MMP-TIMP interaction depends on residue 2 in TIMP-4

Stratmann B, Farr M, Tschesche H (2001)
FEBS LETTERS 507(3): 285-287.

Zeitschriftenaufsatz | Veröffentlicht | Englisch
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Stratmann, B; Farr, M; Tschesche, HaraldUniBi
Abstract / Bemerkung
Extracellular matrix remodeling and degradation are of great importance in both physiological and pathological: situations. Matrix metalloproteinases (MMPs) and their, natural occurring inhibitors - tissue inhibitors of metalloproteinases (TIMPs) - are involved in matrix turnover. Among the TIMP's there is only little specificity for inhibiting individual MMPs. In this report we describe the mutational analysis of the interaction of human TIMP-4 with several MMPs. The effects of different substitutions of residue 2 (Ser(2)) in the inhibitory domain of TIMP-4 were determined by kinetic measurements. Size, charge and polarity of residue 2 in the TIMP structure are key factors in MMP inhibition. (C) 2001 Published by Elsevier Science B.V. on behalf of the Federation of European Biochemical Societies.
metalloproteinase-tissue inhibitor of metalloproteinase interaction; matrix metalloproteinase; tissue inhibitor of metalloproteinase; matrix; tissue inhibitor of metalloproteinase specifity
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Stratmann B, Farr M, Tschesche H. MMP-TIMP interaction depends on residue 2 in TIMP-4. FEBS LETTERS. 2001;507(3):285-287.
Stratmann, B., Farr, M., & Tschesche, H. (2001). MMP-TIMP interaction depends on residue 2 in TIMP-4. FEBS LETTERS, 507(3), 285-287.
Stratmann, B., Farr, M., and Tschesche, H. (2001). MMP-TIMP interaction depends on residue 2 in TIMP-4. FEBS LETTERS 507, 285-287.
Stratmann, B., Farr, M., & Tschesche, H., 2001. MMP-TIMP interaction depends on residue 2 in TIMP-4. FEBS LETTERS, 507(3), p 285-287.
B. Stratmann, M. Farr, and H. Tschesche, “MMP-TIMP interaction depends on residue 2 in TIMP-4”, FEBS LETTERS, vol. 507, 2001, pp. 285-287.
Stratmann, B., Farr, M., Tschesche, H.: MMP-TIMP interaction depends on residue 2 in TIMP-4. FEBS LETTERS. 507, 285-287 (2001).
Stratmann, B, Farr, M, and Tschesche, Harald. “MMP-TIMP interaction depends on residue 2 in TIMP-4”. FEBS LETTERS 507.3 (2001): 285-287.

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PMID: 21314431
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PMID: 19190762
Tissue inhibitor of metalloproteinases-4. The road less traveled.
Melendez-Zajgla J, Del Pozo L, Ceballos G, Maldonado V., Mol Cancer 7(), 2008
PMID: 19025595
Environmental arsenic exposure and sputum metalloproteinase concentrations.
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Collagenases in cancer.
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PMID: 15781314

26 References

Daten bereitgestellt von Europe PubMed Central.

Matrix metalloproteinases.
Nagase H, Woessner JF Jr., J. Biol. Chem. 274(31), 1999
PMID: 10419448
Mechanism of cell surface activation of 72-kDa type IV collagenase. Isolation of the activated form of the membrane metalloprotease.
Strongin AY, Collier I, Bannikov G, Marmer BL, Grant GA, Goldberg GI., J. Biol. Chem. 270(10), 1995
PMID: 7890645
Processing of a precursor of 72-kilodalton type IV collagenase/gelatinase A by a recombinant membrane-type 1 matrix metalloproteinase.
Kinoshita T, Sato H, Takino T, Itoh M, Akizawa T, Seiki M., Cancer Res. 56(11), 1996
PMID: 8653693
Molecular cloning and characterization of human tissue inhibitor of metalloproteinase 4.
Greene J, Wang M, Liu YE, Raymond LA, Rosen C, Shi YE., J. Biol. Chem. 271(48), 1996
PMID: 8939999
Tissue inhibitors of metalloproteinases: structure, regulation and biological functions.
Gomez DE, Alonso DF, Yoshiji H, Thorgeirsson UP., Eur. J. Cell Biol. 74(2), 1997
PMID: 9352216
Tissue inhibitors of metalloproteinases: evolution, structure and function.
Brew K, Dinakarpandian D, Nagase H., Biochim. Biophys. Acta 1477(1-2), 2000
PMID: 10708863
Inhibition of tumor growth and metastasis of human breast cancer cells transfected with tissue inhibitor of metalloproteinase 4.
Wang M, Liu YE, Greene J, Sheng S, Fuchs A, Rosen EM, Shi YE., Oncogene 14(23), 1997
PMID: 9190892
Preparation and characterization of recombinant tissue inhibitor of metalloproteinase 4 (TIMP-4).
Liu YE, Wang M, Greene J, Su J, Ullrich S, Li H, Sheng S, Alexander P, Sang QA, Shi YE., J. Biol. Chem. 272(33), 1997
PMID: 9252358
Crystal structure of the complex formed by the membrane type 1-matrix metalloproteinase with the tissue inhibitor of metalloproteinases-2, the soluble progelatinase A receptor.
Fernandez-Catalan C, Bode W, Huber R, Turk D, Calvete JJ, Lichte A, Tschesche H, Maskos K., EMBO J. 17(17), 1998
PMID: 9724659
Mechanism of inhibition of the human matrix metalloproteinase stromelysin-1 by TIMP-1.
Gomis-Ruth FX, Maskos K, Betz M, Bergner A, Huber R, Suzuki K, Yoshida N, Nagase H, Brew K, Bourenkov GP, Bartunik H, Bode W., Nature 389(6646), 1997
PMID: 9288970
Structure of full-length porcine synovial collagenase reveals a C-terminal domain containing a calcium-linked, four-bladed beta-propeller.
Li J, Brick P, O'Hare MC, Skarzynski T, Lloyd LF, Curry VA, Clark IM, Bigg HF, Hazleman BL, Cawston TE., Structure 3(6), 1995
PMID: 8590015
The N-terminal domain of tissue inhibitor of metalloproteinases retains metalloproteinase inhibitory activity.
Murphy G, Houbrechts A, Cockett MI, Williamson RA, O'Shea M, Docherty AJ., Biochemistry 30(33), 1991
PMID: 1868085
The specificity of TIMP-2 for matrix metalloproteinases can be modified by single amino acid mutations.
Butler GS, Hutton M, Wattam BA, Williamson RA, Knauper V, Willenbrock F, Murphy G., J. Biol. Chem. 274(29), 1999
PMID: 10400663

Latent collagenase and gelatinase from human neutrophils and their activation.
Tschesche H, Knauper V, Kramer S, Michaelis J, Oberhoff R, Reinke H., Matrix Suppl 1(), 1992
PMID: 1480034
Preparation of active recombinant TIMP-1 from Escherichia coli inclusion bodies and complex formation with the recombinant catalytic domain of PMNL-collagenase.
Kleine T, Bartsch S, Blaser J, Schnierer S, Triebel S, Valentin M, Gote T, Tschesche H., Biochemistry 32(51), 1993
PMID: 8260495

Copeland, Bioorg. Med. Chem. Lett. 17(), 1995
Insights into MMP-TIMP interactions.
Bode W, Fernandez-Catalan C, Grams F, Gomis-Ruth FX, Nagase H, Tschesche H, Maskos K., Ann. N. Y. Acad. Sci. 878(), 1999
PMID: 10415721
Structural properties of matrix metalloproteinases.
Bode W, Fernandez-Catalan C, Tschesche H, Grams F, Nagase H, Maskos K., Cell. Mol. Life Sci. 55(4), 1999
PMID: 10357232


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