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See detailDetection of specific nitrated markers
REGINSTER, Jean-Yves ULg; DEBERG, Michelle ULg; Henrotin, Yves ULg et al

Patent (2008)

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See detailPhenotypic Characterization of Osteoblasts from the Sclerotic Zones of Osteoarthritic Subchondral Bone
Sanchez, Christelle ULg; Deberg, Michelle ULg; Bellahcene, Akeila ULg et al

in Arthritis and Rheumatism (2008), 58(2), 442-55

OBJECTIVE: To determine the phenotype of osteoblasts from the sclerotic zones of human osteoarthritic (OA) subchondral bone. METHODS: Human osteoblasts were isolated from sclerotic or nonsclerotic areas ... [more ▼]

OBJECTIVE: To determine the phenotype of osteoblasts from the sclerotic zones of human osteoarthritic (OA) subchondral bone. METHODS: Human osteoblasts were isolated from sclerotic or nonsclerotic areas of subchondral bone and cultured for 14 days in monolayer. The expression of 14 genes was investigated by real-time reverse transcription-polymerase chain reaction. The activities of alkaline phosphatase (AP) and transglutaminases (TGases) were quantified by enzymatic assays. C-terminal type I procollagen propeptide (CPI), interleukin-1beta (IL-1beta), IL-6, IL-8, transforming growth factor beta1 (TGFbeta1), osteocalcin (OC), and osteopontin (OPN) were assayed in the culture medium by immunoassay. RESULTS: Gene expression levels of matrix metalloproteinase 13, COL1A1 and COL1A2, OPN, tissue-nonspecific AP, OC, vascular endothelial growth factor, ANKH, TGase 2, factor XIIIA, and dentin matrix protein 1 were significantly up-regulated in sclerotic osteoblasts compared with nonsclerotic osteoblasts. In contrast, parathyroid hormone receptor gene expression was depressed in sclerotic osteoblasts, but bone sialoprotein levels were unchanged. The activities of AP and TGases were increased in sclerotic osteoblasts, while matrix mineralization, revealed by alizarin red staining, was decreased. In parallel, protein synthesis of CPI, OC, OPN, IL-6, IL-8, and TGFbeta1 was significantly higher in sclerotic osteoblasts than in nonsclerotic osteoblasts, while IL-1beta production was similar in both groups. CONCLUSION: These findings contribute to a better understanding of the mechanisms involved in subchondral bone sclerosis and identify osteoblasts with an altered phenotype as a potential target for future OA therapies. [less ▲]

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See detailOne-Year Follow-up of Coll2-1, Coll2-1no2 and Myeloperoxydase Serum Levels in Osteoarthritis Patients after Hip or Knee Replacement
Deberg, Michelle ULg; Dubuc, Jean Emile; Labasse, Alain ULg et al

in Annals of the Rheumatic Diseases (2008), 67(2), 168-74

OBJECTIVES: To determine Coll2-1, Coll2-1NO(2) and myeloperoxydase (MPO) levels in serum of patients with knee or hip osteoarthritis (OA) before the surgery, 3 months and 1 year after knee or hip ... [more ▼]

OBJECTIVES: To determine Coll2-1, Coll2-1NO(2) and myeloperoxydase (MPO) levels in serum of patients with knee or hip osteoarthritis (OA) before the surgery, 3 months and 1 year after knee or hip replacement. METHODS: Coll2-1, Coll2-1NO(2) and MPO were measured in 103 patients with isolated symptomatic knee or hip OA candidates for joint replacement. Sera were taken the day before surgery, 3 months and 1 year after hip or knee replacement. Coll2-1 and Coll2-1NO(2) immunohistochemistry was performed on biopsies removed from cartilage lesions. RESULTS: Immunostainings revealed the extensive presence of Coll2-1 and Coll2-1NO(2) in the superficial layer of fibrillated cartilage and around some chondrocytes clusters. Three months after joint replacement, Coll2-1 and MPO serum levels were decreased and even reached the reference value for Coll2-1. By contrast, Coll2-1NO(2) levels remained elevated. At 1-year follow-up, Coll2-1 levels remained at the reference value, MPO levels were similar to those measured at 3 months, and Coll2-1NO(2) levels were unchanged and comparable to the pre-surgery values. However, in patients with pre-surgery values above the median (more than 0.42 nM), Coll2-1NO(2) levels significantly and progressively decreased post-operatively, but tended towards an increase in patients with pre-surgery Coll2-1NO(2) values below the median. CONCLUSIONS: The normalisation of Coll2-1 levels 3 months after surgery indicates that Coll2-1 is a disease-specific marker that is sensitive to the structural changes occurring in a single joint. Furthermore, the immunohistochemical findings are consistent with the concept that the major source of serum Coll2-1 is the damaged articular cartilage. Finally, serum MPO levels decreased after joint replacement indicating that neutrophil activation occurs in OA joints, even in the late stage of the disease. [less ▲]

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See detailThe chemical biomarkers C2C, Coll2-1, and Coll2-1NO(2) provide complementary information on type II collagen catabolism in healthy and osteoarthritic mice
Ameye, L. G.; Deberg, Michelle ULg; Oliveira, M. et al

in Arthritis and Rheumatism (2007), 56(10), 3336-3346

Objective. Compared with wild-type (WT) mice, biglycan/fibromodulin double-deficient mice develop severe knee osteoarthritis. We undertook this study to compare type 11 collagen catabolism in the 2 ... [more ▼]

Objective. Compared with wild-type (WT) mice, biglycan/fibromodulin double-deficient mice develop severe knee osteoarthritis. We undertook this study to compare type 11 collagen catabolism in the 2 genotypes and to compare the usefulness of 3 biomarkers of collagen degradation (C2C [also known as Col23/4C(long mono)] as well as the peptide Coll2-1 and its nitrated form, Coll2-1NO(2)) for evaluating collagen catabolism in vivo. Methods. In 15 WT mice and 15 biglycan/ fibromodulin double-deficient mice, we determined serum levels of C2C at ages 66 and 141 days, and we determined serum levels of Coll2-1 and Coll2-1NO(2) at ages 49, 81, 95, and 141 days. Expression of the biomarkers in knee sections was examined using immunohistochemistry. Results. The mean concentrations of C2C and Coll2-1 were higher in biglycan/fibromodulin double-deficient mice at all time points. For C2C and Coll2-1, the ratio of the serum concentration in biglycan/ fibromodulin double-deficient mice to that in WT mice (the double-deficient:WT ratio) was constant over time and was similar to 1.63 and similar to 1.15, respectively. In contrast, the double-deficient:WT ratio for Coll2-1NO(2) varied and, depending on age, was >1 or <1. No significant correlation was found between the expression of the different biomarkers, except for a weak, negative correlation between Coll2-1NO(2) and C2C. In both genotypes, antibodies to each biomarker labeled some fibroblasts in the tendons and menisci as well as chondrocytes above the tidemark in articular cartilage. Growth plates were unstained. For each biomarker, extracellular staining was limited to fibrocartilage areas in the tendons and menisci in all mice and was limited to some focal lesions of the cartilage in biglyean/fibromodulin double-deficient mice. Conclusion. The different double-deficient:WT ratios observed with C2C, Coll2-1, and Coll2-1NO(2) in the absence of any correlation between the expression of the 3 biomarkers indicate that these biomarkers give complementary, rather than redundant, information about in vivo type 11 collagen catabolism. [less ▲]

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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 detailInterleukin-6 mediates subchondral osteoblasts-induced cartilage degradation
Sanchez, Christelle ULg; Kaut, Elizabeth; DEBERG, Michelle ULg et al

Conference (2006)

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