Cyclooxygenase inhibitors augment the production of pro‐matrix metalloproteinase 9 (progelatinase B) in rabbit articular chondrocytes

Ito, Akira; Nose, Takashi; Takahashi, Soichiro; Mori, Yo

doi:10.1016/0014-5793(95)00085-n

Cited by 52 publications

(34 citation statements)

References 29 publications

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“…MMP-9 has been implicated in cellular migration and invasion in patients with such conditions as inflammation, tumor invasion, and metastasis. In addition, recent studies of this proteinase in the skeleton suggest that MMP-9 could exist in matrix vesicles (27), digest cartilage proteoglycans (28,29), and play important roles in chondrocyte apoptosis (30) and osteoclastic bone resorption (31)(32)(33). MMP-9 can also be produced by activated osteoclasts (34).…”

Section: Discussionmentioning

confidence: 99%

Significant increases in serum and plasma concentrations of matrix metalloproteinases 3 and 9 in patients with rapidly destructive osteoarthritis of the hip

Masuhara

Nakai

Yamaguchi

et al. 2002

Arthritis & Rheumatism

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Objective. Rapidly destructive osteoarthritis (OA) of the hip is an uncommon subset of OA that affects mainly elderly women. Previous studies indicate that elevated levels of matrix metalloproteinases (MMPs) are produced within the tissue of patients with the condition. In the present study, we sought to determine whether serum and plasma levels of MMPs and tissue inhibitors of metalloproteinases (TIMPs) are also elevated.Methods. Blood samples were obtained from 16 patients with rapidly destructive hip OA and from 20 patients with OA before total hip arthroplasty was performed. Synovial specimens were obtained during surgery. Synovial fibroblasts that had migrated sufficiently from explants were subcultured in vitro for 72 hours after confluency, and harvested supernatants were collected. Blood, tissue samples, and fibroblasts were assayed for MMPs 1, 2, 3, and 9, and TIMPs 1 and 2 by sandwich enzyme immunoassay.Results. In blood samples, the levels of MMP-3 and MMP-9 in the group with rapidly destructive hip OA were significantly higher than the normal range and were also significantly higher than those in the OA group. In tissue samples, the levels of MMP-1, MMP-3, MMP-9, and TIMP-1 in the group with rapidly destructive hip OA were significantly higher than those in the OA group. Conclusion.The results of this study show that serum and plasma levels of MMP-3 and MMP-9 are significantly increased in patients with rapidly destructive hip OA. Significantly large amounts of these MMPs produced in synovial tissues within the hip joint could contribute in part to elevation of blood levels. Detection of increased levels of MMP-3 and MMP-9 in patients with painful, disabling hip OA may be of diagnostic value for rapidly destructive hip OA.

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Section: Discussionmentioning

confidence: 99%

Significant increases in serum and plasma concentrations of matrix metalloproteinases 3 and 9 in patients with rapidly destructive osteoarthritis of the hip

Masuhara

Nakai

Yamaguchi

et al. 2002

Arthritis & Rheumatism

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“…and other matrix molecules (22,34,54,55). Normal human and rabbit articular cartilage and cultured chondrocytes express little or undctectable levels of MMP-9 under basal conditions, but the gene is induced by treatment with inflammatory cytokines such as interleukin-la (IL-la) (32,35,43,51,57,64). In osteoarthritis, the expression of MMP-9 mRNA and protein is increased in articular cartilage and isolated chondrocytes (24.51.71).…”

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confidence: 99%

Biomechanical regulation of matrix metalloproteinase‐9 in cultured chondrocytes

Jin

Sah

et al. 2000

Journal Orthopaedic Research

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Summary:Abnormal mechanical loading of joints may induce degeneration of articular cartilage. Shear stress is one mode of mechanical loading that may regulate chondrocyte metabolism. We investigated the mechanism by which shear stress induccs the gene encoding matrix metalloproteinase-9, a mediator of the progressive degradation of articular cartilage in ostcoarthritis. In vifro experiments using passaged rabbit chondrocytes in monolayer culture subjected to a shear stress of 16 dynicn? (1.6 Pa) in a flow channel showed increased expression of the matrix mctalloproteinase-9 gcne. The induction of matrix metalloproteinase-9 appeared to depend on a region in the 5' promoter of the gcnc that contains a 12-0-tetradecanoylphorbol 13-acetateresponsive element. Transfection experiments using a construct containing a luciferase reporter driven by a 12-0-tetradecanoylphorbol 13-acetate-responsive clement indicated that shear stress activated a 12-0-tetradecanoylphorbol 13-acetate-responsive element-mediated transcription in chondrocytes. Similar experiments showed that shear stress induced a matrix metalloproteinase-9 promoter construct (matrix metalloproteinase-9-luciferase). Shear stress activated c-Jun NH1-terniinal kinasc, cxtraccllular signal-regulated kinase. and p3X. 'Transfection of matrix inetalloproteinase-9-lucifcrase together with thc dominant negative mutant of c-.Tun NH,-terminal kinase. hut not with that of cxtraccllular signal-regulated kinase or p38. attenuated the shearinduced matrix metalloproteinasc-9 promoter activity. In addition. transfection of constructs encoding dominant negative mutants o C Ras. Rac. and Cdc42 attenuated the induction of c-Jun transcriptional activity by shear stress. Thus. shear stimulation of chondrocytes stimulates Kas, Rac, and Cdc42, which subsequcntly activate c-Jun NH?-terminal kinasc to induce a 12-0-tetradecanoylphorhol 13-acetate-responsive clementmcdiatcd expression of matrix metalloproteinase-9. ~The metabolic activity of chondrocytes is regulated by mechanical factors (28). Such biomechanical regulation map affect the balance between anabolic and catabolic processes in articular cartilage. In osteoarthritis, a metabolic imbalance results in lie1 matrix degradation and the degeneration of articular cartilage (59). Many in vivo and in vitro studies have examined the effect of biomechanical stimuli on the synthesis of matrix proteins by chondrocytes (28). However. relatively few studies have analyzed the extracellular or cellular mechanisms by which mechanical stimuli may alter cartilage matrix degradationincluding the modulation of matrix protcinascs and their inhibitors (68)-and thereby contribute to the initiation or progression of osteoarthritis.In osteoarthritis, the synthesis of matrix metalloprotcinascs (MMPs) by chondrocytes is incrcased (20) and the balancc betwcen proteases and protease

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“…These results are in agreement with those of others. [24][25][26] Studies by Ito et al have reported that diclofenac has a positive effect on the inhibition of cartilage metabolism. 26) B. platyphylla inhibited MMP-3 and MMP-13 mRNA and protein expression, as well as their activity, in articular cartilage explants (Figs.…”

Section: Discussionmentioning

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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Cyclooxygenase inhibitors augment the production of pro‐matrix metalloproteinase 9 (progelatinase B) in rabbit articular chondrocytes

Cited by 52 publications

References 29 publications

Significant increases in serum and plasma concentrations of matrix metalloproteinases 3 and 9 in patients with rapidly destructive osteoarthritis of the hip

Significant increases in serum and plasma concentrations of matrix metalloproteinases 3 and 9 in patients with rapidly destructive osteoarthritis of the hip

Biomechanical regulation of matrix metalloproteinase‐9 in cultured chondrocytes

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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