pubmed-article:16192646 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:16192646 | lifeskim:mentions | umls-concept:C0003873 | lld:lifeskim |
pubmed-article:16192646 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
pubmed-article:16192646 | lifeskim:mentions | umls-concept:C0040300 | lld:lifeskim |
pubmed-article:16192646 | lifeskim:mentions | umls-concept:C0039103 | lld:lifeskim |
pubmed-article:16192646 | lifeskim:mentions | umls-concept:C0009331 | lld:lifeskim |
pubmed-article:16192646 | lifeskim:mentions | umls-concept:C1510411 | lld:lifeskim |
pubmed-article:16192646 | lifeskim:mentions | umls-concept:C1171362 | lld:lifeskim |
pubmed-article:16192646 | lifeskim:mentions | umls-concept:C0017262 | lld:lifeskim |
pubmed-article:16192646 | lifeskim:mentions | umls-concept:C1515670 | lld:lifeskim |
pubmed-article:16192646 | lifeskim:mentions | umls-concept:C1879547 | lld:lifeskim |
pubmed-article:16192646 | pubmed:issue | 4 | lld:pubmed |
pubmed-article:16192646 | pubmed:dateCreated | 2005-9-29 | lld:pubmed |
pubmed-article:16192646 | pubmed:abstractText | It has traditionally been believed that only the human collagenases (matrix metalloproteinase-1, -8, and -13) are capable of initiating the degradation of collagens. Here, we show that human trypsin-2 is also capable of cleaving the triple helix of human cartilage collagen type II. We purified human trypsin-2 and tumor-associated trypsin inhibitor by affinity chromatography whereas collagen type II was purified from cartilage extracts using pepsin digestion and salt precipitation. Degradation of type II collagen and gelatin by trypsin-2 was demonstrated with sodium dodecyl sulfate-polyacrylamide gel electrophoresis, zymography, and mass spectrometry, and tumor-associated trypsin inhibitor specifically inhibited this degradation. Although human trypsin-2 efficiently digested type II collagen, bovine trypsin did not. Furthermore, immunohistochemical staining detected trypsin-2 in the fibroblast-like synovial lining and in stromal cells of human rheumatoid arthritis synovial membrane. These findings were confirmed by reverse transcriptase-polymerase chain reaction and nucleotide sequencing. Trypsin-2 alone and complexed with alpha(1)-proteinase inhibitor were also detected in the synovial fluid of affected joints by time-resolved immunofluorometric assay, suggesting that trypsin-2 is activated locally. These results are the first to assess the ability of human trypsin to cleave human type II collagen. Thus, trypsin-2 and its regulators should be further studied for use as markers of prognosis and disease activity in rheumatoid arthritis. | lld:pubmed |
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pubmed-article:16192646 | pubmed:language | eng | lld:pubmed |
pubmed-article:16192646 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16192646 | pubmed:citationSubset | AIM | lld:pubmed |
pubmed-article:16192646 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16192646 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16192646 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16192646 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16192646 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16192646 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16192646 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16192646 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16192646 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16192646 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:16192646 | pubmed:month | Oct | lld:pubmed |
pubmed-article:16192646 | pubmed:issn | 0002-9440 | lld:pubmed |
pubmed-article:16192646 | pubmed:author | pubmed-author:StenmanUlf-Hå... | lld:pubmed |
pubmed-article:16192646 | pubmed:author | pubmed-author:KonttinenYrjö... | lld:pubmed |
pubmed-article:16192646 | pubmed:author | pubmed-author:SorsaTimoT | lld:pubmed |
pubmed-article:16192646 | pubmed:author | pubmed-author:BjartellAnder... | lld:pubmed |
pubmed-article:16192646 | pubmed:author | pubmed-author:LuukkainenRei... | lld:pubmed |
pubmed-article:16192646 | pubmed:author | pubmed-author:AinolaMariM | lld:pubmed |
pubmed-article:16192646 | pubmed:author | pubmed-author:ValmuLeenaL | lld:pubmed |
pubmed-article:16192646 | pubmed:author | pubmed-author:StenmanMathia... | lld:pubmed |
pubmed-article:16192646 | pubmed:author | pubmed-author:MaGuofengG | lld:pubmed |
pubmed-article:16192646 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:16192646 | pubmed:volume | 167 | lld:pubmed |
pubmed-article:16192646 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:16192646 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:16192646 | pubmed:pagination | 1119-24 | lld:pubmed |
pubmed-article:16192646 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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