The Experts below are selected from a list of 912 Experts worldwide ranked by ideXlab platform
Hiroshi Sakamoto - One of the best experts on this subject based on the ideXlab platform.
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Analysis of cartilage oligomeric matrix protein (COMP) degradation and synthesis in Equine Joint Disease
Equine veterinary journal, 2010Co-Authors: Koh Arai, Kazuhiro Misumi, Stuart D. Carter, S. Shinbara, Makoto Fujiki, Hiroshi SakamotoAbstract:Summary Reasons for performing study: Cartilage oligomeric matrix protein (COMP) is abundant within cartilage; its turnover and/or degradation have been investigated in various Equine Joint Diseases and it has been suggested that COMP fragmentation might be useful for monitoring such conditions. Objectives: To determine whether COMP metabolism is compromised in Equine osteoarthritis (OA) and whether COMP degradation is a useful Joint marker representing cartilage destruction. Hypothesis: A monoclonal antibody (mAb) with a higher affinity for degraded COMP allows discrimination of Diseased Joints by quantifying COMP levels and fragmentation. Methods: A mAb (clone14G4) was generated against Equine cartilage COMP. The NH2-terminal sequence of enzyme-cut COMP fragments recognised by 14G4 was determined, as was the efficiency of binding to COMP (using a generated COMP peptide). COMP concentration and fragmentation were analysed in synovial fluid (SF) from normal horses and those with OA. Results: The mAb 14G4 had a higher affinity for the smaller fragments of Equine COMP, compared with a mAb (clone 12C4) generated against human COMP. The 14G4 epitope was identified as between C134 and F147. The COMP values in OA (mean ± s.d. 205.8 ± 90.9 μg/ml) were significantly higher than in the normal (133.1 ± 31.5 μg/ml) SF. On the immunoblots of OA sample, the proportions of intact COMP were significantly lower, while smaller fragments ranging from 75 to 290 kDa were higher compared with the normal SF. Conclusions and potential relevance: The mAb 14G4 reliably detects COMP degradation as well as synthesis, and fragmentation analysis combined with quantification in SF could be useful to study Equine OA.
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serum level of cartilage oligomeric matrix protein comp in Equine osteoarthritis
Equine Veterinary Journal, 2010Co-Authors: Kazuhiro Misumi, Makoto Fujiki, Hiroshi Sakamoto, V Vilim, Takashi Hatazoe, T Murata, T Oka, S D CartersAbstract:This study was designed to assay and compare cartilage oligomeric matrix protein (COMP) in horse sera, in samples from normal and Joint Diseased horses, and to investigate the relationships between COMP in sera and synovial fluids (SF) with keratan sulphate (KS) data. Sera from 38 horses free of any Joint pathology (controls) and from horses with aseptic Joint Disease (AJD horses, n = 40) were assayed for COMP and KS concentrations. Of the 78 horses in the study, 53 were also assayed for COMP and KS concentrations in SF. COMP and KS were measured by inhibition ELISA, using monoclonal antibodies 12C4 and 5D4, respectively. The COMP concentration in sera from AJD horses (mean +/- s.d. 10.7 +/- 7.4 microg/ml) was significantly (P<0.02) lower than in control sera (14.8 +/- 7.8 microg/ml). The Joint Disease sera also had significantly lower (P<0.01) KS levels (180.5 +/- 61.8 ng/ml) than controls (237.1 +/- 116.1 ng/ml). A significant correlation (r = 0.52, n = 53, P<0.001) was seen between serum and SF in COMP levels; no such relationship was seen in KS levels. It is possible that serum COMP concentration could be a more specific marker of Equine Joint Disease than any other described to date.
Kazuhiro Misumi - One of the best experts on this subject based on the ideXlab platform.
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Analysis of cartilage oligomeric matrix protein (COMP) degradation and synthesis in Equine Joint Disease
Equine veterinary journal, 2010Co-Authors: Koh Arai, Kazuhiro Misumi, Stuart D. Carter, S. Shinbara, Makoto Fujiki, Hiroshi SakamotoAbstract:Summary Reasons for performing study: Cartilage oligomeric matrix protein (COMP) is abundant within cartilage; its turnover and/or degradation have been investigated in various Equine Joint Diseases and it has been suggested that COMP fragmentation might be useful for monitoring such conditions. Objectives: To determine whether COMP metabolism is compromised in Equine osteoarthritis (OA) and whether COMP degradation is a useful Joint marker representing cartilage destruction. Hypothesis: A monoclonal antibody (mAb) with a higher affinity for degraded COMP allows discrimination of Diseased Joints by quantifying COMP levels and fragmentation. Methods: A mAb (clone14G4) was generated against Equine cartilage COMP. The NH2-terminal sequence of enzyme-cut COMP fragments recognised by 14G4 was determined, as was the efficiency of binding to COMP (using a generated COMP peptide). COMP concentration and fragmentation were analysed in synovial fluid (SF) from normal horses and those with OA. Results: The mAb 14G4 had a higher affinity for the smaller fragments of Equine COMP, compared with a mAb (clone 12C4) generated against human COMP. The 14G4 epitope was identified as between C134 and F147. The COMP values in OA (mean ± s.d. 205.8 ± 90.9 μg/ml) were significantly higher than in the normal (133.1 ± 31.5 μg/ml) SF. On the immunoblots of OA sample, the proportions of intact COMP were significantly lower, while smaller fragments ranging from 75 to 290 kDa were higher compared with the normal SF. Conclusions and potential relevance: The mAb 14G4 reliably detects COMP degradation as well as synthesis, and fragmentation analysis combined with quantification in SF could be useful to study Equine OA.
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serum level of cartilage oligomeric matrix protein comp in Equine osteoarthritis
Equine Veterinary Journal, 2010Co-Authors: Kazuhiro Misumi, Makoto Fujiki, Hiroshi Sakamoto, V Vilim, Takashi Hatazoe, T Murata, T Oka, S D CartersAbstract:This study was designed to assay and compare cartilage oligomeric matrix protein (COMP) in horse sera, in samples from normal and Joint Diseased horses, and to investigate the relationships between COMP in sera and synovial fluids (SF) with keratan sulphate (KS) data. Sera from 38 horses free of any Joint pathology (controls) and from horses with aseptic Joint Disease (AJD horses, n = 40) were assayed for COMP and KS concentrations. Of the 78 horses in the study, 53 were also assayed for COMP and KS concentrations in SF. COMP and KS were measured by inhibition ELISA, using monoclonal antibodies 12C4 and 5D4, respectively. The COMP concentration in sera from AJD horses (mean +/- s.d. 10.7 +/- 7.4 microg/ml) was significantly (P<0.02) lower than in control sera (14.8 +/- 7.8 microg/ml). The Joint Disease sera also had significantly lower (P<0.01) KS levels (180.5 +/- 61.8 ng/ml) than controls (237.1 +/- 116.1 ng/ml). A significant correlation (r = 0.52, n = 53, P<0.001) was seen between serum and SF in COMP levels; no such relationship was seen in KS levels. It is possible that serum COMP concentration could be a more specific marker of Equine Joint Disease than any other described to date.
Makoto Fujiki - One of the best experts on this subject based on the ideXlab platform.
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Analysis of cartilage oligomeric matrix protein (COMP) degradation and synthesis in Equine Joint Disease
Equine veterinary journal, 2010Co-Authors: Koh Arai, Kazuhiro Misumi, Stuart D. Carter, S. Shinbara, Makoto Fujiki, Hiroshi SakamotoAbstract:Summary Reasons for performing study: Cartilage oligomeric matrix protein (COMP) is abundant within cartilage; its turnover and/or degradation have been investigated in various Equine Joint Diseases and it has been suggested that COMP fragmentation might be useful for monitoring such conditions. Objectives: To determine whether COMP metabolism is compromised in Equine osteoarthritis (OA) and whether COMP degradation is a useful Joint marker representing cartilage destruction. Hypothesis: A monoclonal antibody (mAb) with a higher affinity for degraded COMP allows discrimination of Diseased Joints by quantifying COMP levels and fragmentation. Methods: A mAb (clone14G4) was generated against Equine cartilage COMP. The NH2-terminal sequence of enzyme-cut COMP fragments recognised by 14G4 was determined, as was the efficiency of binding to COMP (using a generated COMP peptide). COMP concentration and fragmentation were analysed in synovial fluid (SF) from normal horses and those with OA. Results: The mAb 14G4 had a higher affinity for the smaller fragments of Equine COMP, compared with a mAb (clone 12C4) generated against human COMP. The 14G4 epitope was identified as between C134 and F147. The COMP values in OA (mean ± s.d. 205.8 ± 90.9 μg/ml) were significantly higher than in the normal (133.1 ± 31.5 μg/ml) SF. On the immunoblots of OA sample, the proportions of intact COMP were significantly lower, while smaller fragments ranging from 75 to 290 kDa were higher compared with the normal SF. Conclusions and potential relevance: The mAb 14G4 reliably detects COMP degradation as well as synthesis, and fragmentation analysis combined with quantification in SF could be useful to study Equine OA.
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serum level of cartilage oligomeric matrix protein comp in Equine osteoarthritis
Equine Veterinary Journal, 2010Co-Authors: Kazuhiro Misumi, Makoto Fujiki, Hiroshi Sakamoto, V Vilim, Takashi Hatazoe, T Murata, T Oka, S D CartersAbstract:This study was designed to assay and compare cartilage oligomeric matrix protein (COMP) in horse sera, in samples from normal and Joint Diseased horses, and to investigate the relationships between COMP in sera and synovial fluids (SF) with keratan sulphate (KS) data. Sera from 38 horses free of any Joint pathology (controls) and from horses with aseptic Joint Disease (AJD horses, n = 40) were assayed for COMP and KS concentrations. Of the 78 horses in the study, 53 were also assayed for COMP and KS concentrations in SF. COMP and KS were measured by inhibition ELISA, using monoclonal antibodies 12C4 and 5D4, respectively. The COMP concentration in sera from AJD horses (mean +/- s.d. 10.7 +/- 7.4 microg/ml) was significantly (P<0.02) lower than in control sera (14.8 +/- 7.8 microg/ml). The Joint Disease sera also had significantly lower (P<0.01) KS levels (180.5 +/- 61.8 ng/ml) than controls (237.1 +/- 116.1 ng/ml). A significant correlation (r = 0.52, n = 53, P<0.001) was seen between serum and SF in COMP levels; no such relationship was seen in KS levels. It is possible that serum COMP concentration could be a more specific marker of Equine Joint Disease than any other described to date.
S D Carters - One of the best experts on this subject based on the ideXlab platform.
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serum level of cartilage oligomeric matrix protein comp in Equine osteoarthritis
Equine Veterinary Journal, 2010Co-Authors: Kazuhiro Misumi, Makoto Fujiki, Hiroshi Sakamoto, V Vilim, Takashi Hatazoe, T Murata, T Oka, S D CartersAbstract:This study was designed to assay and compare cartilage oligomeric matrix protein (COMP) in horse sera, in samples from normal and Joint Diseased horses, and to investigate the relationships between COMP in sera and synovial fluids (SF) with keratan sulphate (KS) data. Sera from 38 horses free of any Joint pathology (controls) and from horses with aseptic Joint Disease (AJD horses, n = 40) were assayed for COMP and KS concentrations. Of the 78 horses in the study, 53 were also assayed for COMP and KS concentrations in SF. COMP and KS were measured by inhibition ELISA, using monoclonal antibodies 12C4 and 5D4, respectively. The COMP concentration in sera from AJD horses (mean +/- s.d. 10.7 +/- 7.4 microg/ml) was significantly (P<0.02) lower than in control sera (14.8 +/- 7.8 microg/ml). The Joint Disease sera also had significantly lower (P<0.01) KS levels (180.5 +/- 61.8 ng/ml) than controls (237.1 +/- 116.1 ng/ml). A significant correlation (r = 0.52, n = 53, P<0.001) was seen between serum and SF in COMP levels; no such relationship was seen in KS levels. It is possible that serum COMP concentration could be a more specific marker of Equine Joint Disease than any other described to date.
Koh Arai - One of the best experts on this subject based on the ideXlab platform.
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Analysis of cartilage oligomeric matrix protein (COMP) degradation and synthesis in Equine Joint Disease
Equine veterinary journal, 2010Co-Authors: Koh Arai, Kazuhiro Misumi, Stuart D. Carter, S. Shinbara, Makoto Fujiki, Hiroshi SakamotoAbstract:Summary Reasons for performing study: Cartilage oligomeric matrix protein (COMP) is abundant within cartilage; its turnover and/or degradation have been investigated in various Equine Joint Diseases and it has been suggested that COMP fragmentation might be useful for monitoring such conditions. Objectives: To determine whether COMP metabolism is compromised in Equine osteoarthritis (OA) and whether COMP degradation is a useful Joint marker representing cartilage destruction. Hypothesis: A monoclonal antibody (mAb) with a higher affinity for degraded COMP allows discrimination of Diseased Joints by quantifying COMP levels and fragmentation. Methods: A mAb (clone14G4) was generated against Equine cartilage COMP. The NH2-terminal sequence of enzyme-cut COMP fragments recognised by 14G4 was determined, as was the efficiency of binding to COMP (using a generated COMP peptide). COMP concentration and fragmentation were analysed in synovial fluid (SF) from normal horses and those with OA. Results: The mAb 14G4 had a higher affinity for the smaller fragments of Equine COMP, compared with a mAb (clone 12C4) generated against human COMP. The 14G4 epitope was identified as between C134 and F147. The COMP values in OA (mean ± s.d. 205.8 ± 90.9 μg/ml) were significantly higher than in the normal (133.1 ± 31.5 μg/ml) SF. On the immunoblots of OA sample, the proportions of intact COMP were significantly lower, while smaller fragments ranging from 75 to 290 kDa were higher compared with the normal SF. Conclusions and potential relevance: The mAb 14G4 reliably detects COMP degradation as well as synthesis, and fragmentation analysis combined with quantification in SF could be useful to study Equine OA.