| pubmed-article:10788434 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10788434 | lifeskim:mentions | umls-concept:C0026339 | lld:lifeskim |
| pubmed-article:10788434 | lifeskim:mentions | umls-concept:C0026336 | lld:lifeskim |
| pubmed-article:10788434 | lifeskim:mentions | umls-concept:C0009325 | lld:lifeskim |
| pubmed-article:10788434 | lifeskim:mentions | umls-concept:C0020291 | lld:lifeskim |
| pubmed-article:10788434 | lifeskim:mentions | umls-concept:C0030956 | lld:lifeskim |
| pubmed-article:10788434 | lifeskim:mentions | umls-concept:C0623362 | lld:lifeskim |
| pubmed-article:10788434 | pubmed:issue | 18 | lld:pubmed |
| pubmed-article:10788434 | pubmed:dateCreated | 2000-6-1 | lld:pubmed |
| pubmed-article:10788434 | pubmed:abstractText | The matrix metalloproteinase (MMP) family has been implicated in the process of a variety of diseases such as arthritis, atherosclerosis, and tumor cell metastasis. To study the mechanisms of MMP action on collagenous substrates, we have constructed homotrimeric triple-helical peptide (THP) models of the collagenase cleavage sites in types I and II collagen. The THPs incorporate either the alpha1(I)772-786 or the alpha1(II)772-783 sequence. The alpha1(I)772-786 and alpha1(II)772-783 THPs were hydrolyzed by MMP-1 at the Gly-Ile and Gly-Leu bonds, respectively, analogous to the bonds cleaved in corresponding native collagens. Thus, the THPs contained all necessary information to direct MMP-1 binding and proteolysis. Subsequent investigations using the alpha1(I)772-786 THP showed hydrolysis by MMP-2, MMP-13, and a COOH-terminal domain-deleted MMP-1 (MMP-1(Delta(243-450))) but not by MMP-3 or a COOH-terminal domain-deleted MMP-3 (MMP-3(Delta(248-460))). Kinetic analyses showed a k(cat)/K(m) value of 1,808 s(-1) m(-1) for MMP-1 hydrolysis of alpha1(I)772-786 THP, approximately 10-fold lower than for type I collagen. The effect is caused primarily by relative K(m) values. MMP-2 and MMP-13 cleaved the THP more rapidly than MMP-1, but MMP-2 cleavage occurred at distinct multiple sites. Comparison of MMP-1 and MMP-1(Delta(243-450)) hydrolysis of alpha1(I)772-786 THP showed that both can cleave a triple-helical substrate with a slightly higher K(m) value for MMP-1(Delta(243-450)). We propose that the COOH-terminal domain of MMPs is necessary for orienting whole, native collagen molecules but may not be necessary for binding to and cleaving a THP. This proposal is consistent with the large distance between the MMP-1 catalytic and COOH-terminal domains observed by three-dimensional structural analysis and supports previous suggestions that the features of the catalytic domain contribute significantly toward enzyme specificity. | lld:pubmed |
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| pubmed-article:10788434 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10788434 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10788434 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:10788434 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:10788434 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10788434 | pubmed:month | May | lld:pubmed |
| pubmed-article:10788434 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:10788434 | pubmed:author | pubmed-author:NagaseHH | lld:pubmed |
| pubmed-article:10788434 | pubmed:author | pubmed-author:FieldsG BGB | lld:pubmed |
| pubmed-article:10788434 | pubmed:author | pubmed-author:Lauer-FieldsJ... | lld:pubmed |
| pubmed-article:10788434 | pubmed:author | pubmed-author:TuzinskiK AKA | lld:pubmed |
| pubmed-article:10788434 | pubmed:author | pubmed-author:ShimokawaK iK | lld:pubmed |
| pubmed-article:10788434 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10788434 | pubmed:day | 5 | lld:pubmed |
| pubmed-article:10788434 | pubmed:volume | 275 | lld:pubmed |
| pubmed-article:10788434 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10788434 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10788434 | pubmed:pagination | 13282-90 | lld:pubmed |
| pubmed-article:10788434 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:10788434 | pubmed:meshHeading | pubmed-meshheading:10788434... | lld:pubmed |
| pubmed-article:10788434 | pubmed:meshHeading | pubmed-meshheading:10788434... | lld:pubmed |
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| pubmed-article:10788434 | pubmed:meshHeading | pubmed-meshheading:10788434... | lld:pubmed |
| pubmed-article:10788434 | pubmed:meshHeading | pubmed-meshheading:10788434... | lld:pubmed |
| pubmed-article:10788434 | pubmed:meshHeading | pubmed-meshheading:10788434... | lld:pubmed |
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| pubmed-article:10788434 | pubmed:meshHeading | pubmed-meshheading:10788434... | lld:pubmed |
| pubmed-article:10788434 | pubmed:year | 2000 | lld:pubmed |
| pubmed-article:10788434 | pubmed:articleTitle | Hydrolysis of triple-helical collagen peptide models by matrix metalloproteinases. | lld:pubmed |
| pubmed-article:10788434 | pubmed:affiliation | Department of Chemistry and Biochemistry, Florida Atlantic University, Boca Raton, Florida 33431-0991, USA. fieldsg@fau.edu | lld:pubmed |
| pubmed-article:10788434 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10788434 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:10788434 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| entrez-gene:4322 | entrezgene:pubmed | pubmed-article:10788434 | lld:entrezgene |
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