Measurement of matrilin-3 levels in human serum and synovial fluid using a competitive enzyme-linked immunosorbent assay

Vincourt, J.-B.; Gillet, Pierre; Rat, Anne‐Christine; Guillemin, François; Netter, Patrick; Mainard, Didier; Magdalou, Jacques

doi:10.1016/j.joca.2012.03.017

Cited by 6 publications

(3 citation statements)

References 8 publications

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“…13,[58][59][60] In addition, distribution pattern I provides clear indications that in early or moderate OA, a marked degradation of the proteins analyzed took place in the upper zones of human knee joint cartilage. In this way, our study supports the approach to use molecules such as COMP, 61 matrilin-3, 62 collagen IX, 48 and collagen II 63 that are degraded in OA and whose fragments can be assayed in body fluids such as synovial fluid, blood, or urine, as biomarkers of cartilage metabolism. 12 In conclusion, the loss of perifibrillar adapter proteins in the upper zones of articular cartilage seems to be a critical event in early OA.…”

Section: Discussionsupporting

confidence: 71%

Extracellular Distribution of Collagen II and Perifibrillar Adapter Proteins in Healthy and Osteoarthritic Human Knee Joint Cartilage

Firner

Zaucke

Michael

et al. 2017

J Histochem Cytochem.

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Perifibrillar adapter proteins, interconnecting collagen fibrils, and linking the collagen network with the aggrecan matrix seem to play a crucial role in the pathogenesis of osteoarthritis (OA). Therefore, we examined immunohistochemically the extracellular distribution of collagen II and the main perifibrillar adapter proteins-collagen IX, decorin, cartilage oligomeric matrix protein (COMP), and matrilin-3-in human samples of healthy (n=4) and OA (n=42) knee joint cartilage. Histopathology assessment was performed using an OA score. Staining patterns were evaluated in relation to the disease stage. The perifibrillar adapter proteins were uniformly distributed in the upper zones of healthy cartilage. In moderate OA (n=8; score 14.3 ± 4.7), all proteins analyzed were locally absent in the fibrillated area or the superficial and upper mid zone. In advanced OA (n=20; score 18.9 ± 5.3), they were uniformly distributed in these zones and accumulated pericellularly. Perifibrillar adapter proteins are important for the stabilization of the collagen network in the upper zones of healthy cartilage. Their degradation might be a critical event in early OA. In advanced OA, there are indications for an increased synthesis in an attempt to regenerate the lost tissue and to protect the remaining cartilage from further destruction.

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Section: Discussionsupporting

confidence: 71%

Extracellular Distribution of Collagen II and Perifibrillar Adapter Proteins in Healthy and Osteoarthritic Human Knee Joint Cartilage

Firner

Zaucke

Michael

et al. 2017

J Histochem Cytochem.

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“…Matrilin-3 (MATN3) is a matrix protein that is highly upregulated during OA [76, 77]. Although the protein is a part of healthy cartilage matrix, the soluble form of MATN3 is upregulated and released to synovial fluid in OA [78].…”

Section: The Effects Of Changes In Extracellular Matrix On Articulmentioning

confidence: 99%

The Role of Changes in Extracellular Matrix of Cartilage in the Presence of Inflammation on the Pathology of Osteoarthritis

Maldonado

Nam

2013

BioMed Research International

396

297

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Osteoarthritis (OA) is a degenerative disease that affects various tissues surrounding joints such as articular cartilage, subchondral bone, synovial membrane, and ligaments. No therapy is currently available to completely prevent the initiation or progression of the disease partly due to poor understanding of the mechanisms of the disease pathology. Cartilage is the main tissue afflicted by OA, and chondrocytes, the sole cellular component in the tissue, actively participate in the degeneration process. Multiple factors affect the development and progression of OA including inflammation that is sustained during the progression of the disease and alteration in biomechanical conditions due to wear and tear or trauma in cartilage. During the progression of OA, extracellular matrix (ECM) of cartilage is actively remodeled by chondrocytes under inflammatory conditions. This alteration of ECM, in turn, changes the biomechanical environment of chondrocytes, which further drives the progression of the disease in the presence of inflammation. The changes in ECM composition and structure also prevent participation of mesenchymal stem cells in the repair process by inhibiting their chondrogenic differentiation. This review focuses on how inflammation-induced ECM remodeling disturbs cellular activities to prevent self-regeneration of cartilage in the pathology of OA.

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“…Interestingly, matrilin-3 was found to be upregulated in OA patient cartilage and synovial fluid and increased matrilin-3 cartilage deposition was associated with decease severity (66,67). Furthermore, matrilin-3 is detectable in serum and the serum levels increase in accordance with matrilin-3 cartilage release into the synovial fluid (67). Matrilin-3 binds to COMP and collagens (22,68).…”

Section: Discussionmentioning

confidence: 99%

COMP does not directly modify the expression of genes involved in cartilage homeostasis in contrast to several other cartilage matrix proteins

Ruthard

Kamper

Renno

et al. 2014

Connective Tissue Research

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Measurement of matrilin-3 levels in human serum and synovial fluid using a competitive enzyme-linked immunosorbent assay

Cited by 6 publications

References 8 publications

Extracellular Distribution of Collagen II and Perifibrillar Adapter Proteins in Healthy and Osteoarthritic Human Knee Joint Cartilage

Extracellular Distribution of Collagen II and Perifibrillar Adapter Proteins in Healthy and Osteoarthritic Human Knee Joint Cartilage

The Role of Changes in Extracellular Matrix of Cartilage in the Presence of Inflammation on the Pathology of Osteoarthritis

COMP does not directly modify the expression of genes involved in cartilage homeostasis in contrast to several other cartilage matrix proteins

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