Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2005-9-29
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.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/16192646-10429241, http://linkedlifedata.com/resource/pubmed/commentcorrection/16192646-10671485, http://linkedlifedata.com/resource/pubmed/commentcorrection/16192646-10693864, http://linkedlifedata.com/resource/pubmed/commentcorrection/16192646-11315916, http://linkedlifedata.com/resource/pubmed/commentcorrection/16192646-11382594, http://linkedlifedata.com/resource/pubmed/commentcorrection/16192646-11953972, http://linkedlifedata.com/resource/pubmed/commentcorrection/16192646-12731883, http://linkedlifedata.com/resource/pubmed/commentcorrection/16192646-1689939, http://linkedlifedata.com/resource/pubmed/commentcorrection/16192646-203207, http://linkedlifedata.com/resource/pubmed/commentcorrection/16192646-2180568, http://linkedlifedata.com/resource/pubmed/commentcorrection/16192646-2366031, http://linkedlifedata.com/resource/pubmed/commentcorrection/16192646-2461702, http://linkedlifedata.com/resource/pubmed/commentcorrection/16192646-2503510, http://linkedlifedata.com/resource/pubmed/commentcorrection/16192646-2542542, http://linkedlifedata.com/resource/pubmed/commentcorrection/16192646-3358796, http://linkedlifedata.com/resource/pubmed/commentcorrection/16192646-3838593, http://linkedlifedata.com/resource/pubmed/commentcorrection/16192646-6198355, http://linkedlifedata.com/resource/pubmed/commentcorrection/16192646-6344809, http://linkedlifedata.com/resource/pubmed/commentcorrection/16192646-6851475, http://linkedlifedata.com/resource/pubmed/commentcorrection/16192646-7078441, http://linkedlifedata.com/resource/pubmed/commentcorrection/16192646-7520847, http://linkedlifedata.com/resource/pubmed/commentcorrection/16192646-7628846, http://linkedlifedata.com/resource/pubmed/commentcorrection/16192646-8486933, http://linkedlifedata.com/resource/pubmed/commentcorrection/16192646-8576151, http://linkedlifedata.com/resource/pubmed/commentcorrection/16192646-8653892, http://linkedlifedata.com/resource/pubmed/commentcorrection/16192646-9261109, http://linkedlifedata.com/resource/pubmed/commentcorrection/16192646-9395486
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
AIM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0002-9440
pubmed:author
pubmed:issnType
Print
pubmed:volume
167
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1119-24
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed-meshheading:16192646-Humans, pubmed-meshheading:16192646-Animals, pubmed-meshheading:16192646-Arthritis, Rheumatoid, pubmed-meshheading:16192646-Aged, pubmed-meshheading:16192646-Aged, 80 and over, pubmed-meshheading:16192646-Cattle, pubmed-meshheading:16192646-Synovial Fluid, pubmed-meshheading:16192646-Synovial Membrane, pubmed-meshheading:16192646-Trypsin, pubmed-meshheading:16192646-Molecular Weight, pubmed-meshheading:16192646-Female, pubmed-meshheading:16192646-Male, pubmed-meshheading:16192646-Adult, pubmed-meshheading:16192646-Europium, pubmed-meshheading:16192646-Fluorometry, pubmed-meshheading:16192646-Middle Aged, pubmed-meshheading:16192646-Base Sequence, pubmed-meshheading:16192646-Cells, Cultured, pubmed-meshheading:16192646-RNA, Messenger, pubmed-meshheading:16192646-Trypsinogen, pubmed-meshheading:16192646-Amino Acid Sequence, pubmed-meshheading:16192646-Cell Culture Techniques, pubmed-meshheading:16192646-Electrophoresis, Polyacrylamide Gel, pubmed-meshheading:16192646-Molecular Sequence Data, pubmed-meshheading:16192646-Mass Spectrometry, pubmed-meshheading:16192646-Immunohistochemistry, pubmed-meshheading:16192646-Antibodies, Monoclonal, pubmed-meshheading:16192646-Trypsin Inhibitor, Kazal Pancreatic, pubmed-meshheading:16192646-Collagen Type II
More...