Characterization of monoclonal antibodies recognizing different fragments of cartilage oligomeric matrix protein in human body fluids
Jazyk angličtina Země Spojené státy americké Médium print
Typ dokumentu časopisecké články, práce podpořená grantem, Research Support, U.S. Gov't, P.H.S.
Grantová podpora
1-P50-AR39239
NIAMS NIH HHS - United States
AG04736
NIA NIH HHS - United States
PubMed
9143347
DOI
10.1006/abbi.1997.9941
PII: S0003-9861(97)99941-0
Knihovny.cz E-zdroje
- MeSH
- antigeny imunologie metabolismus MeSH
- chrupavka imunologie MeSH
- chrupavkový oligomerní matrixový protein MeSH
- denzitometrie MeSH
- ELISA MeSH
- epitopy chemie MeSH
- extracelulární matrix - proteiny chemie imunologie metabolismus MeSH
- glykoproteiny chemie imunologie metabolismus MeSH
- kompetitivní vazba MeSH
- konformace proteinů MeSH
- lidé MeSH
- matriliny MeSH
- monoklonální protilátky imunologie metabolismus MeSH
- myši inbrední BALB C MeSH
- myši MeSH
- peptidové fragmenty imunologie metabolismus MeSH
- revmatoidní artritida metabolismus MeSH
- synoviální tekutina chemie imunologie metabolismus MeSH
- trypsin metabolismus MeSH
- western blotting MeSH
- zvířata MeSH
- Check Tag
- lidé MeSH
- myši MeSH
- ženské pohlaví MeSH
- zvířata MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Research Support, U.S. Gov't, P.H.S. MeSH
- Názvy látek
- antigeny MeSH
- chrupavkový oligomerní matrixový protein MeSH
- epitopy MeSH
- extracelulární matrix - proteiny MeSH
- glykoproteiny MeSH
- Matn1 protein, mouse MeSH Prohlížeč
- matriliny MeSH
- monoklonální protilátky MeSH
- peptidové fragmenty MeSH
- trypsin MeSH
- TSP5 protein, human MeSH Prohlížeč
Cartilage oligomeric matrix protein (COMP) is a high-molecular-weight glycoprotein found at a high concentration in articular cartilage. Recent studies have shown that the joint fluid and serum levels of antigenic COMP, measured by an enzyme-linked immunosorbent assay (ELISA) which uses a polyclonal antiserum raised against bovine COMP, provide important information about metabolic changes occurring in the cartilage matrix in joint disease. In this report, we describe the specificity of three monoclonal antibodies (mAbs) to human COMP and their usefulness in quantifying antigenic COMP fragments in body fluids. Two of the mAbs (16-F12 and 18-G3) recognized both oligomeric and monomeric forms of COMP, but the third (17-C10) reacted positively only with the former. Immunoblots of human COMP, predigested with trypsin for up to 6 h, showed that the three mAbs are directed against different epitopes identified on small tryptic fragments of 30 kDa (16-F12), 25 kDa (17-C10), and 40 kDa as well as 30 kDa (18-G3), respectively. The antibodies also recognized a different pattern of fragments in human pathological synovial fluids. This was particularly striking in the case of the medium size fragments (16-F12: 90 and 110 kDa; 17-C10: 70 and 90 kDa; 18-G3: up to five bands from 70 to 130 kDa). Competitive indirect inhibition ELISAs developed with mAbs 16-F12 and 17-C10 revealed further differences in the specificities of these antibodies. Thus, while mAb 16-F12 can be used only to quantify antigenic COMP in human synovial fluid and serum, mAb 17-C10 is useful in addition when analyzing canine and horse synovial fluid as well as canine serum. The results of analyses of synovial fluid samples from patients with osteoarthritis and rheumatoid arthritis provided preliminary evidence in support of the contention that measurement of the different COMP epitopes recognized by these mAbs in body fluids could prove useful in the clinical assessment of patients with joint disease.
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