Amplification of IL-1β-Induced Matrix Metalloproteinase-9 Expression by Superoxide in Rat Glomerular Mesangial Cells Is Mediated by Increased Activities of NF-κB and Activating Protein-1 and Involves Activation of the Mitogen-Activated Protein Kinase Pathways

Eberhardt, W.; Huwiler, Andrea; Beck, Karl‐Friedrich; Walpen, Sebastian; Pfeilschifter, Josef

doi:10.4049/jimmunol.165.10.5788

Cited by 202 publications

(191 citation statements)

References 51 publications

(46 reference statements)

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“…Cigarette smoke may increase matrix metalloproteinase expression via activation of inflammatory transcription factors. The expression of the AP-1 transcription factor complex is positively associated with matrix metalloproteinase expression, 94,95 and cigarette smoke is associated with increased expression of AP-1. 96,97 Secretion of MMP-1 and MMP-3 from macrophages stimulated in vitro or in vivo depends on the activation of NF-B, 98 and NF-B is required for cytokine upregulation of MMP-1, MMP-3, and MMP-9 in VSMCs.…”

Section: Smoking and Regulation Of Matrix Metalloproteinase Activitymentioning

confidence: 99%

Smoking, Metalloproteinases, and Vascular Disease

Perlstein

Lee

2006

ATVB

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Abstract-Smoking causes up to 11% of total global cardiovascular deaths. Smoking has numerous effects that may promote atherosclerosis through vascular inflammation and oxidative stress, but the pathogenesis of smoking-related cardiovascular disease remains incompletely understood. The matrix metalloproteinases, a family of endopeptidases that can degrade extracellular matrix components in both physiological and pathophysiological states, play an important role in smoking-associated chronic obstructive pulmonary disease, the second leading cause of smoking attributable mortality. Emerging evidence indicates that the matrix metalloproteinases may also contribute to smoking-related vascular disease. Here we discuss the potential relationship between smoking, matrix metalloproteinases, and acceleration of vascular disease.

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Section: Smoking and Regulation Of Matrix Metalloproteinase Activitymentioning

confidence: 99%

Smoking, Metalloproteinases, and Vascular Disease

Perlstein

Lee

2006

ATVB

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“…are similar to other MMPs except for the addition of a transmembrane domain and a cytoplasmic tail at the C terminus; and MT-MMPs are also expressed in many carcinomas (Seiki, 1999). The activities of the MMPs are regulated by gene expression (Eberhardt et al, 2000;Sato and Seiki, 1993), proenzyme activation (Crabbe et al, 1994;Imai et al, 1995) and inhibition of the active enzymes by their specific tissue inhibitors (Gomez et al, 1997).…”

Section: Introductionmentioning

confidence: 99%

Adenovirus-mediated expression of antisense MMP-9 in glioma cells inhibits tumor growth and invasion

et al. 2002

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Matrix metalloproteinase 9 (MMP-9) is known to play a major role in cell migration and invasion in both physiological and pathological processes. Our previous work has shown that increased MMP-9 levels are associated with human glioma tumor progression. In this study, we evaluated the ability of an adenovirus containing a 528 bp cDNA sequence in antisense orientation to the 5' end of the human MMP-9 gene (Ad-MMP-9AS) to inhibit the invasiveness and migratory capacity of the human glioblastoma cell line SBN19 in in vitro and in vivo models. Infection of glioma cells with Ad-MMP-9AS reduced MMP-9 enzyme activity by approximately 90% compared with mock-or Ad-CMV-infected cells. Migration and invasion of glioblastoma cells infected with Ad-MMP-9AS were significantly inhibited relative to Ad-CMV-infected controls in spheroid and Matrigel assays. Intracranial injections of SNB19 cells infected with Ad-MMP-9AS did not produce tumors in nude mice. However, injecting the Ad-MMP-9AS construct into subcutaneous U87MG tumors in nude mice caused regression of tumor growth. These results support the theory that adenoviral-mediated delivery of the MMP-9 gene in the antisense orientation has therapeutic potential for treating gliomas.

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“…MMP-9 Induction in C6 Cells or in Clones Overexpressing PKC-Is NF-B-dependent-Up-regulation of mmp-9 gene expression upon exposure to inflammatory cytokines critically depends on the activation of NF-B (24,25). To evaluate the possible implication of this transcription factor in the regulation of MMP-9 by PKC-, we tested the effect of an NF-Bspecific inhibitory peptide, SN50, that blocks its translocation to the nucleus (26).…”

Section: Fig 2 Induction Of Pkc-activity By Il-1 and Tnf-␣mentioning

confidence: 99%

Protein Kinase C-ζ Regulates Transcription of the Matrix Metalloproteinase-9 Gene Induced by IL-1 and TNF-α in Glioma Cells via NF-κB

Estève

Chicoine

Robledo

et al. 2002

Journal of Biological Chemistry

183

124

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The regulation of matrix metalloproteinase-9 (MMP-9) expression in glioma cells is one of the key processes in tumor invasion through the brain extracellular matrix. Although some studies have demonstrated the implication of classic protein kinase C (PKC) isoforms in the regulation of MMP-9 production by phorbol esters or lipopolysaccharide, the involvement of specific PKC isoforms in the signaling pathways leading to MMP-9 expression by inflammatory cytokines remains unclear. Here we report that the atypical PKC-isoform participates in the induction of MMP-9 expression by interleukin-1 (IL-1) and tumor necrosis factor-␣ (TNF-␣) in rat C6 glioma cells. Indeed, zymography and semi-quantitative reverse transcriptase-PCR analysis showed that pretreatment of C6 cells with PKC-pseudosubstrate abolished MMP-9 activity and gene expression induced by IL-1 or TNF-␣. Accordingly, IL-1 and TNF-␣ were able to induce PKC-activity, as demonstrated by in vitro kinase assay using immunoprecipitated PKC-. Furthermore, stable C6 clones overexpressing PKC-, but not PKC-⑀, displayed an up-regulation of MMP-9 constitutive expression as well as an increase of mmp-9 promoter activity. These processes were inhibited by an NF-B-blocking peptide and completely prevented by NF-B-binding site mutation in the mmp-9 promoter. Taken together, these results indicate that PKC-plays a key role in the regulation of MMP-9 expression in C6 glioma cells through NF-B.Glioma cells have the ability to invade brain tissues by secreting matrix metalloproteinases (MMPs), 1 a family of proteases able to degrade different components of the extracellular matrix including collagen, fibronectin, and proteoglycans. One of these MMPs, MMP-9, has received much attention as its expression correlates with the progression of glioma (1). Furthermore, MMP-9 seems to be essential for the invasiveness of glioma cells, as it was recently reported that the inhibition of MMP-9 expression by antisense gene transfer strongly reduced the invasion of glioblastoma cells in vitro and in vivo (2). Therefore, understanding the role of the molecules implicated in the signaling pathways leading to mmp-9 gene expression in glioma cells is important in order to identify new therapeutic targets. Several studies (3-5) have focused on the implication of protein kinase C (PKCs) in the regulation of mmp-9 gene expression, most notably by testing the effect of phorbol 12-myristate 13-acetate (PMA) on different types of cells, including human glioma cells. Members of the PKC family are divided into the following three groups of isoenzymes: the conventional PKC isoforms, which are activated by calcium and diacylglycerol (␣, ␤I, ␤II, and ␥); the novel PKCs, which are activated by diacylglycerol but are calcium-insensitive (␦, ⑀, , and ); and the atypical PKCs, which are calcium-and diacylglycerol-insensitive ( and /). Despite the fact that a large number of studies (5-7) have established a link between PKCs and MMP-9 expression using PKC inhibitors, very few studies have addressed the implicat...

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Amplification of IL-1β-Induced Matrix Metalloproteinase-9 Expression by Superoxide in Rat Glomerular Mesangial Cells Is Mediated by Increased Activities of NF-κB and Activating Protein-1 and Involves Activation of the Mitogen-Activated Protein Kinase Pathways

Cited by 202 publications

References 51 publications

Smoking, Metalloproteinases, and Vascular Disease

Smoking, Metalloproteinases, and Vascular Disease

Adenovirus-mediated expression of antisense MMP-9 in glioma cells inhibits tumor growth and invasion

Protein Kinase C-ζ Regulates Transcription of the Matrix Metalloproteinase-9 Gene Induced by IL-1 and TNF-α in Glioma Cells via NF-κB

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