Tissue inhibitor of metalloproteinases-2 inhibits the activation of 72 kDa progelatinase by fibroblast membranes

Ward, Robin V.; Atkinson, Susan J.; Slocombe, Patrick M.; Docherty, Andrew; Reynolds, John J.; Murphy, Gillian

doi:10.1016/0167-4838(91)90132-j

Cited by 193 publications

(137 citation statements)

References 14 publications

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“…We speculate that binding of progelatinase A to TIMP-4 could be involved in the formation of an alternative trimolecular complex, perhaps preferentially with one of the other MT-MMPs, giving rise to an alternative activation pathway which is functional only in tissues which express TIMP-4. Formation of the MT-MMP-TIMP-2-progelatinase A trimolecular complex appears to be sequential, such that preformed TIMP-2-progelatinase A complex will not bind (43) and is therefore resistant to activation (36,42,43). Hence, an alternative possibility is that complex formation between progelatinase A and TIMP-4 prevents the enzyme from association with membrane bound TIMP-2 and therefore blocks activation.…”

Section: Discussionmentioning

confidence: 98%

Specific, High Affinity Binding of Tissue Inhibitor of Metalloproteinases-4 (TIMP-4) to the COOH-terminal Hemopexin-like Domain of Human Gelatinase A

Bigg¹,

Shi²,

Liu³

et al. 1997

Journal of Biological Chemistry

156

106

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The binding properties of the newly described tissue inhibitor of metalloproteinases-4 (TIMP-4) to progelatinase A and to the COOH-terminal hemopexin-like domain (C domain) of the enzyme were examined. We present evidence for the first time of a specific, high affinity interaction between TIMP-4 and the C domain of human gelatinase A and show that TIMP-4 binds both progelatinase A and the C domain in a similar manner to that of TIMP-2. Saturable binding of recombinant C domain to TIMP-4 and to TIMP-2 but not to TIMP-1 was demonstrated using a microwell protein binding assay.

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Section: Discussionmentioning

confidence: 98%

Specific, High Affinity Binding of Tissue Inhibitor of Metalloproteinases-4 (TIMP-4) to the COOH-terminal Hemopexin-like Domain of Human Gelatinase A

Bigg¹,

Shi²,

Liu³

et al. 1997

Journal of Biological Chemistry

156

106

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show abstract

“…22 In contrast, TIMP-2 binds selectively to pro-MMP-2, an interaction that can serve to present the enzyme for activation by membrane type MMP-1 (MT1-MMP). [22][23][24][25] Higher concentrations of TIMP-2, but not TIMP-1, inhibit MT1-MMP. 26,27 In a recent study of adenovirus-mediated TIMP gene transfer into isolated SMC, 19 TIMP-2, but not TIMP-1, was shown to inhibit proliferation, an effect not mediated by inhibition of MMPs.…”

Section: Correspondence: Ah Bakermentioning

confidence: 99%

Gene transfer of tissue inhibitor of metalloproteinase-2 inhibits metalloproteinase activity and neointima formation in human saphenous veins

et al. 1998

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Metalloproteinases (MMPs) are implicated in neointima for-21.8 ± 2.9 ng/mg wet weight/day (P Ͻ 0.05, n = 3). In situ mation and hence vein graft failure. Gene transfer to elevzymography revealed a marked inhibition of gelatinolytic ate local levels of tissue inhibitor of metalloproteinases activity by TIMP-2 gene transfer throughout the vein seg-(TIMPs) is therefore a potential treatment. In this study, we ments. Neointima formation and neointimal cell numbers have used lumenal application of a replication-defective were reduced 79% and 71%, respectively (P Ͻ 0.05; recombinant adenovirus to overexpress TIMP-2 and n = 8). TIMP-2 overexpression had no effect on smooth observe the effects on neointimal thickening in a well muscle cell proliferation, secretion of pro-MMP-2 or -9 and characterised human saphenous vein organ culture model.did not inhibit the processing of pro-MMP-2 to its active Increased TIMP-2 expression was localised to lumenal form. Our data indicate that TIMP-2 overexpression surface cells but nevertheless increased total functional reduces neointimal thickening, primarily by inhibiting MMP TIMP-2 secretion after 14 days culture from 4.0 ± 2.0 to activity and hence smooth muscle cell migration.

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“…MMP-2 activation is mediated by a membrane-associated mechanism that can be induced in vitro by tumor necrosis factor-α, concanavalin A (ConA), cytochalasin D, and phorbol esters such as tetradecanoylphorbol 13-ace-tate (TPA) [13][14][15][16][17][18][19][20][21]. Sato and co-workers have identified MT1-MMP (membrane type 1 MMP or MMP-14): a MMP possessing a hydrophobic C-terminal transmembrane domain, which is considered as a physiological MMP-2 activator [22][23][24][25].…”

Section: Introductionmentioning

confidence: 99%

Type IV Collagen Induces Matrix Metalloproteinase 2 Activation in HT1080 Fibrosarcoma Cells

Maquoi

Frankenne

Noël

et al. 2000

Experimental Cell Research

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Matrix metalloproteinase 2 (MMP-2) activation has been described as a "master switch" which triggers tumor spread and metastatic progression. We show here that type IV collagen, a major component of basement membranes, promotes MMP-2 activation by HT1080 cells. When plated on plastic, HT1080 cells constitutively processed the 66-kDa pro-MMP-2 into a 62-kDa intermediate activated form, most probably through a membrane type (MT) 1 MMP-dependent mechanism. In the presence of type IV collagen, part of this intermediate form was further processed to fully activated 59-kDa MMP-2. This activation was prevented by tissue inhibitor of MMP (TIMP)-2 and a broad-spectrum hydroxamic acid-based synthetic MMP inhibitor (GI129471). Type IV collagen-mediated pro-MMP-2 activation did not involve either a transcriptional modulation of MMP-2, MT1-MMP, or TIMP-2 expression nor any alteration of MT1-MMP protein synthesis or processing. An inverse relationship between MMP-2 activation and the concentration of secreted TIMP-2 was observed. This is consistent with our previous report that TIMP-2 degradation is probably linked to the MT1-MMP-dependent MMP-2 activation mechanism. Because invasive tumor cells must breach basement membranes at different steps of the metastatic dissemination, the ability of HT1080 cells to activate pro-MMP-2 in the presence of type IV collagen might represent a key regulatory mechanism for the acquisition of an invasive potential.

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Tissue inhibitor of metalloproteinases-2 inhibits the activation of 72 kDa progelatinase by fibroblast membranes

Cited by 193 publications

References 14 publications

Specific, High Affinity Binding of Tissue Inhibitor of Metalloproteinases-4 (TIMP-4) to the COOH-terminal Hemopexin-like Domain of Human Gelatinase A

Specific, High Affinity Binding of Tissue Inhibitor of Metalloproteinases-4 (TIMP-4) to the COOH-terminal Hemopexin-like Domain of Human Gelatinase A

Gene transfer of tissue inhibitor of metalloproteinase-2 inhibits metalloproteinase activity and neointima formation in human saphenous veins

Type IV Collagen Induces Matrix Metalloproteinase 2 Activation in HT1080 Fibrosarcoma Cells

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