<b>TNF‐α‐mediated expression of membrane‐type matrix metalloproteinase in rheumatoid synovial fibroblasts</b>

Migita, Kiyoshi; Eguchi, Katsumi; Kawabe, Yojiro; Ichinose, Yasufumi; Tsukada, Toshiaki; Aoyagi, Takahiko; Nakamura, Hideki; Nagataki, Shigenobu

doi:10.1046/j.1365-2567.1996.d01-789.x

Cited by 85 publications

(52 citation statements)

References 21 publications

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“…Reverse Transcriptase-Polymerase Chain Reaction (RT-PCR)-A total of 3 g of isolated RNA was subjected to first strand cDNA synthesis with Moloney-murine leukemia virus reverse transcriptase, RNase inhibitor (Roche Molecular Biochemicals), and oligo(dT) [12][13][14][15][16][17][18] primer (Life Technologies, Inc.) for 1 h at 37°C according to the manufacturer's instructions. One-tenth of the cDNA generated from the reverse transcriptase reaction was used for PCR amplification in the presence of Taq DNA polymerase (Roche Molecular Biochemicals) and oligonucleotide primers, 5Ј-CAG ATC TTC GGG GAC TAT TAC CAC-3Ј (sense) and 5Ј-CCT GTT GTC ATT CAT CTG TGT GTA CC-3Ј (antisense).…”

Section: Methodsmentioning

confidence: 99%

“…Recent studies have shown that MT1-MMP is an endogenous activator of pro-MMP-2 (9). On the other hand, the increased expression of MT1-MMP has been correlated with physiological and pathological events such as embryogenesis (10), wound healing (11), angiogenesis (12), rheumatoid arthritis (13), osteoarthritis (14). and tumor invasion (15)(16)(17).…”

Section: Extracellular Matrix (Ecm)mentioning

confidence: 99%

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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%

Section: Extracellular Matrix (Ecm)mentioning

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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“…Effect of Selenite on Stimulatory or Inhibitory Chemicals of MMP-9 Expression-We attempted to detect whether selenite is also effective in the presence of TPA and TNF-␣, which are known to up-regulate MMP-9 expression and activate pro-MMP-2 to active MMP-2 (19,20). Treatment of HT1080 cells with TPA and TNF-␣ resulted in increased levels of MMP-9 expression, but pretreatment with selenite also decreased level of MMP-9 (Fig.…”

Section: Effects Of Selenite and Selenate On Adhesion Of Ht1080 Cellsmentioning

confidence: 99%

Inhibitory Effect of Selenite on Invasion of HT1080 Tumor Cells

Yoon

Kim

Chung

2001

Journal of Biological Chemistry

161

114

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Selenium, an essential biological trace element, has been shown to reduce and prevent the incidence of cancer. Our previous studies have shown that selenite is involved in the chemoprevention of cancer and induction of apoptosis of cancer cells. In this study, we demonstrate that selenite also inhibits the invasion of tumor cells. Cancer cell invasion requires coordinated processes, such as changes in cell-cell and cell-matrix adhesion, degradation of the extracellular matrix, and cell migration. We found that selenite inhibited invasion of HT1080 human fibrosarcoma cells. Adhesion of HT1080 cells to the collagen matrix was also inhibited by treatment with selenite, but cell-cell interaction and cell motility were not affected by selenite. Moreover, selenite reduced expression of matrix metalloproteinase-2 and -9 and urokinase-type plasminogen activator, which are involved in matrix degradation, but increased a tissue inhibitor of metalloproteinase-1. This inhibitory effect of selenite on the protease expressions was mediated by the suppression of transcription factors, NF-B and AP-1. However, selenate showed no remarkable effect on all the steps of cancer cell invasion.Metastasis is the major cause of death among cancer patients. The cancer cells metastasis requires several sequential steps, such as changes in cell-ECM 1 interaction, disconnection of intercellular adhesions, and separation of single cells from solid tumor tissue, degradation of ECM, locomotion of tumor cells into the extracellular matrix, invasion of lymph and blood vessels, immunologic escape in the circulatory system, adhesion to endothelial cells, extravasation from lymph and blood vessels, proliferation of cells, and induction of angiogenesis (1).Attachment of cells to ECM molecules is mediated by the integrin family of extracellular matrix receptors. Integrins are a large family of heterodimeric proteins that transduce a variety of signals from the ECM. Through integrin and matrix interactions, many of the genes, which are critical for cell migration, survival, proliferation, differentiation (2), and ECM degradation, are activated (3, 4). In the majority of metastasizing tumors, cellular interactions with the ECM, which promote adhesion and migration, are thought to be required for primary tumor invasion, migration, and metastasis.The main groups of proteolytic enzymes involved in the tumor invasion are matrix metalloproteinases (MMPs) and serine proteases. The MMPs, a family of zinc-dependent endopeptidases, are involved in tumor invasion, metastasis, and angiogenesis in cancer (5). MMPs are important enzymes for the proteolysis of extracellular matrix proteins such as collagen, proteoglycan, elastin, laminin, and fibronectin (6). MMPs are synthesized as preproenzymes, and most of them are secreted from the cells as proenzymes. Among human MMPs reported previously, MMP-2 (gelatinase A/M r 72,000 type IV collagenase) and MMP-9 (gelatinase B/M r 92,000 type IV collagenase) are thought to be key enzymes for degrading type IV collagen, which ...

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“…Previous reports have shown that MMPs are regulated by various cytokines in different tissues [13][14][15][16][17]. The basal lamina of LECs is composed primarily of collagen type IV and laminin, which are the substrates for MMP-2 [20].…”

Section: Expression Of Mmp Mrnas Following Treatment With Tgf-βmentioning

confidence: 99%

Overexpression of matrix metalloproteinase-2 mediates phenotypic transformation of lens epithelial cells

et al. 2001

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TNF‐α‐mediated expression of membrane‐type matrix metalloproteinase in rheumatoid synovial fibroblasts

Cited by 85 publications

References 21 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

Inhibitory Effect of Selenite on Invasion of HT1080 Tumor Cells

Overexpression of matrix metalloproteinase-2 mediates phenotypic transformation of lens epithelial cells

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