Determination of metalloproteinases, plasminogenactivators and their inhibitors in the synovial fluids of patients with rheumatoid arthritis during chemical synoviorthesis

Bläser, Jörg; Triebel, Susanne; Maasjosthusmann, Ulrich; Römisch, Jürgen; Krahl-Mateblowski, Ute; Freudenberg, W.; Fricke, R; Tschesche, Harald

doi:10.1016/0009-8981(95)06172-x

Cited by 47 publications

(34 citation statements)

References 30 publications

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“…In keeping with the current results, studies on the neutrophil inflammatory response have shown a positive association between MMP-9 and the proinflammatory cytokines IL-8 and TNF-a [8,9]. Along this line, BLÄ SER et al [23] reported that MMP-8 and MMP-9 correlate with u-PA and PAI-2 Ag in the synovial fluid of patients undergoing chemical synoviorthesis.…”

Section: Association Of Mmps and Timps With Inflammatory And Fibrinolsupporting

confidence: 88%

Metalloproteinases and tissue inhibitors of metalloproteinases in exudative pleural effusions

Iglesias¹

2005

European Respiratory Journal

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The aim of this study was to assess the expression of several metalloproteinases (MMPs) and tissue inhibitors of metalloproteinases (TIMPs) in exudative pleural effusions, and their relationship with inflammatory and fibrinolytic mediators in parapneumonic effusions.The study included 51 parapneumonic effusions (30 empyema or complicated parapneumonic, 21 noncomplicated parapneumonic), 28 tuberculous, 30 malignant and 30 transudates. Inflammatory markers (tumour necrosis factor-a, interleukin-8, polymorphonuclear elastase), fibrinolytic system variables (tissue plasminogen activator (PA), urokinase PA (u-PA), plasminogen activation inhibitor (PAI)-1, PAI-2), and several MMPs (MMP-1, MMP-2, MMP-8, MMP-9) and TIMPs (TIMP-1, TIMP-2) were determined by ELISA in plasma and pleural fluid.Elevated MMP-2 and TIMP-1 concentrations were observed in all the pleural fluid samples studied. The group of empyema or complicated parapneumonic effusions showed higher MMP-1, MMP-8 and MMP-9 concentrations than the remaining exudates. There was no correlation between MMP and TIMP levels in plasma and pleural fluid in this group of effusions. In parapneumonic effusions, MMP-1, MMP-8 and MMP-9 showed a positive correlation with the inflammatory markers and with u-PA and PAI-1. Moreover, there was a relationship between MMP-8 concentration in pleural fluid and pleural thickening at the end of treatment.In conclusion, elevated metalloproteinase-1, -8 and -9 expression was found in parapneumonic pleural effusions. These metalloproteinases could be implicated in the local inflammatory response existing in this group of effusions.

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Section: Association Of Mmps and Timps With Inflammatory And Fibrinolsupporting

confidence: 88%

Metalloproteinases and tissue inhibitors of metalloproteinases in exudative pleural effusions

Iglesias¹

2005

European Respiratory Journal

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“…Although the concentrations of MMPs are unknown in the interstitial fluid of atherosclerotic lesions, MMP concentrations have been measured in synovial fluids from arthritic joints, which like atherosclerotic lesions, are inflamed tissues. Thus, in the synovial fluid of patients with rheumatoid arthritis the concentrations of MMPs-1,-8, and -9 ranged from 1 to 15 g/ml (52), that of MMP-3 ranged from 6 to 110 g/ml, with a mean concentration of 40 g/ml (53). Importantly, synovial fluid from rheumatoid arthritis patients demonstrated 100-fold higher levels of active MMP-3 than synovial fluid from control subjects (54).…”

Section: Fig 6 Proteolytic Degradation Of Hdlmentioning

confidence: 99%

Matrix Metalloproteinases-3, -7, and -12, but Not -9, Reduce High Density Lipoprotein-induced Cholesterol Efflux from Human Macrophage Foam Cells by Truncation of the Carboxyl Terminus of Apolipoprotein A-I

Lindstedt

Saarinen

Kalkkinen

et al. 1999

Journal of Biological Chemistry

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Matrix metalloproteinases (MMPs) have been suggested to function in remodeling of the arterial wall, but no information is available on their possible role in early atherogenesis, when cholesterol accumulates in the cells of the arterial intima, forming foam cells. Here, we incubated the major component responsible for efflux of cholesterol from foam cells, high density lipoprotein 3 (HDL 3 ), with MMP-1, -3, -7, -9, or -12 at 37°C before adding it to cholesterol-loaded human monocyte-derived macrophages. After incubation with MMP-3, -7, or -12, the ability of HDL 3 to induce the high affinity component of cholesterol efflux from the macrophage foam cells was strongly reduced, whereas preincubation with MMP-1 reduced cholesterol efflux only slightly and preincubation with MMP-9 had no effect. These differential effects of the various MMPs were reflected in their differential abilities to degrade the small pre-␤ migrating particles present in the HDL 3 fraction. NH 2 -terminal sequence and mass spectrometric analyses of the apolipoprotein (apo) A-I fragments generated by MMPs revealed that those MMPs that strongly reduced cholesterol efflux (MMPs-3, -7, and -12) cleaved the COOH-terminal region of apoA-I and produced a major fragment of about 22 kDa, whereas MMPs-1 and -9, which had little and no effect on cholesterol efflux, degraded apoA-I only slightly and not at all, respectively. These results show, for the first time, that some members of the MMP family can degrade the apoA-I of HDL 3 , so blocking cholesterol efflux from macrophage foam cells. This expansion of the substrate repertoire of MMPs to include apoA suggests that these proteinases are directly involved in the accumulation of cholesterol in atherosclerotic lesions.

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“…MMP-9 can also break down myelin basic protein, and the generation of myelin peptides via MMP-9 is thought to lead to an autoreactive neuritis (41). In rheumatoid arthritis (RA), MMPs play a similar destructive role (5,28,30,53). Monocyte/macrophage-derived MMP-1 and MMP-9 along with MMPs released from synoviocytes and neutrophils are thought to be responsible for collagen degradation and joint destruction in RA (11,48,51,56).…”

mentioning

confidence: 99%

BorreliaSpirochetes Upregulate Release and Activation of Matrix Metalloproteinase Gelatinase B (MMP-9) and Collagenase 1 (MMP-1) in Human Cells

Gebbia¹,

Coleman

Benach

2001

Infect Immun

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Borrelia burgdorferi, the spirochetal agent of Lyme disease, stimulated human peripheral blood monocytes to release pro-matrix metalloproteinase-9 (gelatinase B; pro-MMP-9) and active matrix metalloproteinase-1 (collagenase-1; MMP-1). Human neutrophils also released pro-MMP-9 and a 130-kDa protein with gelatinolytic activity in response to live B. burgdorferi. In addition, U937 cells and human keratinocyte cells were also stimulated to release pro-MMP-9 under the same conditions. However, human umbilical vein endothelial cells (HUVECs) released pro-MMP-9 and pro-MMP-2 in a constitutive manner and were not influenced by live spirochetes. MMPs produced by human monocytes also enhanced the penetration of B. burgdorferi through extracellular matrix component barriers in vitro. Plasmin stabilized on the surface of the Lyme disease spirochete was shown to activate pro-MMP-9 to its active form. This active form was also observed in the plasma of mice infected with a relapsing fever borrelia. These results suggest that borreliae can upregulate MMPs and possibly mediate an activation cascade initiated by plasmin bound to the microbial surface. MMPs may play a role in dissemination of the Lyme disease spirochete and in the pathogenesis of Borrelia infection.

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Determination of metalloproteinases, plasminogenactivators and their inhibitors in the synovial fluids of patients with rheumatoid arthritis during chemical synoviorthesis

Cited by 47 publications

References 30 publications

Metalloproteinases and tissue inhibitors of metalloproteinases in exudative pleural effusions

Metalloproteinases and tissue inhibitors of metalloproteinases in exudative pleural effusions

Matrix Metalloproteinases-3, -7, and -12, but Not -9, Reduce High Density Lipoprotein-induced Cholesterol Efflux from Human Macrophage Foam Cells by Truncation of the Carboxyl Terminus of Apolipoprotein A-I

BorreliaSpirochetes Upregulate Release and Activation of Matrix Metalloproteinase Gelatinase B (MMP-9) and Collagenase 1 (MMP-1) in Human Cells

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