Clinical Correlations of Osteoarthritis Associated with a Single‐Base Mutation (Arginine519 to Cysteine) in Type II Procollagen Gene

Pun, Yvonne L.; Moskowitz, Roland W.; Lie, Sutek; Sundstrom, Walter R.; Block, Sidney R.; McEwen, Currier; Williams, H. James; Bleasel, Jane; Holderbaum, Daniel; Haqqi, Tariq M.

doi:10.1002/art.1780370216

Cited by 52 publications

(38 citation statements)

References 21 publications

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“…Osteoarthritis (OA), the most prevalent disease of the articulating joints affecting millions of people worldwide is a chronic degenerative joint disease that is characterized by deterioration in the integrity of cartilage and is coupled with pain, tenderness, disability and inflammation without systemic effects (1). Although multiple factors are included in OA etiology, chondrocytes are crucial to tissue function and dominate the degenerative process of cartilage if the genes are expressed inappropriately when compared with adjacent tissues.…”

Section: Introductionmentioning

confidence: 99%

MiR-15a-5p regulates viability and matrix degradation of human osteoarthritis chondrocytes via targeting VEGFA

Chen

Tian

2016

BST

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Section: Introductionmentioning

confidence: 99%

MiR-15a-5p regulates viability and matrix degradation of human osteoarthritis chondrocytes via targeting VEGFA

Chen

Tian

2016

BST

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“…Upregulated collagenase activity is also seen in the development of OA in ageing and unstable joints [38]. Additional implication of collagen I1 in the ethiopathogenesis of OA is highlighted when the slow turnover of collagen in adult cartilage is considered [32], and in light of animal models of OA where tissue defects are induced by collagen 11 mutations [33].…”

Section: Introductionmentioning

confidence: 99%

Cyclic compression of cartilage/bone explants in vitro leads to physical weakening, mechanical breakdown of collagen and release of matrix fragments

Thibault¹,

Poole²,

Buschmann³

2002

Journal Orthopaedic Research

122

107

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Mechanical loading of articular cartilage can produce catabolic and anabolic changes in tissue metabolism. Most previous studies in this area have focussed on aggrecan. Little information concerning load-induced collagen modifications has been obtained. We have therefore conducted studies where mechanical loads are applied in vitro to full thickness cartilage explants retaining a thin layer of bone, in order to investigate mechanically induced collagen breakdown and consequent turnover, in addition to aggrecan changes and mechanical property alterations. Tissue explant disks were subjected to unconfined compression and either immediately frozen or kept in static culture for 10 days. Mechanical tests of the disks immediately prior to and just after the cyclic loading period were also performed. They showed a weakening of the collagen network and an increased hydraulic permeability due to the cyclic loading. Load-induced alterations of the extracellular matrix was then clearly evidenced by an increase in denatured collagen in the disks frozen immediately after loading compared to unloaded controls. Loaded disks maintained in culture for 10 additional days following cyclic loading no longer expressed this increase in denatured collagen suggesting that mechanically denatured collagen I1 had undergone a removal process which could represent turnover or repair, or the beginning of progressive degradation. Indeed matrix fragments of collagen I1 and glycosaminoglycans were found to be released to post-loading culture medium in increased quantities compared to unloaded controls. Our data further demonstrates the ability of mechanical load of articular cartilage to modulate turnover and metabolism of collagen and proteoglycan in a complex and multifactorial manner that may be of particular significance in the pathogenesis of osteoarthritis and in the development of pharmacological agents to modulate its progression.

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“…Similarly in the 1990s, particular families were discovered to have missense mutation (R519C) causing the production of abnormal type II collagen pro-alphachains. These alpha chains formed protein dimers leading to mild chondrodysplasia followed by a unique form of familial OA (Byers, 2001;Eyre et al, 1991;Pun et al, 1994;Bleasel et al, 1998).…”

Section: Collagen IImentioning

confidence: 99%

Cartilage Extracellular Matrix Integrity and OA

Jayasuriya¹,

Chen²

2012

Principles of Osteoarthritis- Its Definition, Character, Derivation and Modality-Related Recognition

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Clinical Correlations of Osteoarthritis Associated with a Single‐Base Mutation (Arginine⁵¹⁹ to Cysteine) in Type II Procollagen Gene

Cited by 52 publications

References 21 publications

MiR-15a-5p regulates viability and matrix degradation of human osteoarthritis chondrocytes <i>via</i> targeting VEGFA

MiR-15a-5p regulates viability and matrix degradation of human osteoarthritis chondrocytes <i>via</i> targeting VEGFA

Cyclic compression of cartilage/bone explants in vitro leads to physical weakening, mechanical breakdown of collagen and release of matrix fragments

Cartilage Extracellular Matrix Integrity and OA

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