Linked Life Data

11063004

Source:http://linkedlifedata.com/resource/pubmed/id/11063004

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2000-11-9
pubmed:abstractText
The presence of cartilage oligomeric matrix protein (COMP) in extracts of ligament, tendon, meniscus, and canine articular cartilage was demonstrated by Western blot analysis using anti-dog COMP antibody. When the tissues were cultured in the presence of [35-S]methionine/cysteine, metabolically labeled COMP was purified from the culture media and from tissue extracts by DEAE-cellulose gel chromatography. SDS-Polyacrylamide gel electrophoresis (SDS-PAGE) followed by autoradiography and immunoblotting under reducing and non-reducing conditions revealed that COMP is synthesized by the cells of these connective tissues. Increased levels of COMP in samples of both synovial fluid and serum of patients with various joint diseases may not only be derived from cartilage but also from ligaments and tendons. COMP is not a highly tissue-specific cartilage molecule.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0300-8207
pubmed:author
pubmed:issnType
Print
pubmed:volume
39
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
233-44
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1998
pubmed:articleTitle
COMP (cartilage oligomeric matrix protein) is synthesized in ligament, tendon, meniscus, and articular cartilage.
pubmed:affiliation
Institute of Hygiene and Environmental Medicine, University of Griefswald, Germany. muellerg@rz.uni_greifswald
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't