Involvement of MMP-1 and MMP-3 in collagen degradation induced by IL-1 in rabbit cartilage explant culture

Saito, Shigeki; Katoh, Miyuki; Masumoto, Mari; Matsumoto, S.; Masuho, Yasuhiko

doi:10.1016/s0024-3205(98)00181-7

Cited by 31 publications

(27 citation statements)

References 16 publications

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“…1B). Because CTS-mediated abrogation of IL-1-induced expression of iNOS mRNA results in decreased synthesis of iNOS (29), this inhibition in NO synthesis can be attributed to suppression of iNOS synthesis. Under these conditions chondrocytes subjected to CTS exhibited minimal cell deformation compared with unstressed control cells and negligible cell detachment (Ͻ0.1%), as assessed by counting nonadherent cells in the wells, or cell death, as assessed by DNA fragmentation (data not shown).…”

Section: Cts Suppresses Il-1␤-dependent Induction Of Inosmentioning

confidence: 99%

Cyclic Tensile Strain Acts as an Antagonist of IL-1β Actions in Chondrocytes

Buckley

Evans

et al. 2000

The Journal of Immunology

103

125

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Inflammatory cytokines play a major role in cartilage destruction in diseases such as osteoarthritis and rheumatoid arthritis. Because physical therapies such as continuous passive motion yield beneficial effects on inflamed joints, we examined the intracellular mechanisms of mechanical strain-mediated actions in chondrocytes. By simulating the effects of continuous passive motion with cyclic tensile strain (CTS) on chondrocytes in vitro, we show that CTS is a potent antagonist of IL-1β actions and acts as both an anti-inflammatory and a reparative signal. Low magnitude CTS suppresses IL-1β-induced mRNA expression of multiple proteins involved in catabolic responses, such as inducible NO synthase, cyclo-oxygenase II, and collagenase. CTS also counteracts cartilage degradation by augmenting mRNA expression for tissue inhibitor of metalloproteases and collagen type II that are inhibited by IL-1β. Additionally, CTS augments the reparative process via hyperinduction of aggrecan mRNA expression and abrogation of IL-1β-induced suppression of proteoglycan synthesis. Nonetheless, the presence of an inflammatory signal is a prerequisite for the observed CTS actions, as exposure of chondrocytes to CTS alone has little effect on these parameters. Functional analysis suggests that CTS-mediated anti-inflammatory actions are not mediated by IL-1R down-regulation. Moreover, as an effective antagonist of IL-1β, the actions of CTS may involve disruption/regulation of signal transduction cascade of IL-1β upstream of mRNA transcription. These observations are the first to show that CTS directly acts as an anti-inflammatory signal on chondrocytes and provide a molecular basis for its actions.

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Section: Cts Suppresses Il-1␤-dependent Induction Of Inosmentioning

confidence: 99%

Cyclic Tensile Strain Acts as an Antagonist of IL-1β Actions in Chondrocytes

Buckley

Evans

et al. 2000

The Journal of Immunology

103

125

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“…It is present in normal tissues in inactive forms as a proenzyme or as complexes with tissue inhibitors of metalloproteinases (TIMPs) [18]. How the MMP activity is regulated in normal tendon or what signal may trigger injured tendon cells to express MMPs in a tissue- [29,[31][32][33][34]36,40].…”

mentioning

confidence: 99%

“…However, ample precedents for this pathologic mechanism exist in other tissues such as cartilage [29,34,39,40,46].…”

mentioning

confidence: 99%

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IL‐1β induces COX2, MMP‐1, ‐3 and ‐13, ADAMTS‐4, IL‐1β and IL‐6 in human tendon cells

Tsuzaki

Guyton

Garrett

et al. 2003

Journal Orthopaedic Research

341

287

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Overuse injuries and trauma in tendon often involve acute or chronic pain and eventual matrix destruction. Anti-inflammatory drugs have been used as a treatment, however, the cellular and molecular mechanisms of the destructive processes in tendon are not clearly understood. It is thought that an inflammatory event may be involved as an initiating factor. Mediators of the inflammatory response include cytokines released from macrophages and monocytes. Interleukin-1 beta (IL-1 p) is a candidate proinflammatory cytokine that is active in connective tissues such as bone and cartilage. We hypothesized that tendon cells would express receptors and respond to IL-1 b in an initial "molecular inflammation" cascade, that is, connective tissue cell expression of cytokines that induce matrix destructive enzymes. This cascade results in expression of matrix metalloproteinases (MMPs) and aggrecanases that may lead to matrix destruction. Normal human tendon cells from six patients were isolated, grown to quiescence and treated with human recombinant IL-lP in serum-free medium for 16 h. Total RNA was isolated and mRNA expression assessed by semiquantitative RT-PCR. IL-lP (1 nM) induced mRNAs for cyclooxygenase 2 (COX2), MMP-I, -3, -13 and aggrecanase-1 as well as IL-1 j3 and IL-6, whereas mRNAs for COX1 and MMP-2 were expressed constitutively. The IL-lj3-treated tendon cells released prostaglandin E2 (PGE2) in the medium, suggesting that the inducible COX2 catalyzed this synthesis. Induction of PGE2 was detectable at 10 pM IL-1 j3. IL-10 also stimulated MMP-1 and -3 protein secretion. Induction of MMP-1 and -3 was detectable at 10 pM IL-1 fi. Post-injury or after some other inciting events, exogenous IL-1 P released upon bleeding or as leakage of local capillaries may drive a proinflammatory response at the connective tissue cell level. The resulting induction of COX2, MMP-1 and -3 may underscore a potential for nonlymphocyte-mediated cytokine production of MMPs that causes matrix destruction and a loss of tendon biomechanical properties. Endogenous IL-1 b might contribute to the process through a positive feedback loop by stimulating expression and accumulation of MMPs in the tendon matrix.

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“…15,16) MMP-13 is expressed by normal and osteoarthritic chondrocytes, and has been localized to both rheumatoid and osteoarthritic cartilage.…”

Section: )mentioning

confidence: 99%

Effect of Betula platyphylla var. japonica on Proteoglycan Release, Type II Collagen Degradation, and Matrix Metalloproteinase Expression in Rabbit Articular Cartilage Explants

Cho¹,

Huh

Kim³

et al. 2006

Biological & Pharmaceutical Bulletin

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Osteoarthritis (OA) is a degenerative joint disease characterized by the progressive loss of articular cartilage, subchondral bond remodeling, spur formation, synovial inflammation, and in particular, the degradation of proteoglycan and collagen. The integrity of these macromolecules is vital to cartilage and joint function. 1)Proteoglycan is a component of the articular cartilage extracellular matrix, providing it with many of its characteristic physicochemical properties.2) The carbohydrate component of aggrecan, which constitutes at least 90% of its molecular mass, consists of many long keratin sulfate, chondroitin sulfate, and glycosaminoglycan (GAG) chains covalently linked to a core protein.3) The contribution of these GAG polymers to cartilage function can be divided into two categories: firstly, maintenance of hydration, a property dependent on their polyanionicity, which engenders in cartilage the ability to withstand compression, and secondly, interactions with other macromolecules that depend on the specific distribution of the negative charges of GAG and its carbohydrate backbone conformation. 4,5) Thus, the importance of these proteoglycans is clear. However, neither their specific role nor the mechanisms regulating their synthesis are fully understood.Collagen is another component of articular cartilage, and it is present primarily as type II collagen.6) It plays a role in maintaining the integrity of the cartilage matrix and allows proteoglycan to be held in the matrix. 7) Healthy cartilage maintains a dynamic equilibrium between processes that produce and processes that degrade matrix components. It is thought that this equilibrium is disturbed in OA, and that matrix-component degradative processes dominate, leading to an increased loss of the matrix. According to in vitro studies, collagen is much less readily released than proteoglycan, but collagen degradation results in the irreversible loss of structural integrity.8) There is circumstantial in vitro and in vivo evidence indicating a significant role for matrix metalloproteinases (MMPs) in cartilage destruction in arthritis. 9)MMPs can be classified into four subgroups: collagenases (MMP-1, -8, -13), stromyelins (MMP-3, -10, -11), gelatinases (MMP-2, -9), and membrane-type MMPs.10) MMPs are synthesized in response to cytokines such as interleukin-1 (IL-1) and tumor necrosis factor-a, which is thought to be involved in the pathogenesis of arthritis. [10][11][12][13] MMPs are released as inactive proenzyme forms and are then activated by limited proteolysis of the propeptide domain by plasmin, kallikrein, or trypsin.10,14) MMP-3 is capable of cleaving aggrecan core protein, as well as type II collagen (in the aminoterminal telopeptide) in vitro, but it is not clear if it is involved in the degradation of these proteins in cartilage. 15,16) MMP-13 is expressed by normal and osteoarthritic chondrocytes, and has been localized to both rheumatoid and osteoarthritic cartilage.17) MMP-13 is the most efficient collagenase against type II collagen, sug...

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Involvement of MMP-1 and MMP-3 in collagen degradation induced by IL-1 in rabbit cartilage explant culture

Cited by 31 publications

References 16 publications

Cyclic Tensile Strain Acts as an Antagonist of IL-1β Actions in Chondrocytes

Cyclic Tensile Strain Acts as an Antagonist of IL-1β Actions in Chondrocytes

IL‐1β induces COX2, MMP‐1, ‐3 and ‐13, ADAMTS‐4, IL‐1β and IL‐6 in human tendon cells

Effect of Betula platyphylla var. japonica on Proteoglycan Release, Type II Collagen Degradation, and Matrix Metalloproteinase Expression in Rabbit Articular Cartilage Explants

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