| pubmed-article:9691094 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9691094 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
| pubmed-article:9691094 | lifeskim:mentions | umls-concept:C1135918 | lld:lifeskim |
| pubmed-article:9691094 | lifeskim:mentions | umls-concept:C0264956 | lld:lifeskim |
| pubmed-article:9691094 | lifeskim:mentions | umls-concept:C0017262 | lld:lifeskim |
| pubmed-article:9691094 | lifeskim:mentions | umls-concept:C0054874 | lld:lifeskim |
| pubmed-article:9691094 | lifeskim:mentions | umls-concept:C0033268 | lld:lifeskim |
| pubmed-article:9691094 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
| pubmed-article:9691094 | lifeskim:mentions | umls-concept:C2911684 | lld:lifeskim |
| pubmed-article:9691094 | lifeskim:mentions | umls-concept:C0185117 | lld:lifeskim |
| pubmed-article:9691094 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:9691094 | pubmed:dateCreated | 1998-8-26 | lld:pubmed |
| pubmed-article:9691094 | pubmed:abstractText | Formation of the atherosclerotic intima must involve altered metabolism of the elastin-rich arterial extracellular matrix. Proteases potentially involved in these processes remain unclear. This study examined the expression of the potent elastases cathepsins S and K in human atheroma. Normal arteries contained little or no cathepsin K or S. In contrast, macrophages in atheroma contained abundant immunoreactive cathepsins K and S. Intimal smooth muscle cells (SMC), especially cells appearing to traverse the internal elastic laminae, also contained these enzymes. Extracts of atheromatous tissues had approximately twofold greater elastase-specific activity than extracts of uninvolved arteries, mostly due to cysteine proteases. Cultured human SMC displayed no immunoreactive cathepsins K and S and exhibited little or no elastolytic activity when incubated with insoluble elastin. SMC stimulated with the atheroma-associated cytokines IL-1beta or IFN-gamma secreted active cathepsin S and degraded substantial insoluble elastin (15-20 microg/10(6) cells/24 h). A selective inhibitor of cathepsin S blocked > 80% of this elastolytic activity. The presence of cathepsins K and S at sites of vascular matrix remodeling and the ability of SMC and macrophages to use these enzymes to degrade elastin supports a role for elastolytic cathepsins in vessel wall remodeling and identifies novel therapeutic targets in regulating plaque stability. | lld:pubmed |
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| pubmed-article:9691094 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9691094 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9691094 | pubmed:citationSubset | AIM | lld:pubmed |
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| pubmed-article:9691094 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9691094 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:9691094 | pubmed:issn | 0021-9738 | lld:pubmed |
| pubmed-article:9691094 | pubmed:author | pubmed-author:SukhovaG KGK | lld:pubmed |
| pubmed-article:9691094 | pubmed:author | pubmed-author:ChapmanH AHA | lld:pubmed |
| pubmed-article:9691094 | pubmed:author | pubmed-author:LibbyPP | lld:pubmed |
| pubmed-article:9691094 | pubmed:author | pubmed-author:SimonD IDI | lld:pubmed |
| pubmed-article:9691094 | pubmed:author | pubmed-author:ShiG PGP | lld:pubmed |
| pubmed-article:9691094 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9691094 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:9691094 | pubmed:volume | 102 | lld:pubmed |
| pubmed-article:9691094 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9691094 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9691094 | pubmed:pagination | 576-83 | lld:pubmed |
| pubmed-article:9691094 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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| pubmed-article:9691094 | pubmed:year | 1998 | lld:pubmed |
| pubmed-article:9691094 | pubmed:articleTitle | Expression of the elastolytic cathepsins S and K in human atheroma and regulation of their production in smooth muscle cells. | lld:pubmed |
| pubmed-article:9691094 | pubmed:affiliation | Brigham and Women's Hospital, Vascular Medicine and Atherosclerosis Unit and Cardiovascular and Respiratory Divisions, Department of Medicine, Boston, Massachusetts 02115, USA. | lld:pubmed |
| pubmed-article:9691094 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:9691094 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:9691094 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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