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See detailPlasma concentrations of a type II collagen-derived peptide and its nitrated form in growing ardenner sound horses and in horses suffering from juvenile digital degenerative osteoarthropathy
Lejeune, Jean-Philippe ULg; Serteyn, Didier ULg; Gangl, Monika et al

in Veterinary Research Communications (2007), 31(5), 591-601

Several breeds of draft horses suffer from degenerative digital osteoarthropathy, resulting in a reduced active lifespan. A group of 30 Ardenner horses was followed, in standardized conditions, from 15 to ... [more ▼]

Several breeds of draft horses suffer from degenerative digital osteoarthropathy, resulting in a reduced active lifespan. A group of 30 Ardenner horses was followed, in standardized conditions, from 15 to 28 months of age to detect the early manifestations of the disease. The severity of the disease was assessed according to a personal grading system including clinical and radiographic items. Coll 2-1, a peptide of the helical region of type II collagen, and its nitrated form (Coll 2-1 NO2) were assayed in blood plasma collected at 452 +/- 18 days, 504 +/- 20 days, 558 +/- 18 days, 613 +/- 19 days, 675 +/- 19 days, 752 +/- 21 days and 852 +/- 19 days of age. At the end of the follow-up period, 53.3% of Ardenner horses were affected by a degenerative digital osteoarthropathy. A significant effect (p < 0.05) of time, sex and pathology was observed for Coll 2-1 NO2. Variations of Coll 2-1 were not significant except for the time effect. The elevation of Coll 2-1 NO2 in the pathological group could indicate an inflammatory process during the growth of the affected horses, as nitration of tyrosine is mediated through reactive oxygen/nitrogen species and/or myeloperoxidase activity. Coll 2-1 NO2 appears to be an interesting early marker of cartilage degradation and oxidation in degenerative osteoarthropathy. [less ▲]

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See detailType II collagen markers in osteoarthritis: what do they indicate?
Henrotin, Yves ULg; Addison, Shelby; Kraus, Virginia et al

in Current Opinion in Rheumatology (2007), 19(5), 444-50

PURPOSE OF REVIEW: We provide a critical review of recent in-vitro, animal and human clinical studies on type II collagen biomarkers. In describing the human studies, we have applied the BIPED (burden of ... [more ▼]

PURPOSE OF REVIEW: We provide a critical review of recent in-vitro, animal and human clinical studies on type II collagen biomarkers. In describing the human studies, we have applied the BIPED (burden of disease, investigative, prognostic, efficacy of intervention, and diagnostic) classification scheme recently proposed by the Osteoarthritis Biomarkers Network (a consortium of five US National Institutes of Health designated sites). Based on this analysis, we propose an update to the classification of the type II collagen biomarkers. RECENT FINDINGS: Various type II collagen epitopes have been described as potential biomarkers for osteoarthritis. Some have demonstrated ability in the following areas: classification of individuals as either diseased or nondiseased; assessment of severity or extent of osteoarthritis; prediction of future onset of osteoarthritis among those without osteoarthritis at baseline or the progression of osteoarthritis among those with existing disease; and monitoring treatment efficacy. SUMMARY: Type II collagen biomarkers provide useful information for clinical and research applications. Furthermore, they are promising tools for the monitoring the influence of drug treatment on cartilage metabolism in joint diseases such as osteoarthritis. [less ▲]

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See detailA type II-collagen derived peptide and its nitrated form as new markers of inflammation and cartilage degradation in equine osteochondral lesions.
Gangl, Monika; Deberg, Michelle ULg; Lejeune, Jean-Philippe ULg et al

in Research in Veterinary Science (2007), 82

Markers of cartilage breakdown enable studying the degradation of cartilage matrix in equine joint pathologies. This study was designed to determine the levels of Coll2-1, a peptide of the triple helix of ... [more ▼]

Markers of cartilage breakdown enable studying the degradation of cartilage matrix in equine joint pathologies. This study was designed to determine the levels of Coll2-1, a peptide of the triple helix of type II collagen, and Coll2-1NO(2), its nitrated form in the plasma of healthy horses (controls; n=37) and horses suffering from osteochondrosis (n=34). Clinical and arthroscopic scores were attributed reflecting the severity of lesions and were related to the plasma levels of Coll2-1 and Coll2-1NO(2). The median of Coll2-1 was significantly higher in the control group, whereas the mean of Coll2-1NO(2) showed significant elevation in the pathological group. However, the measurement means of scoring classes did not vary significantly. The markers were able to differentiate the group of horses suffering from osteochondrosis from the group of healthy horses. The elevation of Coll2-1NO(2) in the pathological group indicates an inflammation, mediated through reactive oxygen species and/or increased myeloperoxidase activity. [less ▲]

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See detailStudy of the in vitro conditions promoting hypertrophic differentiation of osteoarthritic articular chondrocytes
Sanchez, Christelle ULg; Deberg, Michelle ULg; Msika, Philippe et al

in Osteoarthritis and Cartilage (2007), 15(Suppl C), 109-110

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See detailFollow-up of COLL2-1, COLL2-1NO2 and myeloperoxidase serum levels in marathon runners
Deberg, Michelle ULg; Labasse, Alain ULg; Sanchez, Christelle ULg et al

in Osteoarthritis and Cartilage (2007), 15(Suppl C), 67

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See detailEtude des conditions in vitro favorables à la differenciation hypertrophique des chondrocytes articulaires arthrosiques
Sanchez, Christelle ULg; Deberg, Michelle ULg; Msika, Philippe et al

in Revue du Rhumatisme (2007), 74(10-11), 1085-1086

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See detailAvocado/soybean unsaponifiables prevent the inhibitory effect of osteoarthritic subchondral osteoblasts on aggrecan and type II collagen synthesis by chondrocytes
Henrotin, Yves ULg; Deberg, Michelle ULg; Crielaard, Jean-Michel ULg et al

in Journal of Rheumatology (2006), 33(8), 1668-1678

Objective. To determine the effects of avocado/soybean unsaponifiables (ASU) on osteoblast-induced dysregulation of chondrocyte metabolism. Methods. Human chondrocytes were isolated from osteoarthritis ... [more ▼]

Objective. To determine the effects of avocado/soybean unsaponifiables (ASU) on osteoblast-induced dysregulation of chondrocyte metabolism. Methods. Human chondrocytes were isolated from osteoarthritis (OA) cartilage and cultured in alginate beads for 4 or 10 days in the absence or presence of osteoblasts isolated from nonsclerotic (NSC) or sclerotic (SC) zones of OA subchondral bone plate in monolayer. Before co-culture, osteoblasts were incubated or not with 10 mu g/ml ASU for 72 hours. Aggrecan, type 11 collagen, matrix metalloproteinase-3 (MMP-3) and MMP-13, tissue inhibitor of metalloproteinase (TIMP-1), transforming growth factor-beta 1 (TGF-beta 1) and TGF-beta 3, inducible NO synthase (iNOS), and cyclooxygenase-2 (COX-2) mRNA levels in chondrocytes were quantified by RT-PCR. Aggrecan, osteocalcin, TGF-beta 1, interleukin 18 (IL-1 beta), and IL-6 production were assayed by inummoassays. Results. In co-culture, SC osteoblasts induced a significant inhibition of matrix protein production and a significant increase of MMP synthesis by chondrocytes. In contrast, SC osteoblasts did not modify TIMP-1, TGF-beta 1 and TGF-beta 3, iNOS, or COX-2 mRNA levels in chondrocytes. The pretreatment of SC osteoblasts with ASU fully prevented the inhibitory effects of SC osteoblasts on matrix component production, and even significantly increased type 11 collagen mRNA level over the control (chondrocytes alone) value. In contrast, pretreatment of SC osteoblasts with ASU did not significantly modify the expression of NIMP, TIMP-1, TGF-beta 1, TGF-beta 3, iNOS, or COX-2 gene by chondrocytes. Conclusion. ASU prevent the osteoarthritic osteoblast-induced inhibition of matrix molecule production, suggesting that this compound may promote OA cartilage repair by acting on subchondral bone osteoblasts. This finding constitutes a new mechanism of action for this compound, known for its beneficial effects on cartilage. [less ▲]

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See detailInterleukin-6 mediates subchondral osteoblasts-induced cartilage degradation
Sanchez, Christelle ULg; Kaut, Elisabeth; Deberg, Michelle ULg et al

in Osteoporosis International (2006, March), 17(Suppl. 1), 53

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See detailOsteoblasts from the sclerotic subchondral bone downregulate aggrecan but upregulate metalloproteinases expression by chondrocytes. This effect is mimicked by interleukin-6, -1 beta and oncostatin M pre-treated non-sclerotic osteoblasts
Sanchez, Christelle ULg; Deberg, Michelle ULg; Piccardi, Nathalie et al

in Osteoarthritis and Cartilage (2005), 13(11), 979-987

OBJECTIVE: To determine the effects of osteoarthritic (OA) subchondral osteoblasts on the metabolism of human OA chondrocytes in alginate beads. METHODS: Human chondrocytes were isolated from OA cartilage ... [more ▼]

OBJECTIVE: To determine the effects of osteoarthritic (OA) subchondral osteoblasts on the metabolism of human OA chondrocytes in alginate beads. METHODS: Human chondrocytes were isolated from OA cartilage and cultured in alginate beads for 4 days in the absence or in the presence of osteoblasts isolated from non-sclerotic (N) or sclerotic (SC) zones of human OA subchondral bone in monolayer (co-culture system). Before co-culture, osteoblasts were incubated for 72 h with or without 1.7ng/ml interleukin (IL)-1beta, 100 ng/ml IL-6 with its soluble receptor (50 ng/ml) or 10 ng/ml oncostatin M (OSM). Aggrecan (AGG) and matrix metalloproteases (MMP)-3 and -13 mRNA levels in chondrocytes were quantified by real-time polymerase chain reaction. AGG production was assayed by a specific enzyme amplified sensitivity immunoassay. RESULTS: SC, but not N, osteoblasts induced a significant inhibition of AGG production and AGG gene expression by human OA chondrocytes in alginate beads, and significantly increased MMP-3 and MMP-13 gene expression by chondrocytes. When they were pre-incubated with IL-1beta, IL-6 or OSM, N osteoblasts inhibited AGG synthesis and increased MMP-3 and -13 gene expression by chondrocytes in alginate beads in a same order of magnitude as SC osteoblasts. CONCLUSIONS: These results demonstrate that SC OA subchondral osteoblasts could contribute to cartilage degradation by stimulating chondrocytes to produce more MMP and also by inhibiting AGG synthesis. [less ▲]

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See detailSubchondral bone osteoblasts induce phenotypic changes in human osteoarthritic chondrocytes
Sanchez, Christelle ULg; Deberg, Michelle ULg; Piccardi, Nathalie et al

in Osteoarthritis and Cartilage (2005), 13(11), 988-997

Objective: To determine the influence of osteoarthritic (OA) phenotype of subchondral osteoblasts on the phenotype of human chondrocytes Methods: Human chondrocytes were isolated from CA cartilage and ... [more ▼]

Objective: To determine the influence of osteoarthritic (OA) phenotype of subchondral osteoblasts on the phenotype of human chondrocytes Methods: Human chondrocytes were isolated from CA cartilage and cultured in alginate beads for 4 or 10 days in the absence or in the presence of osteoblasts in monolayer. The osteoblasts were either isolated from non-sclerotic (N) or sclerotic (SC) zones of human subchondral bone. Before co-culture, osteoblasts were incubated for 72 h with or without 1.7 ng/ml interleukin (IL)-1 beta, 100 ng/ml IL-6 with its soluble receptor (50 ng/ml) or 10 ng/ml oncostatin M. SOX9, type I, II and X collagen (COL1, COL2, COL10), osteoblasts-stimulating factor (OSF)-1, bone alkaline phosphatase (ALP), parathyroid hormone related peptide (PTHrP) and its receptor (PTH-R) messenger RNA (mRNA) levels in chondrocytes were quantified by real-time polymerase chain reaction. Results: In comparison with chondrocytes cultured alone in alginate beads, chondrocytes after 4 days in co-culture with N or SC osteoblasts expressed significantly less SOX9 and COL2 mRNA. The decrease of SOX9 and COL2 gene expression was significantly more pronounced in the presence of SC than in the presence of N osteoblasts (P < 0.001). OSF-1 mRNA level in chondrocyte was increased by both N and SC osteoblasts, but to a larger extent by SC osteoblasts (P < 0.001). PTHrP expression in chondrocytes was 21 -fold increased by N osteoblasts but four-fold inhibited by SC osteoblasts. PTHrP secretion was also increased by N but reduced by SC osteoblasts. SC, but not N osteoblasts, induced a significant decrease of PTH-R gene expression in chondrocyte. In our experimental conditions, chondrocytes did not express COL1, COL10 or ALP, even after 10 days of co-culture with osteoblasts. Conclusions: In co-culture, SC subchondral osteoblasts decrease SOX9, COL2, PTHrP and PTH-R gene expression by chondrocytes but increase that of OSF-1. These findings suggest that SC osteoblasts could initiate chondrocyte phenotype shift towards hypertrophic differentiation and subsequently further matrix mineralization. (c) 2005 OsteoArthritis Research Society International. Published by Elsevier Ltd. All rights reserved. [less ▲]

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See detailNew serum biochemical markers (Coll 2-1 and Coll 2-1 NO2) for studying oxidative-related type II collagen network degradation in patients with osteoarthritis and rheumatoid arthritis
Deberg, Michelle ULg; Labasse, Alain ULg; Christgau, S. et al

in Osteoarthritis and Cartilage (2005), 13(3), 258-265

Objective: Protein nitration is a prominent feature of inflammatory processes in the joint. We have developed immunoassays specific for a peptide of the alpha-helical region of type II collagen (108 ... [more ▼]

Objective: Protein nitration is a prominent feature of inflammatory processes in the joint. We have developed immunoassays specific for a peptide of the alpha-helical region of type II collagen (108)HRGYPGLDG(116) (Coll 2-1) and its nitrated form (108)HRGY(NO2)PGLDG(116) (Coll 2-1 NO2) in biological fluids. Design: Coll 2-1 and Coll 2-1 NO2 peptides were injected into rabbits. Two antisera (D3 and D37) were selected for their specificity and affinity and used to develop specific immunoassays. Coll 2-1 and Coll 2-1 NO2 were measured in sera of 242 healthy subjects (N), 67 patients with primary knee osteoarthritis (OA) and 19 patients with rheumatoid arthritis (RA). Results: In healthy subjects, Coll 2-1 and Coll 2-1 NO2 concentrations were 125.13 +/- 3.71 nM and 0.16 +/- 0.08 nM, respectively. In OA and RA, Coll 2-1 and Coll 2-1 NO2 serum levels were found to be significantly increased compared to controls of the same range of age (Coll 2-1: OA: 200.80 +/- 8.98 nM, RA: 172.30 +/- 19.05 nM, normal: 126.60 +/- 6.70 nM and Coll 2-1 NO2: OA: 0.26 +/- 0.02, RA: 0.38 +/- 0.05, normal: 0.12 +/- 0.01 nM). Coll 2-1 NO2 levels were significantly more elevated in RA than in OA patients (P < 0.05). As a consequence, the ratio Coll 2-1 NO2/Coll 2-1 was 1.6 times higher in RA than in OA subjects. No relationship was found between the radiological OA severity and the levels of Coll 2-1 and Coll 2-1 NO2 in serum. Coll 2-1 NO2, but not Coll 2-1, was correlated with C-reactive protein in the sera of OA and RA patients. Conclusions: The determination of both Coll 2-1 and Coll 2-1 NO2 in serum of arthritic patients seems to be a promising useful tool for the detection of oxidative-related cartilage degradation episode. Further, these markers could be helpful for monitoring the effects of anti-inflammatory or antioxidant drugs on cartilage degradation. (c) 2004 OsteoArthritis Research Society International. Published by Elsevier Ltd. All rights reserved. [less ▲]

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See detailSubchondral Bone Osteoblasts Induce Phenotypic Changes in Human Osteoarthritic Chondrocytes
Sanchez, Christelle ULg; Deberg, Michelle ULg; Piccardi, Nathalie et al

in Osteoporosis International (2005), 16(Suppl.3), 55-56

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See detailAvocado/soybean unsaponifiables prevent osteoarthritic subchondral osteoblasts-induced cartilage degradation
Sanchez, Christelle ULg; Deberg, Michelle ULg; Piccardi, Nathalie et al

in Osteoporosis International (2005), 16(Suppl.3), 56

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