Tumor necrosis factor α (TNFα) induces pro‐matrix metalloproteinase 9 production in human uterine cervical fibroblasts but interleukin 1 α antagonizes the inductive effect of TNFα

Sato, Takashi; Ito, Akira; Osuga, Yutaka; Nagase, Hideaki; Mori, Yo

doi:10.1016/0014-5793(96)00808-3

Cited by 42 publications

(22 citation statements)

References 26 publications

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“…Gelatin Zymography-Gelatinolytic activity in the harvested culture media was detected by gelatin zymography with 10% (w/v) acrylamide gel containing gelatin (0.6 mg/ml; Difco) as described previously (37).…”

Section: Methodsmentioning

confidence: 99%

Furin-independent Pathway of Membrane Type 1-Matrix Metalloproteinase Activation in Rabbit Dermal Fibroblasts

Sato¹,

Kondo²,

Fujisawa³

et al. 1999

Journal of Biological Chemistry

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We investigated the gene expression and intracellular activity of processing protease furin and its involvement in the process of membrane type 1-matrix metalloproteinase (MT1-MMP) activation in rabbit dermal fibroblasts. When the rabbit fibroblasts were treated with concanavalin A (ConA), pro-MMP-2 was converted to an active 62-kDa MMP-2 through the appearance of a 64-kDa intermediate MMP-2. The ConA-induced pro-MMP-2 activation resulted from increasing the gene expression and production of MT1-MMP in the rabbit fibroblasts. Reverse transcriptase-polymerase chain reaction demonstrated that in rabbit dermal fibroblasts furin mRNA was detected and, unlike MT1-MMP, was not increased by ConA. These findings are further supported by the fact that the intracellular furin activity also was constitutively detected and was unchanged by the ConA treatment. Very similar phenomena were also observed in human uterine cervical fibroblasts, which are known to produce MT1-MMP by ConA stimulation. These results suggest that the expression of the furin gene and the intracellular activity are not regulated by ConA. On the other hand, neither a synthetic furin inhibitor, decanoyl-RVKR-CH 2 Cl (25-100 M) nor a furin antisense oligonucleotide (40 M) inhibited the MT1-MMP-mediated pro-MMP-2 activation in ConA-treated rabbit dermal fibroblasts, whereas these compounds interfered with pro-MMP-2 activation in ConA-treated human uterine cervical fibroblasts. Nonetheless, the furin antisense oligonucleotide completely suppressed furin gene expression in both rabbit and human fibroblasts. These results suggest that furin does not participate in the process of MT1-MMP activation induced by ConA in rabbit dermal fibroblasts.

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Section: Methodsmentioning

confidence: 99%

Furin-independent Pathway of Membrane Type 1-Matrix Metalloproteinase Activation in Rabbit Dermal Fibroblasts

Sato¹,

Kondo²,

Fujisawa³

et al. 1999

Journal of Biological Chemistry

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“…41 Some mesenchymal cells also produce this enzyme in response to certain stimuli. [42][43][44] Our coimmunolocalization studies of MMP-9 and HAM-56 in AAA aortic tissue showed that MMP-9 is a product of macrophages. Although these results are consistent with those of in situ hybridization studies by Thompson et al 21 and McMillan et al, 23 Patel et al 34 reported that AAA-derived SMCs in culture produce MMP-9.…”

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confidence: 86%

Matrix Metalloproteinase-2 Production and Its Binding to the Matrix Are Increased in Abdominal Aortic Aneurysms

Davis

Persidskaia

Baca-Regen

et al. 1998

ATVB

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227

196

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Abstract-Degradation of the elastic media is a hallmark of abdominal aortic aneurysms (AAAs). We examined the expression of 2 elastolytic matrix metalloproteinases (MMPs), MMP-2 and MMP-9, in AAA aortic tissues compared with those from atherosclerotic occlusive disease (AOD) and nondiseased control tissues. Quantitative competitive reverse transcription-polymerase chain reaction and gelatin zymography showed increased MMP-9 mRNA and protein in both AAA and AOD tissues compared with those in control tissue, but there was no significant difference between AAA and AOD. In contrast, MMP-2 mRNA and protein levels were significantly higher in AAA than in AOD or control tissues. Sequential extraction of the MMPs from the aortic tissue with a physiological salt solution, 2% dimethylsulfoxide (DMSO), and 10 mol/L urea showed that large amounts of MMP-2 and MMP-9 were bound to the matrix. The most conspicuous finding was that the levels of MMP-2 were significantly elevated in the DMSO fraction in AAA tissues compared with AOD and control tissues. In addition, a large portion of MMP-2 found in the DMSO and urea fractions was in the active 62-kDa form, indicating that the precursor of MMP-2 in AAA is largely activated locally and binds to the tissue matrix tightly. By immunolocalization, MMP-9 was found to be primarily produced by macrophages and MMP-2 by mesenchymal cells.

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“…For immunoblotting, proteins of the culture medium (10 µl from 1×10 6 cells) separated by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) under reducing conditions were transferred onto a nitrocellulose membrane. The membrane was blocked and treated for 1 h at room temperature with antibodies against human MMPs (anti-humanproMMP-1, proMMP-2, proMMP-3 and proMMP-9) [10,15]. The rest of the samples were stored at -80°for further Western blotting as controls.…”

Section: Western Blot Analysismentioning

confidence: 99%

Matrix metalloproteinases in patients with osteoarthritis of the hip

Masuhara¹,

Lee

Nakai

et al. 2000

International Orthopaedics

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In 78 patients undergoing a total hip replacement we examined the production of matrix metalloproteinases (MMP) by the fibroblasts from the connective tissue of the acetabulum; we then correlated these findings with clinical and radiological characteristics of the same patients. In 53 patients only MMP-2 was produced; in 15 cases MMP-1, -2 and -3 were present; and in 10 cases not only MMP-1, -2, -3 but also MMP-9. Significant differences among the clinical and radiological parameters were found in the 3 subsets. A positive correlation between the production of MMP-9 and a rapid destruction of the hip joint was found.Résumé Nous avons examiné la production de métallo-protéinases (MMP) par des fibroblastes dans 78 patients souffrant d'une ostéo-arthrite de la hanche. La production de MMP fut classée en 3 sous-sembles: 53 patients dans lequel seulement des MMP-2 furent détectées; 15 patients dans lequels des MMP-1, -2 et -3 étaient pré-sentes; et 10 patients où des MMP-1, -2, -3 et aussi des MMP-9 furent détectées. Des différences importantes furent découvertes pour des paramètres cliniques et radiologiques parmi les sous-sembles. Il y'a une correlation positive entre la production de MMP-9 et une destruction rapide de la hanche.

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Tumor necrosis factor α (TNFα) induces pro‐matrix metalloproteinase 9 production in human uterine cervical fibroblasts but interleukin 1 α antagonizes the inductive effect of TNFα

Cited by 42 publications

References 26 publications

Furin-independent Pathway of Membrane Type 1-Matrix Metalloproteinase Activation in Rabbit Dermal Fibroblasts

Furin-independent Pathway of Membrane Type 1-Matrix Metalloproteinase Activation in Rabbit Dermal Fibroblasts

Matrix Metalloproteinase-2 Production and Its Binding to the Matrix Are Increased in Abdominal Aortic Aneurysms

Matrix metalloproteinases in patients with osteoarthritis of the hip

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