| pubmed-article:12656676 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:12656676 | lifeskim:mentions | umls-concept:C0030190 | lld:lifeskim |
| pubmed-article:12656676 | lifeskim:mentions | umls-concept:C0023688 | lld:lifeskim |
| pubmed-article:12656676 | lifeskim:mentions | umls-concept:C0032521 | lld:lifeskim |
| pubmed-article:12656676 | lifeskim:mentions | umls-concept:C0205263 | lld:lifeskim |
| pubmed-article:12656676 | pubmed:issue | Pt 3 | lld:pubmed |
| pubmed-article:12656676 | pubmed:dateCreated | 2003-6-4 | lld:pubmed |
| pubmed-article:12656676 | pubmed:abstractText | Negatively charged organochemical inactivators of the anti-proteolytic activity of plasminogen activator inhibitor-1 (PAI-1) convert it to inactive polymers. As investigated by native gel electrophoresis, the size of the PAI-1 polymers ranged from dimers to multimers of more than 20 units. As compared with native PAI-1, the polymers exhibited an increased resistance to temperature-induced unfolding. Polymerization was associated with specific changes in patterns of digestion with non-target proteases. During incubation with urokinase-type plasminogen activator, the polymers were slowly converted to reactive centre-cleaved monomers, indicating substrate behaviour of the terminal PAI-1 molecules in the polymers. A quadruple mutant of PAI-1 with a retarded rate of latency transition also had a retarded rate of polymerization. Studying a number of serpins by native gel electrophoresis, ligand-induced polymerization was observed only with PAI-1 and heparin cofactor II, which were also able to copolymerize. On the basis of these results, we suggest that the binding of ligands in a specific region of PAI-1 leads to so-called loop-sheet polymerization, in which the reactive centre loop of one molecule binds to beta-sheet A in another molecule. Induction of serpin polymerization by small organochemical ligands is a novel finding and is of protein chemical interest in relation to pathological protein polymerization in general. | lld:pubmed |
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| pubmed-article:12656676 | pubmed:language | eng | lld:pubmed |
| pubmed-article:12656676 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12656676 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:12656676 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:12656676 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:12656676 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:12656676 | pubmed:issn | 0264-6021 | lld:pubmed |
| pubmed-article:12656676 | pubmed:author | pubmed-author:WindTroelsT | lld:pubmed |
| pubmed-article:12656676 | pubmed:author | pubmed-author:AndreasenPete... | lld:pubmed |
| pubmed-article:12656676 | pubmed:author | pubmed-author:KenneyJohn... | lld:pubmed |
| pubmed-article:12656676 | pubmed:author | pubmed-author:PedersenKatri... | lld:pubmed |
| pubmed-article:12656676 | pubmed:author | pubmed-author:ChristensenAn... | lld:pubmed |
| pubmed-article:12656676 | pubmed:author | pubmed-author:EinholmAnja... | lld:pubmed |
| pubmed-article:12656676 | pubmed:author | pubmed-author:SchackLotteL | lld:pubmed |
| pubmed-article:12656676 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:12656676 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:12656676 | pubmed:volume | 372 | lld:pubmed |
| pubmed-article:12656676 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:12656676 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:12656676 | pubmed:pagination | 747-55 | lld:pubmed |
| pubmed-article:12656676 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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