcontrib>CAPPAI, R</creatorcontrib><creatorcontrib>MASTERS, C. L</creatorcontrib><creatorcontrib>TAMAOKA, A</creatorcontrib><creatorcontrib>GRAY, C. W</creatorcontrib><creatorcontrib>GARDNER, R. L</creatorcontrib><creatorcontrib>RIVETT, A. J</creatorcontrib><creatorcontrib>KARRAN, E. H</creatorcontrib><creatorcontrib>ALLSOP, D</creatorcontrib><creatorcontrib>SMITH, L</creatorcontrib><creatorcontrib>GODFREY, F</creatorcontrib><creatorcontrib>MANSFIELD, F</creatorcontrib><creatorcontrib>WADSWORTH, H</creatorcontrib><creatorcontrib>KING, R</creatorcontrib><creatorcontrib>MCLAUGHLIN, M</creatorcontrib><creatorcontrib>COOPER, D. G</creatorcontrib><title>Alzheimer's disease : Correlation of the suppression of β-amyloid Peptide secretion from cultured cells with inhibition of the chymotrypsin-like activity of the proteasome</title><title>Journal of neurochemistry</title><addtitle>J Neurochem</addtitle><description>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.</description><subject>Aldehydes - pharmacology</subject><subject>Alzheimer Disease - metabolism</subject><subject>Amyloid beta-Peptides - analysis</subject><subject>Amyloid beta-Peptides - metabolism</subject><subject>Amyloid beta-Protein Precursor - genetics</subject><subject>Biological and medical sciences</subject><subject>Boronic Acids - pharmacology</subject><subject>Cell Line</subject><subject>Chymotrypsin - antagonists & inhibitors</subject><subject>Chymotrypsin - metabolism</subject><subject>Cysteine Endopeptidases - metabolism</subject><subject>Degenerative and inherited degenerative diseases of the nervous system. Leukodystrophies. Prion diseases</subject><subject>Medical sciences</subject><subject>Multienzyme Complexes - metabolism</subject><subject>Neurology</subject><subject>Peptide Fragments - analysis</subject><subject>Peptide Fragments - metabolism</subject><subject>Proteasome Endopeptidase Complex</subject><subject>proteasomes</subject><subject>Transfection</subject><issn>0022-3042</issn><issn>1471-4159</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1999</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkcFu1DAQhi0EokvhFZCFEJwS7Dhx7N6qFQWkSnCAs-U4Y8VLsg62Aw3PxKkPwjORsAF64zSS5_tnxvoQekZJTknJXx1yWtY0K2klcyqlzEnNCJVVfnMP7f627qMdIUWRMVIWZ-hRjAdCKC85fYjOKGGCy5ru0I_L_nsHboDwMuLWRdAR8AXe-xCg18n5I_YWpw5wnMYxQIzb08_bTA9z712LP8CYXLsQYAL8jtjgB2ymPk0BWmyg7yP-5lKH3bFzjbs71nTz4FOYx-iOWe8-A9Ymua8uzX-IMfi0nOUHeIweWN1HeLLVc_Tp6vXH_dvs-v2bd_vL68wwKlImq0pA3bCC0EYyI4nhwGxhG25LUgtbGMHb1nLBaM1raispS63bhsnGllYIdo5enOYuq79MEJMaXFx_oY_gp6i4FBWTgvwXpHVJqCB0AS9OoAk-xgBWjcENOsyKErVKVQe1mlOrObVKVZtUdbOEn25bpmaA9k70ZHEBnm-Ajkb3NuijcfEfJ0QtGGO_AJHnsA4</recordid><startdate>19990701</startdate><enddate>19990701</enddate><creator>CHRISTIE, G</creator><creator>MARKWELL, R. E</creator><creator>WARD, R. V</creator><creator>HOWLETT, D. R</creator><creator>HARTMANN, T</creator><creator>LICHTENTHALER, S. F</creator><creator>BEYREUTHER, K</creator><creator>UNDERWOOD, J</creator><creator>GRIBBLE, S. K</creator><creator>CAPPAI, R</creator><creator>MASTERS, C. L</creator><creator>TAMAOKA, A</creator><creator>GRAY, C. W</creator><creator>GARDNER, R. L</creator><creator>RIVETT, A. J</creator><creator>KARRAN, E. H</creator><creator>ALLSOP, D</creator><creator>SMITH, L</creator><creator>GODFREY, F</creator><creator>MANSFIELD, F</creator><creator>WADSWORTH, H</creator><creator>KING, R</creator><creator>MCLAUGHLIN, M</creator><creator>COOPER, D. G</creator><general>Blackwell</general><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7TK</scope><scope>7X8</scope></search><sort><creationdate>19990701</creationdate><title>Alzheimer's disease : Correlation of the suppression of β-amyloid Peptide secretion from cultured cells with inhibition of the chymotrypsin-like activity of the proteasome</title><author>CHRISTIE, G ; MARKWELL, R. E ; WARD, R. V ; HOWLETT, D. R ; HARTMANN, T ; LICHTENTHALER, S. F ; BEYREUTHER, K ; UNDERWOOD, J ; GRIBBLE, S. K ; CAPPAI, R ; MASTERS, C. L ; TAMAOKA, A ; GRAY, C. W ; GARDNER, R. L ; RIVETT, A. J ; KARRAN, E. H ; ALLSOP, D ; SMITH, L ; GODFREY, F ; MANSFIELD, F ; WADSWORTH, H ; KING, R ; MCLAUGHLIN, M ; COOPER, D. 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Prion diseases</topic><topic>Medical sciences</topic><topic>Multienzyme Complexes - metabolism</topic><topic>Neurology</topic><topic>Peptide Fragments - analysis</topic><topic>Peptide Fragments - metabolism</topic><topic>Proteasome Endopeptidase Complex</topic><topic>proteasomes</topic><topic>Transfection</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>CHRISTIE, G</creatorcontrib><creatorcontrib>MARKWELL, R. E</creatorcontrib><creatorcontrib>WARD, R. V</creatorcontrib><creatorcontrib>HOWLETT, D. R</creatorcontrib><creatorcontrib>HARTMANN, T</creatorcontrib><creatorcontrib>LICHTENTHALER, S. F</creatorcontrib><creatorcontrib>BEYREUTHER, K</creatorcontrib><creatorcontrib>UNDERWOOD, J</creatorcontrib><creatorcontrib>GRIBBLE, S. K</creatorcontrib><creatorcontrib>CAPPAI, R</creatorcontrib><creatorcontrib>MASTERS, C. L</creatorcontrib><creatorcontrib>TAMAOKA, A</creatorcontrib><creatorcontrib>GRAY, C. W</creatorcontrib><creatorcontrib>GARDNER, R. 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H</au><au>ALLSOP, D</au><au>SMITH, L</au><au>GODFREY, F</au><au>MANSFIELD, F</au><au>WADSWORTH, H</au><au>KING, R</au><au>MCLAUGHLIN, M</au><au>COOPER, D. G</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Alzheimer's disease : Correlation of the suppression of β-amyloid Peptide secretion from cultured cells with inhibition of the chymotrypsin-like activity of the proteasome</atitle><jtitle>Journal of neurochemistry</jtitle><addtitle>J Neurochem</addtitle><date>1999-07-01</date><risdate>1999</risdate><volume>73</volume><issue>1</issue><spage>195</spage><epage>204</epage><pages>195-204</pages><issn>0022-3042</issn><eissn>1471-4159</eissn><coden>JONRA9</coden><abstract>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. 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| fulltext | fulltext |
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| ispartof | Journal of neurochemistry, 1999-07, Vol.73 (1), p.195-204 |
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| language | eng |
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| source | Wiley Free Content; MEDLINE; IngentaConnect Free/Open Access Journals; Wiley Online Library Journals Frontfile Complete; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Free Full-Text Journals in Chemistry |
| subjects | Aldehydes - pharmacology Alzheimer Disease - metabolism Amyloid beta-Peptides - analysis Amyloid beta-Peptides - metabolism Amyloid beta-Protein Precursor - genetics Biological and medical sciences Boronic Acids - pharmacology Cell Line Chymotrypsin - antagonists & inhibitors Chymotrypsin - metabolism Cysteine Endopeptidases - metabolism Degenerative and inherited degenerative diseases of the nervous system. Leukodystrophies. Prion diseases Medical sciences Multienzyme Complexes - metabolism Neurology Peptide Fragments - analysis Peptide Fragments - metabolism Proteasome Endopeptidase Complex proteasomes Transfection |
| title | Alzheimer's disease : Correlation of the suppression of β-amyloid Peptide secretion from cultured cells with inhibition of the chymotrypsin-like activity of the proteasome |
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