Preferential inhibition of 72- and 92-kDa gelatinases by tissue inhibitor of metalloproteinases-2

Howard, Eric W.; Bullen, Elizabeth C.; Banda, Michael J.

doi:10.1016/s0021-9258(18)98804-6

Cited by 193 publications

(21 citation statements)

References 36 publications

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“…MMPs currently are classified as a family of more than 20 proteinases whose members are expressed either as secreted or membrane-anchored enzymes (22). The endogenous tissue inhibitor of metalloproteinases (TIMP-1), preferentially targets secreted MMPs as well as the glycophosphatidylinositolanchored MMPs (i.e., MT4-MMP and MT6-MMP) (22)(23)(24). A second member of the TIMP family, TIMP-2, more potently inhibits secreted MMPs, MMP-2, and MMP-9, as well as the type I membrane-anchored MMPs (i.e., MT1-, 2-, 3-, and 5-MMPs) (22)(23)(24).…”

Section: Articlementioning

confidence: 99%

MT1-matrix metalloproteinase directs arterial wall invasion and neointima formation by vascular smooth muscle cells

Filippov

Koenig

Chun

et al. 2005

The Journal of Experimental Medicine

122

111

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During pathologic vessel remodeling, vascular smooth muscle cells (VSMCs) embedded within the collagen-rich matrix of the artery wall mobilize uncharacterized proteolytic systems to infiltrate the subendothelial space and generate neointimal lesions. Although the VSMC-derived serine proteinases, plasminogen activator and plasminogen, the cysteine proteinases, cathepsins L, S, and K, and the matrix metalloproteinases MMP-2 and MMP-9 have each been linked to pathologic matrix-remodeling states in vitro and in vivo, the role that these or other proteinases play in allowing VSMCs to negotiate the three-dimensional (3-D) cross-linked extracellular matrix of the arterial wall remains undefined. Herein, we demonstrate that VSMCs proteolytically remodel and invade collagenous barriers independently of plasmin, cathepsins L, S, or K, MMP-2, or MMP-9. Instead, we identify the membrane-anchored matrix metalloproteinase, MT1-MMP, as the key pericellular collagenolysin that controls the ability of VSMCs to degrade and infiltrate 3-D barriers of interstitial collagen, including the arterial wall. Furthermore, genetic deletion of the proteinase affords mice with a protected status against neointimal hyperplasia and lumen narrowing in vivo. These studies suggest that therapeutic interventions designed to target MT1-MMP could prove beneficial in a range of human vascular disease states associated with the destructive remodeling of the vessel wall extracellular matrix.

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Section: Articlementioning

confidence: 99%

MT1-matrix metalloproteinase directs arterial wall invasion and neointima formation by vascular smooth muscle cells

Filippov

Koenig

Chun

et al. 2005

The Journal of Experimental Medicine

122

111

View full text Add to dashboard Cite

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“…The activity of MMPs is primarily regulated by tissue metalloproteinase inhibitors-1,-2,-3,-4 (TIMPs) (Greene et al, 1996, and references therein). TIMP-2 exerts activity against several MMPs, although preferentially against MMP-2, by binding both its latent and activated forms (Goldberg et al, 1989;Howard et al, 1991). In contrast to all other secretory MMPs, MMP-2 proenzyme is resistant to soluble proteinases (Strongin et al, 1993) and is converted to the mature enzyme by mechanisms involving the recently identified membrane-type matrix metalloproteinases-1,-2,-3 (MT-MMPs) associated with the cell surface (Sato et al, 1994;Okada et al, 1995;Takino et al, 1995;Will and Hinzmann, 1995).…”

Section: Introductionmentioning

confidence: 99%

Matrix metalloproteinase-2 activation modulates glioma cell migration

Deryugina¹,

Bourdon²,

Luo³

et al. 1997

Journal of Cell Science

166

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Stable transfection of U251.3 glioma cells with cDNA encoding MT-MMP-1 resulted in increased cell surface expression of MT-MMP-1 and TIMP-2, constitutive activation of MMP-2 proenzyme and increased collagen degradation. In tumor spheroid outgrowth assays, cell migration of MT-MMP-1 transfectants relative to control was enhanced on collagen and decreased on vitronectin and fibronectin. These effects were reversed by TIMP-2 and were not associated with any substantial changes in cell adhesion. Binding of U251.3 cells to the C-terminal domain of MMP-2 was specifically inhibited by anti-(alpha)vss3 integrin blocking antibody indicating that MMP-2 interacts with (alpha)vss3 through the enzyme's C-terminal portion at or near the integrin's matrix adhesion sites. We propose that these mechanisms could govern directed matrix degradation in the tumor cells' microenvironment by sequestration of active MMP-2 on the cell surface. Our data suggest that activation of MMP-2 and its proteolytic activity localized to the cell surface could differentially modulate tumor cell migration in response to particular matrix proteins by altering both composition of the extracellular matrix and expression of adhesion receptors on the cell surface.

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“…TIMP-2 forma um complexo trimolecular na superfície celular com MT1-MMP e pró-MMP-2, o qual é responsável pela regulação dos níveis da enzima ativa (Butler et aL, 1998). TIMP-1 parece ser mais efetivo na regulação das colagenases, enquanto que TIMP-2 é mais efetivo com o grupo das gelatinases (Howard et aL, 1991).…”

Section: 4 Metaloproteinase De Matrizunclassified

Analise da proliferação celular e expressão de colageno e suas proteinas chaperones, citocinas e metaloproteinas de matriz e seus inibidores teciduais em fibroblastos gengivais de pacientes com fibromatose gengival herditaria

DellaColetta¹

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Preferential inhibition of 72- and 92-kDa gelatinases by tissue inhibitor of metalloproteinases-2

Cited by 193 publications

References 36 publications

MT1-matrix metalloproteinase directs arterial wall invasion and neointima formation by vascular smooth muscle cells

MT1-matrix metalloproteinase directs arterial wall invasion and neointima formation by vascular smooth muscle cells

Matrix metalloproteinase-2 activation modulates glioma cell migration

Analise da proliferação celular e expressão de colageno e suas proteinas chaperones, citocinas e metaloproteinas de matriz e seus inibidores teciduais em fibroblastos gengivais de pacientes com fibromatose gengival herditaria

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