| pubmed-article:8176223 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8176223 | lifeskim:mentions | umls-concept:C0205147 | lld:lifeskim |
| pubmed-article:8176223 | lifeskim:mentions | umls-concept:C0009498 | lld:lifeskim |
| pubmed-article:8176223 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
| pubmed-article:8176223 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
| pubmed-article:8176223 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
| pubmed-article:8176223 | lifeskim:mentions | umls-concept:C1524075 | lld:lifeskim |
| pubmed-article:8176223 | lifeskim:mentions | umls-concept:C0205369 | lld:lifeskim |
| pubmed-article:8176223 | lifeskim:mentions | umls-concept:C1515877 | lld:lifeskim |
| pubmed-article:8176223 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
| pubmed-article:8176223 | lifeskim:mentions | umls-concept:C1879547 | lld:lifeskim |
| pubmed-article:8176223 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
| pubmed-article:8176223 | lifeskim:mentions | umls-concept:C2353566 | lld:lifeskim |
| pubmed-article:8176223 | lifeskim:mentions | umls-concept:C0337112 | lld:lifeskim |
| pubmed-article:8176223 | pubmed:issue | 10 | lld:pubmed |
| pubmed-article:8176223 | pubmed:dateCreated | 1994-6-9 | lld:pubmed |
| pubmed-article:8176223 | pubmed:abstractText | beta-amyloid peptides that accumulate within the brain of individuals with Alzheimer's disease bind to C1q and activate the classical C pathway via a specific interaction with a site within the collagen-like domain of C1q (C1q-CLF). Synthetic analogues of beta-amyloid peptides, beta 1-42 and beta 1-40, bound to C1q and were strong activators of C as assessed by both total C consumption and C4 consumption. beta 1-42 was significantly more effective than beta 1-40 in binding to C1q and triggering C activation, whereas beta 1-28 demonstrated little or no binding or C activation. This C-activating capacity seems to be largely correlated with the assembly of the beta 1-42 into low speed sedimentable aggregates and/or macromolecular fibrils. Radiolabeled C1q and C1q-CLF bind specifically to these aggregates or amyloid fibrils. In addition, using synthetic C1q peptides in a solid phase binding assay, the major binding site of beta 1-42 to C1q was localized to the C1q A chain collagen-like residues 14-26, a region previously described as a novel interaction site for Ab-independent activators of C1. C1q A chain peptide 14-26 blocked the ability of beta-amyloid peptides to activate the classical C pathway, providing evidence that this relatively unrecognized mechanism of C activation (via binding to the C1q-CLF) may have crucial physiologic consequences. Finally, these observations provide further support for the hypothesis that C activation and inflammation may be a component in the pathogenesis of AD and suggest possibilities for modulating the progression of AD. | lld:pubmed |
| pubmed-article:8176223 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8176223 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8176223 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8176223 | pubmed:citationSubset | AIM | lld:pubmed |
| pubmed-article:8176223 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8176223 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8176223 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8176223 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8176223 | pubmed:month | May | lld:pubmed |
| pubmed-article:8176223 | pubmed:issn | 0022-1767 | lld:pubmed |
| pubmed-article:8176223 | pubmed:author | pubmed-author:CotmanC WCW | lld:pubmed |
| pubmed-article:8176223 | pubmed:author | pubmed-author:BurdickDD | lld:pubmed |
| pubmed-article:8176223 | pubmed:author | pubmed-author:TennerA JAJ | lld:pubmed |
| pubmed-article:8176223 | pubmed:author | pubmed-author:GlabeC GCG | lld:pubmed |
| pubmed-article:8176223 | pubmed:author | pubmed-author:JiangHH | lld:pubmed |
| pubmed-article:8176223 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8176223 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:8176223 | pubmed:volume | 152 | lld:pubmed |
| pubmed-article:8176223 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8176223 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8176223 | pubmed:pagination | 5050-9 | lld:pubmed |
| pubmed-article:8176223 | pubmed:dateRevised | 2010-11-18 | lld:pubmed |
| pubmed-article:8176223 | pubmed:meshHeading | pubmed-meshheading:8176223-... | lld:pubmed |
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| pubmed-article:8176223 | pubmed:meshHeading | pubmed-meshheading:8176223-... | lld:pubmed |
| pubmed-article:8176223 | pubmed:meshHeading | pubmed-meshheading:8176223-... | lld:pubmed |
| pubmed-article:8176223 | pubmed:meshHeading | pubmed-meshheading:8176223-... | lld:pubmed |
| pubmed-article:8176223 | pubmed:meshHeading | pubmed-meshheading:8176223-... | lld:pubmed |
| pubmed-article:8176223 | pubmed:meshHeading | pubmed-meshheading:8176223-... | lld:pubmed |
| pubmed-article:8176223 | pubmed:year | 1994 | lld:pubmed |
| pubmed-article:8176223 | pubmed:articleTitle | beta-Amyloid activates complement by binding to a specific region of the collagen-like domain of the C1q A chain. | lld:pubmed |
| pubmed-article:8176223 | pubmed:affiliation | Department of Molecular Biology and Biochemistry, University of California, Irvine 92717. | lld:pubmed |
| pubmed-article:8176223 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8176223 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:8176223 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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