Matrix Metalloproteinase-9 Is Necessary for the Regulation of Smooth Muscle Cell Replication and Migration After Arterial Injury

Cho, Aesim; Reidy, Michael A.

doi:10.1161/01.res.0000040420.17366.2e

Cited by 304 publications

(278 citation statements)

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“…Cho and Reidy (2002) have demonstrated in mice lacking the MMP-9 gene that MMP-9 is critical for VSMC migration and the formation of neointima. Diabetes mellitus has been identified as an independent risk factor for the development of atherosclerosis and is considered a coronary-heart-disease risk equivalent.…”

Section: Discussionmentioning

confidence: 99%

“…VSMC migration, which depends on an alteration of the proteolytic balance within the arterial wall toward matrix breakdown, is partly mediated by matrix metalloproteinases (MMPs). MMP-9 is indispensable for the degradation of type IV collagen, a major component of the basement membrane (Zucker et al, 1993;Cho and Reidy, 2002). Recent experimental data have shown that hyperglycemic diabetes can induce altered expression of the genes encoding MMP-9 (Death et al, 2003) and plasma levels and zymographic activities of MMP-9 are increased in diabetics with peripheral arterial disease as compared with non-diabetics (Signorelli et al, 2005).…”

Section: Introductionmentioning

confidence: 99%

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α-Lipoic acid inhibits matrix metalloproteinase-9 expression by inhibiting NF-κB transcriptional activity

Kim

Kim²,

Park³

et al. 2007

Exp Mol Med

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Abbreviations: ALA, α-lipoic acid; AP-1, activator protein-1; MMP-9, matrix metalloproteinase-9; VSMC, vascular smooth muscle cell AbstractThe migration of vascular smooth muscle cells (VSMCs) into the intima, an important step in injury-induced neointimal hyperplasia, requires the activation of nuclear factor-κB (NF-κB) and the consequent up-regulation of matrix metalloproteinase-9 (MMP-9). This study was undertaken to test for a possible effect of α-lipoic acid (ALA), a potent inhibitor of NF-κB, on MMP-9 expression. ALA inhibited high-glucose-and TNF-α-stimulated VSMC migrations in vitro. It also inhibited high-glucoseand TNF-α-induced increases in MMP-9 expression. The activity of MMP-9-promoter constructs with mutations in the NF-κB binding site was not inhibited by ALA, indicating an involvement of the NF-κB signaling pathway in the ALA-specific inhibition of MMP-9. These data suggest the possibility that ALA may be useful for the prevention of neointimal hyperplasia after angioplasty, by inhibiting the NF-κB/ MMP-9 pathway, especially with hyperglycemia.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

α-Lipoic acid inhibits matrix metalloproteinase-9 expression by inhibiting NF-κB transcriptional activity

Kim

Kim²,

Park³

et al. 2007

Exp Mol Med

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“…Macrophages, depending on their origin and state of activation, express several members of the MMP family including MMP-9 (23, 24). As observed for the uPA/plasminogen system, several studies have suggested a role for MMP-9 in cell migration, and leukocyte infiltration and tissue remodeling are reduced in MMP-9 null mice (20,(25)(26)(27)(28)(29).Because of their role in migration and/or tissue remodeling, the regulation of uPA and MMP-9 expression in macrophages has received much attention. The expression of both proteinases, as well as their specific inhibitors, is regulated by cytokines and growth factors (30 -32).…”

mentioning

confidence: 98%

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confidence: 99%

Extracellular Matrix-induced Cyclooxygenase-2 Regulates Macrophage Proteinase Expression

Khan

Howe

Falcone

2004

Journal of Biological Chemistry

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Chronic inflammatory diseases are characterized by the persistent presence of macrophages and other mononuclear cells, tissue destruction, cell proliferation, and the deposition of extracellular matrix (ECM). The tissue degradation is mediated, in part, by enhanced proteinase expression by macrophages. It has been demonstrated recently that macrophage proteinase expression can be stimulated or inhibited by purified ECM components. However, in an intact ECM the biologically active domains of matrix components may be masked either by tertiary conformation or by complex association with other matrix molecules. In an effort to determine whether a complex ECM produced by vascular smooth muscle cells (SMC) regulates macrophage degradative phenotype, we prepared insoluble SMC matrices and examined their ability to regulate proteinase expression by RAW264.7 and thioglycollate-elicited peritoneal macrophages. Here we demonstrate that macrophage engagement of SMC-ECM triggers PKC-dependent activation of MAPK erk1/2 leading to increased expression of cyclooxygenase (COX)-2 and prostaglandin (PG) E 2 synthesis. The addition of PGE 2 to macrophage cultures stimulates their expression of both urokinase-type plasminogen activator and MMP-9, and the selective COX-2 inhibitor NS-398 blocks ECMinduced proteinase expression. Moreover, ECM-induced PGE 2 and MMP-9 expression by elicited COX-2 ؊/؊ macrophages is markedly reduced when compared with the response of either COX-2 ؉/؊ or COX-2 ؉/؉ macrophages. These data clearly demonstrate that SMC-ECM exerts a regulatory role on the degradative phenotype of macrophages via enhanced urokinase-type plasminogen activator and MMP-9 expression, and identify COX-2 as a targetable component of the signaling pathway leading to increased proteinase expression.The structural integrity of tissue is compromised in a variety of inflammatory settings by macrophage expression of serine and matrix metalloproteinases (MMPs). 1 Principal among the serine proteinases is urokinase-type plasminogen activator (uPA) (1). Cleavage of plasminogen by uPA generates plasmin, which binds to and degrades fibrin and components of the ECM (2-4). Several studies have demonstrated that uPA-dependent plasminogen activation regulates macrophage migration (5-7), degradation of extracellular matrices (7-9) and fibrin (10, 11), and the release of matrix-bound growth factors (12-14). Moreover, the important role of plasminogen activation in macrophage migration and clearance of fibrin and necrotic tissue following injury has been confirmed by utilizing mice deficient in components of the uPA-plasminogen system (15)(16)(17)(18)(19)(20).In addition to the uPA/plasminogen system, macrophages express MMPs, which are associated with tissue remodeling via their ability to degrade ECM components (21,22). Macrophages, depending on their origin and state of activation, express several members of the MMP family including MMP-9 (23, 24). As observed for the uPA/plasminogen system, several studies have suggested a role for MMP-9 in cell ...

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“…Thinning of the fibrous cap by MMPs is undesirable due to the release of sequestered factors that leads to thrombosis [15]. TNF-α regulation of MMP-9 is of particular importance in atherosclerotic lesion development and in fibrous cap thinning [3,20]. Thus, up-regulation of MMP-9 expression by TNF-α can promote development of atherosclerotic lesions by multiple mechanisms that include stimulation of SMC proliferation and MMP-9 production.…”

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confidence: 99%

Lysyl oxidase propeptide inhibits smooth muscle cell signaling and proliferation

Hurtado

Vora

Sume

et al. 2008

Biochemical and Biophysical Research Communications

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Lysyl oxidase is required for the normal biosynthesis and maturation of collagen and elastin. It is expressed by vascular smooth muscle cells, and its increased expression has been previously found in atherosclerosis and in models of balloon angioplasty. The lysyl oxidase propeptide (LOX-PP) has more recently been found to have biological activity as a tumor suppressor, and it inhibits Erk1/2 Map kinase activation. We reasoned that LOX-PP may have functions in normal non-transformed cells. We, therefore, investigated its effects on smooth muscle cells, focusing on important biological processes mediated by Erk1/2-dependent signaling pathways including proliferation and matrix metalloproteinase-9 (MMP-9) expression. In addition, we investigated whether evidence for accumulation of LOX-PP could be found in vivo in a femoral artery injury model. Recombinant LOX-PP was expressed and purified, and was found to inhibit primary rat aorta smooth muscle cell proliferation and DNA synthesis by more than 50%. TNF-α-stimulated MMP-9 expression and Erk1/2 activation were both significantly inhibited by LOX-PP. Immunohistochemistry studies carried out with affinity purified anti-LOX-PP antibody showed that LOX-PP epitopes were expressed at elevated levels in vascular lesions of injured arteries. These novel data suggest that LOX-PP may provide a feedback control mechanism that serves to inhibit properties associated with the development of vascular pathology.Tumor necrosis factor-α (TNF-α) contributes to the development of atherosclerotic lesions [15]. Important among its many activities, TNF-α promotes the proliferation of smooth muscle cells (SMCs) [15] and it stimulates matrix metalloproteinase (MMP) production [6]. Thinning of the fibrous cap by MMPs is undesirable due to the release of sequestered factors that leads to thrombosis [15]. TNF-α regulation of MMP-9 is of particular importance in atherosclerotic lesion development and in fibrous cap thinning [3,20]. Thus, up-regulation of MMP-9 expression by TNF-α can promote development of atherosclerotic lesions by multiple mechanisms that include stimulation of SMC proliferation and MMP-9 production.

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Matrix Metalloproteinase-9 Is Necessary for the Regulation of Smooth Muscle Cell Replication and Migration After Arterial Injury

Cited by 304 publications

References 35 publications

α-Lipoic acid inhibits matrix metalloproteinase-9 expression by inhibiting NF-κB transcriptional activity

α-Lipoic acid inhibits matrix metalloproteinase-9 expression by inhibiting NF-κB transcriptional activity

Extracellular Matrix-induced Cyclooxygenase-2 Regulates Macrophage Proteinase Expression

Lysyl oxidase propeptide inhibits smooth muscle cell signaling and proliferation

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