| pubmed-article:7621597 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:7621597 | lifeskim:mentions | umls-concept:C0067033 | lld:lifeskim |
| pubmed-article:7621597 | lifeskim:mentions | umls-concept:C0521449 | lld:lifeskim |
| pubmed-article:7621597 | lifeskim:mentions | umls-concept:C0004358 | lld:lifeskim |
| pubmed-article:7621597 | lifeskim:mentions | umls-concept:C0597304 | lld:lifeskim |
| pubmed-article:7621597 | lifeskim:mentions | umls-concept:C0439658 | lld:lifeskim |
| pubmed-article:7621597 | lifeskim:mentions | umls-concept:C0439858 | lld:lifeskim |
| pubmed-article:7621597 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:7621597 | pubmed:dateCreated | 1995-8-30 | lld:pubmed |
| pubmed-article:7621597 | pubmed:abstractText | C-ANCA, which are directed against neutrophil proteinase 3 (PR3), are specific markers for the diagnosis of active Wegener's granulomatosis (WG). The correlation between C-ANCA titre and WG disease activity suggests that these autoantibodies are involved in the development of WG. We have previously observed that C-ANCA interfere with PR3 proteolytic activity and with complexation of PR3 with its major physiologic inhibitor alpha 1-antitrypsin (alpha 1-AT). The possible pathogenic importance of C-ANCA may be related to the stability of C-ANCA IgG-PR3 complexes. In the present study we tested proteolysis by PR3 of human IgG and proteolysis of C-ANCA IgG complexed to the enzyme. All human IgG subclass proteins were cleaved by PR3. Digestion products were compared with those obtained by human neutrophil elastase (HNE)-mediated proteolysis of human IgG subclass proteins. Although cleavage products of similar size could be identified, the proteolytic activity of both enzymes towards human IgG differed. Furthermore, inhibiting C-ANCA IgG were cleaved into small peptides when complexed to PR3. The possible pathogenic consequences of these findings will be discussed. | lld:pubmed |
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| pubmed-article:7621597 | pubmed:language | eng | lld:pubmed |
| pubmed-article:7621597 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7621597 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:7621597 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:7621597 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:7621597 | pubmed:issn | 0009-9104 | lld:pubmed |
| pubmed-article:7621597 | pubmed:author | pubmed-author:SonnenbergAA | lld:pubmed |
| pubmed-article:7621597 | pubmed:author | pubmed-author:von dem... | lld:pubmed |
| pubmed-article:7621597 | pubmed:author | pubmed-author:JagerAA | lld:pubmed |
| pubmed-article:7621597 | pubmed:author | pubmed-author:Goldschmeding... | lld:pubmed |
| pubmed-article:7621597 | pubmed:author | pubmed-author:DolmanK MKM | lld:pubmed |
| pubmed-article:7621597 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:7621597 | pubmed:volume | 101 | lld:pubmed |
| pubmed-article:7621597 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:7621597 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:7621597 | pubmed:pagination | 8-12 | lld:pubmed |
| pubmed-article:7621597 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:7621597 | pubmed:meshHeading | pubmed-meshheading:7621597-... | lld:pubmed |
| pubmed-article:7621597 | pubmed:year | 1995 | lld:pubmed |
| pubmed-article:7621597 | pubmed:articleTitle | Proteolysis of classic anti-neutrophil cytoplasmic autoantibodies (C-ANCA) by neutrophil proteinase 3. | lld:pubmed |
| pubmed-article:7621597 | pubmed:affiliation | Central Laboratory, Netherlands Red Cross Blood Transfusion Service, Amsterdam. | lld:pubmed |
| pubmed-article:7621597 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:7621597 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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