Purification and characterization of collagenase activator protein synthesized by articular cartilage

Treadwell, Benjamin V.; Neidel, J.; Pavia, Michele; Towle, Christine A.; Trice, Michael E.; Mankin, Henry J.

doi:10.1016/0003-9861(86)90381-4

Cited by 32 publications

(18 citation statements)

References 14 publications

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“…Enzymes measured with the collagenaseassay include 92kDa collagenase. The caseinase-assay has been shown to detect stromelysin, among other proteases [3]. Whether proteases contained in RA-SF significantly participate in the process of bone-resorption, has yet to be determined.…”

Section: Discussionmentioning

confidence: 99%

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Association between degree of bone-erosion and synovial fluid-levels of tumor necrosis factor α in the knee-joints of patients with rheumatoid arthritis

1995

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Section: Discussionmentioning

confidence: 99%

“…IL-1 and TNFc~ have been shown to suppress cartilage matrix synthesis [1,2], to activate chondrocytes to secrete proteases like 92kDa collagenase and stromelysin [3,4], to suppress production of protease-inhibitors by chondrocytes and synovial cells [4], to stimulate prostaglandin production by synovial…”

Section: Introductionmentioning

confidence: 99%

Association between degree of bone-erosion and synovial fluid-levels of tumor necrosis factor α in the knee-joints of patients with rheumatoid arthritis

1995

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“…The mechanism in which tryptase leads to an active form of collagenase is explored in this report. The activation of procollagenase occurs after cellular release and recent evidence suggests that full activation likely involves an intermediary "proactivator" (7)(8)(9)(10)(11)(12)(13). It has been proposed that this proactivator has in itself a broad spectra of metal-dependent matrix degrading activities and represents a member of a family of metalloproteinases, termed MMP-3 or stromelysin (4)(5)(6)35).…”

Section: Discussionmentioning

confidence: 99%

Synovial procollagenase activation by human mast cell tryptase dependence upon matrix metalloproteinase 3 activation.

Gruber¹,

Marchese²,

Suzuki³

et al. 1989

J. Clin. Invest.

327

183

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Mast cells have been implicated in the pathogenesis of the matrix degradation observed in the cartilaginous and osseous structures of the rheumatoid joint. We previously reported that human mast cell tryptase, a 134-kD granule-associated neutral protease, is present in rheumatoid synovium and can activate collagenase in crude culture medium in vitro. The present study attempts to depict the precise mechanism of this activation. To express full activation of latent collagenase, matrix metalloproteinase 3 (MMP-3) or stromelysin, can be activated by tryptase in a time and dose-dependent manner. Tryptase was not capable of generating active collagenase in the crude media from cultured rheumatoid synoviocytes depleted of proMMP-3 by immunoadsorption. In addition, the function of the tissue inhibitor of metalloproteinases (TIMP) was not altered by tryptase, and SDS-PAGE analysis revealed no degradation of TIMP by tryptase. The tryptase dependent activation of synoviocyte procollagenase thereby appears to be entirely dependent upon its ability to activate proMMP-3.

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“…At the protein level, a similar observation has been made in bovine cartilage. Collagenase activator protein (CAP), which is now recognized to be prostromelysin (30), was shown to be synthesized predominantly in the superficial zone (31). Clearly, chondrocytes at all levels have the potential to synthesize prostromelysin, as illustrated by the uniform pattern of expression seen in cartilage cultured in the presence of IL-lI3, and therefore the pattern of metalloproteinase mRNA expression reflects a preferential stimulation of the superficial chondrocytes, rather than an inherent deficit in the deeper cells.…”

Section: Introductionmentioning

confidence: 99%

Preferential mRNA expression of prostromelysin relative to procollagenase and in situ localization in human articular cartilage.

Nguyen

Mort²,

Roughley³

1992

J. Clin. Invest.

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An imbalance between extracellular proteinases and their inhibitors is thought to underlie cartilage degradation. In cultures of adult cartilage, prostromelysin mRNA levels were much higher than those for procollagenase and this differential was increased in cultures stimulated with IL-1,6. Analysis of mRNA prepared from freshly isolated chondrocytes showed abundant amounts of prostromelysin mRNA in normal adult cartilage but low levels in the neonate. Not all adult cartilage may possess such high levels of prostromelysin mRNA, as the message levels in the cartilage remaining on late-stage osteoarthritic joints were lower than those in normal adult cartilage. Relative to prostromelysin mRNA, little procollagenase and TIMP mRNA were found in the adult cartilage. In situ hybridization revealed that metalloproteinase mRNAs were localized in chondrocytes of the superficial zone in adult cartilage. However, upon IL-1ft treatment, chondrocytes in all cartilage zones were observed tY express prostromelysin mRNA. Relative to the neonate, the normal adult cartilage appears to have a high degradative potential, if one accepts that steady-state mRNA levels reflect prostromelysin production. As the adult cartilage is not apparently undergoing rapid turnover, it would appear that control ofprostromelysin activation may be the major regulatory step in stromelysin-induced cartilage degradation. (J.

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Purification and characterization of collagenase activator protein synthesized by articular cartilage

Cited by 32 publications

References 14 publications

Association between degree of bone-erosion and synovial fluid-levels of tumor necrosis factor α in the knee-joints of patients with rheumatoid arthritis

Association between degree of bone-erosion and synovial fluid-levels of tumor necrosis factor α in the knee-joints of patients with rheumatoid arthritis

Synovial procollagenase activation by human mast cell tryptase dependence upon matrix metalloproteinase 3 activation.

Preferential mRNA expression of prostromelysin relative to procollagenase and in situ localization in human articular cartilage.

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