| pubmed-article:1311314 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1311314 | lifeskim:mentions | umls-concept:C0376525 | lld:lifeskim |
| pubmed-article:1311314 | lifeskim:mentions | umls-concept:C0014436 | lld:lifeskim |
| pubmed-article:1311314 | lifeskim:mentions | umls-concept:C0127082 | lld:lifeskim |
| pubmed-article:1311314 | lifeskim:mentions | umls-concept:C0145988 | lld:lifeskim |
| pubmed-article:1311314 | lifeskim:mentions | umls-concept:C0164371 | lld:lifeskim |
| pubmed-article:1311314 | lifeskim:mentions | umls-concept:C0165519 | lld:lifeskim |
| pubmed-article:1311314 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
| pubmed-article:1311314 | lifeskim:mentions | umls-concept:C0439855 | lld:lifeskim |
| pubmed-article:1311314 | lifeskim:mentions | umls-concept:C1522492 | lld:lifeskim |
| pubmed-article:1311314 | lifeskim:mentions | umls-concept:C1879547 | lld:lifeskim |
| pubmed-article:1311314 | lifeskim:mentions | umls-concept:C1292733 | lld:lifeskim |
| pubmed-article:1311314 | pubmed:issue | 7 | lld:pubmed |
| pubmed-article:1311314 | pubmed:dateCreated | 1992-4-2 | lld:pubmed |
| pubmed-article:1311314 | pubmed:abstractText | Secreted metalloproteases initiating proteolytic degradation of collagens and proteoglycans play a critical role in remodeling of the connective tissue. Activation of the secreted proenzymes and interaction with their specific inhibitors TIMP and TIMP-2 are responsible for regulation of enzyme activity in extracellular space. We have previously demonstrated that 92- and 72-kDa Type IV procollagenases, in contrast to interstitial collagenase (ClI), form specific complexes with TIMP and the related inhibitor TIMP-2, respectively. The physiologic significance of the proenzyme-inhibitor complex and the mechanism of activation of Type IV collagenases remained unclear. Here, we demonstrate that in the absence of TIMP, 92-kDa Type IV procollagenase (92T4Cl) can form a covalent homodimer and a novel complex with ClI. In the presence of TIMP, the formation of a 92T4Cl proenzyme complex with TIMP prevents dimerization, formation of the complex with ClI, and activation of the 92T4Cl proenzyme by stromelysin, a related metalloprotease. The proenzyme homodimer is unable to form a complex with TIMP. All TIMP-free forms of the proenzyme can be activated by stromelysin. The 92T4Cl-ClI complex can be activated to yield a complex active against both gelatin and fibrillar Type I collagen, suggesting a mechanism for cooperative action of two enzymes in reducing collagen fibrils to small peptides under physiologic conditions. | lld:pubmed |
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| pubmed-article:1311314 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1311314 | pubmed:language | eng | lld:pubmed |
| pubmed-article:1311314 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1311314 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:1311314 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:1311314 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1311314 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:1311314 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:1311314 | pubmed:author | pubmed-author:GoldbergG IGI | lld:pubmed |
| pubmed-article:1311314 | pubmed:author | pubmed-author:CollierI EIE | lld:pubmed |
| pubmed-article:1311314 | pubmed:author | pubmed-author:MarmerB LBL | lld:pubmed |
| pubmed-article:1311314 | pubmed:author | pubmed-author:GenrichL TLT | lld:pubmed |
| pubmed-article:1311314 | pubmed:author | pubmed-author:StronginAA | lld:pubmed |
| pubmed-article:1311314 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1311314 | pubmed:day | 5 | lld:pubmed |
| pubmed-article:1311314 | pubmed:volume | 267 | lld:pubmed |
| pubmed-article:1311314 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1311314 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1311314 | pubmed:pagination | 4583-91 | lld:pubmed |
| pubmed-article:1311314 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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| pubmed-article:1311314 | pubmed:year | 1992 | lld:pubmed |
| pubmed-article:1311314 | pubmed:articleTitle | Interaction of 92-kDa type IV collagenase with the tissue inhibitor of metalloproteinases prevents dimerization, complex formation with interstitial collagenase, and activation of the proenzyme with stromelysin. | lld:pubmed |
| pubmed-article:1311314 | pubmed:affiliation | Division of Dermatology, Washington University School of Medicine, St. Louis, Missouri 63110. | lld:pubmed |
| pubmed-article:1311314 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:1311314 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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