Measurement of cartilage oligomeric matrix protein (COMP) in normal and diseased equine synovial fluids.
Abstract: This study was designed to assay cartilage oligomeric matrix protein (COMP) in equine synovial fluids and to compare the concentration in synovial fluids from normal horses with joint diseased horses. The relationship between the COMP degradation and the matrix metalloproteinase activity in synovial fluids was also investigated. Methods: Using COMP antigen prepared from equine articular cartilage and murine monoclonal antibody (12C4) raised against human COMP, an inhibition ELISA was developed. COMP in equine synovial fluids from normal and diseased joints was quantified. Metalloproteinase activities were evaluated in the same synovial fluids by a gelatin degradation ELISA. COMP fragments were evaluated qualitatively by Western blotting. Results: The COMP inhibition ELISA was reliable at concentrations of equine COMP between 62.5 and 2000 ng/ml. COMP values in joint fluids in both aseptic and septic joint disease (19.7+/-15.3 and 16.1+/-11.2 microg/ml, respectively) were significantly (P < 0.001) lower than normal (53.2+/-29.0 microg/ml). The molecular sizes of COMP on immunoblots were different between normal and diseased synovial fluids; more fragments were seen in diseased fluids. The aseptic (26.6 +/- 20.6%) and septic joint disease synovial fluids (36.1 +/- 37.5%) had significantly higher (P < 0.02 and 0.002, respectively) gelatinolytic activities than normal (13.6 +/- 13.7%). There was a negative correlation (R = -0.31, P < 0.002) between COMP level and gelatinase activity. Conclusions We conclude that the fragment pattern and the absolute COMP concentration maybe useful for monitoring joint disease, and that COMP degradation in synovial fluids from progressed joint disease may be due to MMP gelatinolytic activity.
Copyright 2001
Publication Date: 2001-03-10 PubMed ID: 11237659DOI: 10.1053/joca.2000.0367Google Scholar: Lookup
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- Journal Article
- Research Support
- Non-U.S. Gov't
Summary
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The research article focuses on a study conducted to determine the levels of cartilage oligomeric matrix protein (COMP) in the synovial fluids of horses both with and without joint disease. It also examines how COMP degradation relates to matrix metalloproteinase (MMP) activity. The findings suggest that the pattern and concentration of COMP could be effective in monitoring joint disease, and that a higher MMP activity may cause COMP degradation in diseased joints.
Study Objective and Methodology
- The aim of this study was to analyze the presence and concentration of cartilage oligomeric matrix protein or COMP in the synovial fluids of horses, both healthy and affected by joint disease. The researchers also aimed to understand the relationship between COMP degradation and matrix metalloproteinase (MMP) activity in the synovial fluids.
- To accomplish this, the scientists developed an inhibition ELISA (enzyme-linked immunosorbent assay), a common laboratory technique used to measure the concentration of substances such as proteins in biological samples. The ELISA was designed using COMP antigen prepared from equine articular cartilage and a specific type of antibody (12C4) that was raised against human COMP.
- The concentration of COMP in the synovial fluids from both healthy and diseased horse joints was then measured. At the same time, the MMP activities in the same synovial fluids were evaluated through a gelatin degradation ELISA. Additionally, the COMP fragments were examined qualitatively using a technique called Western blotting.
Results
- The COMP inhibition ELISA was found to be reliable at concentrations of equine COMP ranging from 62.5 to 2000 ng/ml.
- The studies revealed that COMP values in the joint fluids of horses with both aseptic and septic joint disease were significantly lower than those in healthy horses.
- Furthermore, the molecular sizes of COMP varied between healthy and diseased synovial fluids, with more fragments being observed in diseased fluids.
- The MMP activity recorded in the synovial fluids of horses with both types of joint disease was significantly higher than in healthy horses. This suggested a negative correlation between COMP levels and gelatinase or MMP activity.
Conclusions
- From the results obtained, the researchers concluded that the pattern of COMP fragments and the absolute concentration of COMP could potentially be useful markers for monitoring joint disease in horses.
- Furthermore, it was posited that the degradation of COMP observed in the synovial fluids of horses suffering from advanced joint disease may be attributed to increased MMP activity.
Cite This Article
APA
Misumi K, Vilim V, Clegg PD, Thompson CC, Carter SD.
(2001).
Measurement of cartilage oligomeric matrix protein (COMP) in normal and diseased equine synovial fluids.
Osteoarthritis Cartilage, 9(2), 119-127.
https://doi.org/10.1053/joca.2000.0367 Publication
Researcher Affiliations
- Department of Veterinary Surgery, Kagoshima University, 21-24 Korimoto 1-chome, Kagoshima, 890-0065, Japan.
MeSH Terms
- Animals
- Blotting, Western / methods
- Cartilage Oligomeric Matrix Protein
- Enzyme-Linked Immunosorbent Assay / methods
- Extracellular Matrix Proteins / metabolism
- Gelatin / metabolism
- Glycoproteins / metabolism
- Hindlimb
- Horse Diseases / diagnosis
- Horses
- Joint Diseases / diagnosis
- Joint Diseases / veterinary
- Joints / metabolism
- Matrilin Proteins
- Synovial Fluid / chemistry
Citations
This article has been cited 5 times.- Smith R, Önnerfjord P, Holmgren K, di Grado S, Dudhia J. Development of a Cartilage Oligomeric Matrix Protein Neo-Epitope Assay for the Detection of Intra-Thecal Tendon Disease. Int J Mol Sci 2020 Mar 20;21(6).
- Bourebaba L, Röcken M, Marycz K. Osteochondritis dissecans (OCD) in Horses - Molecular Background of its Pathogenesis and Perspectives for Progenitor Stem Cell Therapy. Stem Cell Rev Rep 2019 Jun;15(3):374-390.
- Wang SH, Shen CY, Weng TC, Lin PH, Yang JJ, Chen IF, Kuo SM, Chang SJ, Tu YK, Kao YH, Hung CH. Detection of cartilage oligomeric matrix protein using a quartz crystal microbalance. Sensors (Basel) 2010;10(12):11633-43.
- Tseng S, Reddi AH, Di Cesare PE. Cartilage Oligomeric Matrix Protein (COMP): A Biomarker of Arthritis. Biomark Insights 2009 Feb 17;4:33-44.
- Anderson JR, Phelan MM, Caamaño-Gutiérrez E, Clegg PD, Rubio-Martinez LM, Peffers MJ. Metabolomic and proteomic stratification of equine osteoarthritis. Equine Vet J 2025 Sep;57(5):1204-1218.
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