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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
16
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pubmed:dateCreated |
1998-2-26
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pubmed:abstractText |
The activation of complement by beta-amyloid (A beta) has been implicated in the local inflammatory response in Alzheimer's disease. To assess the structural parameters required for this activation, beta-sheet-containing fibrils of A beta1-28 were induced by low pH and then chemically cross-linked to constrain the beta-sheet conformation. Chimeric A beta peptides with a substituted C-terminal sequence derived from two different transmembrane proteins were also assessed for the ability to form fibrils rich in beta-sheet structure and to activate complement. Both the cross-linked A beta1-28 and the chimeric A beta peptides were strong activators of the classical complement pathway. These results suggest that the C-terminal residues (29-42) of A beta facilitate fibril assembly required for complement activation but do not contain the interaction sites required for complement activation, further supporting the hypothesis that C1q binds to the N-terminal hydrophilic domain of A beta, and that a fibrillar beta-sheet-rich conformation is required for effective binding and activation of C1.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Amyloid beta-Peptides,
http://linkedlifedata.com/resource/pubmed/chemical/Complement C1q,
http://linkedlifedata.com/resource/pubmed/chemical/Cross-Linking Reagents,
http://linkedlifedata.com/resource/pubmed/chemical/Ethyldimethylaminopropyl...,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0959-4965
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
10
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pubmed:volume |
8
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
3457-62
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:9427307-Amino Acid Sequence,
pubmed-meshheading:9427307-Amyloid beta-Peptides,
pubmed-meshheading:9427307-Animals,
pubmed-meshheading:9427307-Binding Sites,
pubmed-meshheading:9427307-Complement Activation,
pubmed-meshheading:9427307-Complement C1q,
pubmed-meshheading:9427307-Cross-Linking Reagents,
pubmed-meshheading:9427307-Ethyldimethylaminopropyl Carbodiimide,
pubmed-meshheading:9427307-Guinea Pigs,
pubmed-meshheading:9427307-Humans,
pubmed-meshheading:9427307-Molecular Sequence Data,
pubmed-meshheading:9427307-Peptide Fragments,
pubmed-meshheading:9427307-Protein Conformation,
pubmed-meshheading:9427307-Protein Structure, Secondary,
pubmed-meshheading:9427307-Recombinant Fusion Proteins,
pubmed-meshheading:9427307-Sequence Deletion
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pubmed:year |
1997
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pubmed:articleTitle |
Complement activation by cross-linked truncated and chimeric full-length beta-amyloid.
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pubmed:affiliation |
Institute for Brain Aging and Dementia, Department of Neurology, University of California Irvine, 92697-4540, USA.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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