The matrix metalloproteinases and their natural inhibitors: prospects for treating degenerative tissue diseases

Docherty, Andrew; O’Connell, James P.; Crabbe, Thomas; Angal, Sarojani; Murphy, Gillian

doi:10.1016/0167-7799(92)90214-g

Cited by 192 publications

(125 citation statements)

References 61 publications

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“…In spite of improvements in surgical treatment and chemotherapy, the prognosis is still poor, owing to local recurrence or metastasis [1][2][3]. Degradation of the extracellular matrix during tumor invasion and metastasis is thought to result from a combined action of several proteolytic enzyme systems, including the collagenases and other matrix metalloproteinases (MMPs) [4,5] and serine proteases, such as plasmin generated by the urokinase pathway of plasminogen activation [6].…”

Section: Introductionmentioning

confidence: 99%

Expression of collagenase-3 (matrix metalloproteinase-13) in human gastric cancer

et al. 2003

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tive form of MMP-13 or one of its intermediate forms. Also, zymographic analysis of the tumor specimens revealed strong gelatinolytic bands of MMP-13 and MMP-2, whereas these bands in normal mucosa were weak. There was no significant relationship between MMP-13 mRNA expression and histologic type, lymph node metastasis, wall invasion, or distant metastasis. However, patients with MMP-13 mRNA-positive tumors had a poorer prognosis than those with MMP-13-mRNA-negative cancer. Furthermore, patients with simultaneous expression of MMP-13 and MT1-MMP mRNA showed the poorest prognosis, as compared with those having tumors expressing either MMP-13 or MT1-MMP, or neither MMP-13 nor MT1-MMP mRNA. Conclusion. These findings suggest that MMP-13 expression may contribute to the progression of gastric cancer, and its coordinate overexpression with MT1-MMP and/or MMP-2 may have a cooperative effect in the progression of gastric cancer.

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Section: Introductionmentioning

confidence: 99%

Expression of collagenase-3 (matrix metalloproteinase-13) in human gastric cancer

et al. 2003

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“…Most MMPs are secreted in a latent form (pro-MMP) and activated by serine proteinases or some activated MMPs. The activities of activated MMPs are regulated by natural inhibitors called tissue inhibitors of metalloproteinases (TIMPs) (1)(2)(3).…”

mentioning

confidence: 99%

Expression of Three Membrane-type Matrix Metalloproteinases (MT-MMPs) in Rat Vascular Smooth Muscle Cells and Characterization of MT3-MMPs with and without Transmembrane Domain

Shofuda

Yasumitsu

Nishihashi

et al. 1997

Journal of Biological Chemistry

111

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“…MMP-2 expression has been repeatedly correlated to invasive and metastatic aggressiveness of tumour cells, and TIMP-2 inhibits matrix invasion by transformed cells [6] and endothelial cell proliferation [7] in vitro, as well as metastasis in vivo [8]. Nevertheless, deeper comprehension of proteinase-inhibitor interactions is still crucial for designing and checking pharmacological strategies for controlling pathological matrix proteolysis.…”

Section: Introductionmentioning

confidence: 99%

Synthesis and refolding of human TIMP‐2 from E. coli, with specific activity for MMP‐2

Negro¹,

Onisto²,

Masiero³

et al. 1995

FEBS Letters

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Tissue inhibitors of metalloproteinase (TIMPs) are inhibitory counterparts of collagenases, containing 12 cysteine residues paired to six internal disulphide bridges. TIMP-2, an inhibitory protein of 72 kDa gelatinase/type IV collagenase (MMP-2), was expressed in Escherichia coli as a fusion protein with a 34 amino acid NH2-1inked tail containing six consecutive histidine residues. The protein was purified in a single-step using an ion metal affinity column (IMAC) in denaturing conditions. The immobilized fusion TIMP-2 protein was refolded at a high concentration in the column, producing about 5 mg of protein per litre of bacterial cells. It shows specific binding and inhibitory activity against MMP-2, but has no effect against 92 and 45 kDa gelatinases.

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The matrix metalloproteinases and their natural inhibitors: prospects for treating degenerative tissue diseases

Cited by 192 publications

References 61 publications

Expression of collagenase-3 (matrix metalloproteinase-13) in human gastric cancer

Expression of collagenase-3 (matrix metalloproteinase-13) in human gastric cancer

Expression of Three Membrane-type Matrix Metalloproteinases (MT-MMPs) in Rat Vascular Smooth Muscle Cells and Characterization of MT3-MMPs with and without Transmembrane Domain

Synthesis and refolding of human TIMP‐2 from E. coli, with specific activity for MMP‐2

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