| pubmed-article:7772054 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:7772054 | lifeskim:mentions | umls-concept:C0025543 | lld:lifeskim |
| pubmed-article:7772054 | lifeskim:mentions | umls-concept:C0145988 | lld:lifeskim |
| pubmed-article:7772054 | lifeskim:mentions | umls-concept:C0439855 | lld:lifeskim |
| pubmed-article:7772054 | lifeskim:mentions | umls-concept:C1314939 | lld:lifeskim |
| pubmed-article:7772054 | lifeskim:mentions | umls-concept:C1879547 | lld:lifeskim |
| pubmed-article:7772054 | lifeskim:mentions | umls-concept:C1261552 | lld:lifeskim |
| pubmed-article:7772054 | lifeskim:mentions | umls-concept:C0246551 | lld:lifeskim |
| pubmed-article:7772054 | lifeskim:mentions | umls-concept:C0048055 | lld:lifeskim |
| pubmed-article:7772054 | pubmed:dateCreated | 1995-7-5 | lld:pubmed |
| pubmed-article:7772054 | pubmed:abstractText | Tissue inhibitor of metalloproteinases (TIMP)-2 forms a noncovalent complex with the precursor of matrix metalloproteinase 2 (proMMP-2, progelatinase A) through interaction of the C-terminal domain of each molecule. We have isolated the proMMP-2-TIMP-2 complex from the medium of human uterine cervical fibroblasts and investigated the processes involved in its activation by 4-aminophenylmercuric acetate (APMA). The treatment of the complex with APMA-activated proMMP-2 by disrupting the Cys73-Zn2+ interaction of the zymogen. This is triggered by perturbation of the proMMP-2 molecule, but not by the reaction of the SH group of Cys73 with APMA. The 'activated' proMMP-2 (proMMP-2*) formed a new complex with TIMP-2 by binding to the N-terminal inhibitory domain of the inhibitor without processing the propeptide. Thus the APMA-treated proMMP-2*-TIMP-2 complex exhibited no gelatinolytic activity. In the presence of a small amount of free MMP-2, however, proMMP-2* in the complex was converted into the 65 kDa MMP-2 by proteolytic attack of MMP-2, but the complex did not exhibit gelatinolytic activity. The gelatinolytic activity detected after APMA treatment was solely derived from the activation of free proMMP-2. The removal of the propeptide of the proMMP-2* bound to TIMP-2 was also observed by MMP-3 (stromelysin 1), but not by MMP-1 (interstitial collagenase). MMP-3 cleaved the Asn80-Tyr81 bond of proMMP-2*. On the other hand, when MMP-3 was incubated with the proMMP-2-TIMP-2 complex, it bound to TIMP-2 and rendered proMMP-2 readily activatable by APMA. These results indicate that the blockage of TIMP-2 of the complex with an active MMP is essential for the activation of proMMP-2 when it is complexed with TIMP-2. | lld:pubmed |
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| pubmed-article:7772054 | pubmed:language | eng | lld:pubmed |
| pubmed-article:7772054 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7772054 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:7772054 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:7772054 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:7772054 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:7772054 | pubmed:issn | 0264-6021 | lld:pubmed |
| pubmed-article:7772054 | pubmed:author | pubmed-author:ItohYY | lld:pubmed |
| pubmed-article:7772054 | pubmed:author | pubmed-author:NagaseHH | lld:pubmed |
| pubmed-article:7772054 | pubmed:author | pubmed-author:BinnerSS | lld:pubmed |
| pubmed-article:7772054 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:7772054 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:7772054 | pubmed:volume | 308 ( Pt 2) | lld:pubmed |
| pubmed-article:7772054 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:7772054 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:7772054 | pubmed:pagination | 645-51 | lld:pubmed |
| pubmed-article:7772054 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:7772054 | pubmed:meshHeading | pubmed-meshheading:7772054-... | lld:pubmed |
| pubmed-article:7772054 | pubmed:meshHeading | pubmed-meshheading:7772054-... | lld:pubmed |
| pubmed-article:7772054 | pubmed:meshHeading | pubmed-meshheading:7772054-... | lld:pubmed |
| pubmed-article:7772054 | pubmed:year | 1995 | lld:pubmed |
| pubmed-article:7772054 | pubmed:articleTitle | Steps involved in activation of the complex of pro-matrix metalloproteinase 2 (progelatinase A) and tissue inhibitor of metalloproteinases (TIMP)-2 by 4-aminophenylmercuric acetate. | lld:pubmed |
| pubmed-article:7772054 | pubmed:affiliation | Department of Biochemistry and Molecular Biology, University of Kansas Medical Center, Kansas City 66160-7421, USA. | lld:pubmed |
| pubmed-article:7772054 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:7772054 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:7772054 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
