Linked Life Data

11874987

Source:http://linkedlifedata.com/resource/pubmed/id/11874987

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2002-3-4
pubmed:abstractText
During acute inflammation, leukocytes release proteolytic enzymes including matrix metalloproteinases (MMPs), but the physiopathological mechanisms and consequences of this process are not yet fully understood. Neutrophils, the predominant leukocyte type, produce neutrophil collagenase (MMP-8) and gelatinase B (MMP-9) but not the tissue inhibitors of MMPs. After stimulation, these cells also activate MMPs chemically. In arthritic diseases, neutrophils undergo great chemoattraction to the synovium, are activated by interleukin-8, and are stimulated to release gelatinase B in vivo. Production levels and net activities of gelatinase B were found to be absent in degenerative osteoarthritis but significantly increased in rheumatoid arthritis. The cleavage sites in cartilage type II collagen by gelatinase B were determined by a combination of reverse phase high-performance liquid chromatography, Edman degradation, and mass spectrometry analysis. The analysis revealed the site specificity of proline and lysine hydroxylations and O-linked glycosylation, the cleavage specificities by gelatinase B, and the preferential absence and presence of post-translational modifications at P2' and P5', respectively. Furthermore, gelatinase B leaves the immunodominant peptides intact, which are known from studies with (autoreactive) T cells. Lysine hydroxylation was detected at a critical position for T-cell activation. These data lend support to the thesis that extracellular proteolysis and other post-translational modifications of antigenic peptides may be critical in the establishment and perpetuation of autoimmune processes.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
1530-6860
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
16
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
379-89
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:11874987-Amino Acid Sequence, pubmed-meshheading:11874987-Animals, pubmed-meshheading:11874987-Arthritis, Rheumatoid, pubmed-meshheading:11874987-Binding Sites, pubmed-meshheading:11874987-Cattle, pubmed-meshheading:11874987-Collagen Type II, pubmed-meshheading:11874987-Humans, pubmed-meshheading:11874987-Immunodominant Epitopes, pubmed-meshheading:11874987-Interleukin-8, pubmed-meshheading:11874987-Matrix Metalloproteinase 9, pubmed-meshheading:11874987-Models, Immunological, pubmed-meshheading:11874987-Molecular Sequence Data, pubmed-meshheading:11874987-Neutrophils, pubmed-meshheading:11874987-Peptide Fragments, pubmed-meshheading:11874987-Protein Denaturation, pubmed-meshheading:11874987-Protein Processing, Post-Translational, pubmed-meshheading:11874987-Substrate Specificity, pubmed-meshheading:11874987-Synovial Fluid
pubmed:year
2002
pubmed:articleTitle
Cleavage of denatured natural collagen type II by neutrophil gelatinase B reveals enzyme specificity, post-translational modifications in the substrate, and the formation of remnant epitopes in rheumatoid arthritis.
pubmed:affiliation
Rega Institute for Medical Research, Laboratory of Molecular Immunology, University of Leuven, 3000 Leuven, Belgium.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't