The recombinant catalytic domain of membrane-type matrix metalloproteinase-1 (MT1-MMP) induces activation of progelatinase A and progelatinase A complexed with TIMP-2
Lichte A, Kolkenbrock H, Tschesche H (1996)
FEBS LETTERS 397(2-3): 277-282.
Zeitschriftenaufsatz
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Autor*in
Lichte, A;
Kolkenbrock, H;
Tschesche, HaraldUniBi
Einrichtung
Abstract / Bemerkung
A truncated form of the membrane-type matrix metalloproteinase-1 [(Ala(21)-Ile(318))proMT1-MMP] lacking the hemopexin-like and trans-membrane domain was produced in E. coli. We demonstrate that the recombinant proenzyme was autoproteolytically processed to a fully active catalytic domain with N-terminal Ile(114). The catalytic domain of MT1-MMP initiated the activation of progelatinase A and progelatinase A complexed with tissue inhibitor of metalloproteinases-2 (TIMP-2). As a typical soluble metalloproteinase it was able to cleave physiologic as well as synthetic substrates. Our kinetic data demonstrate that TIMP-2 is a potent inhibitor for the recombinant enzyme.
Stichworte
membrane-type matrix metalloproteinase;
matrix metalloproteinase;
gelatinase A;
type IV collagenase activation;
TIMP-2
Erscheinungsjahr
1996
Zeitschriftentitel
FEBS LETTERS
Band
397
Ausgabe
2-3
Seite(n)
277-282
ISSN
0014-5793
Page URI
https://pub.uni-bielefeld.de/record/1638047
Zitieren
Lichte A, Kolkenbrock H, Tschesche H. The recombinant catalytic domain of membrane-type matrix metalloproteinase-1 (MT1-MMP) induces activation of progelatinase A and progelatinase A complexed with TIMP-2. FEBS LETTERS. 1996;397(2-3):277-282.
Lichte, A., Kolkenbrock, H., & Tschesche, H. (1996). The recombinant catalytic domain of membrane-type matrix metalloproteinase-1 (MT1-MMP) induces activation of progelatinase A and progelatinase A complexed with TIMP-2. FEBS LETTERS, 397(2-3), 277-282. https://doi.org/10.1016/S0014-5793(96)01206-9
Lichte, A, Kolkenbrock, H, and Tschesche, Harald. 1996. “The recombinant catalytic domain of membrane-type matrix metalloproteinase-1 (MT1-MMP) induces activation of progelatinase A and progelatinase A complexed with TIMP-2”. FEBS LETTERS 397 (2-3): 277-282.
Lichte, A., Kolkenbrock, H., and Tschesche, H. (1996). The recombinant catalytic domain of membrane-type matrix metalloproteinase-1 (MT1-MMP) induces activation of progelatinase A and progelatinase A complexed with TIMP-2. FEBS LETTERS 397, 277-282.
Lichte, A., Kolkenbrock, H., & Tschesche, H., 1996. The recombinant catalytic domain of membrane-type matrix metalloproteinase-1 (MT1-MMP) induces activation of progelatinase A and progelatinase A complexed with TIMP-2. FEBS LETTERS, 397(2-3), p 277-282.
A. Lichte, H. Kolkenbrock, and H. Tschesche, “The recombinant catalytic domain of membrane-type matrix metalloproteinase-1 (MT1-MMP) induces activation of progelatinase A and progelatinase A complexed with TIMP-2”, FEBS LETTERS, vol. 397, 1996, pp. 277-282.
Lichte, A., Kolkenbrock, H., Tschesche, H.: The recombinant catalytic domain of membrane-type matrix metalloproteinase-1 (MT1-MMP) induces activation of progelatinase A and progelatinase A complexed with TIMP-2. FEBS LETTERS. 397, 277-282 (1996).
Lichte, A, Kolkenbrock, H, and Tschesche, Harald. “The recombinant catalytic domain of membrane-type matrix metalloproteinase-1 (MT1-MMP) induces activation of progelatinase A and progelatinase A complexed with TIMP-2”. FEBS LETTERS 397.2-3 (1996): 277-282.
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Strongin AY, Collier I, Bannikov G, Marmer BL, Grant GA, Goldberg GI., J. Biol. Chem. 270(10), 1995
PMID: 7890645
Strongin AY, Collier I, Bannikov G, Marmer BL, Grant GA, Goldberg GI., J. Biol. Chem. 270(10), 1995
PMID: 7890645
AUTHOR UNKNOWN, 0
Isolation of latent 31-kDa C-truncated stromelysin and 21-kDa stromelysin from rabbit synovial fibroblasts: an alternative activation pathway for stromelysin.
Kolkenbrock H, Hecker-Kia A, Orgel D, Huser H, Schroder W, Ulbrich N., Biol. Chem. Hoppe-Seyler 375(4), 1994
PMID: 8060532
Kolkenbrock H, Hecker-Kia A, Orgel D, Huser H, Schroder W, Ulbrich N., Biol. Chem. Hoppe-Seyler 375(4), 1994
PMID: 8060532
Molecular cloning, chromosomal localization, and bacterial expression of a murine macrophage metalloelastase.
Shapiro SD, Griffin GL, Gilbert DJ, Jenkins NA, Copeland NG, Welgus HG, Senior RM, Ley TJ., J. Biol. Chem. 267(7), 1992
PMID: 1537850
Shapiro SD, Griffin GL, Gilbert DJ, Jenkins NA, Copeland NG, Welgus HG, Senior RM, Ley TJ., J. Biol. Chem. 267(7), 1992
PMID: 1537850
Structural implications for the role of the N terminus in the 'superactivation' of collagenases. A crystallographic study.
Reinemer P, Grams F, Huber R, Kleine T, Schnierer S, Piper M, Tschesche H, Bode W., FEBS Lett. 338(2), 1994
PMID: 8307185
Reinemer P, Grams F, Huber R, Kleine T, Schnierer S, Piper M, Tschesche H, Bode W., FEBS Lett. 338(2), 1994
PMID: 8307185
Mechanisms of activation of tissue procollagenase by matrix metalloproteinase 3 (stromelysin).
Suzuki K, Enghild JJ, Morodomi T, Salvesen G, Nagase H., Biochemistry 29(44), 1990
PMID: 2176865
Suzuki K, Enghild JJ, Morodomi T, Salvesen G, Nagase H., Biochemistry 29(44), 1990
PMID: 2176865
Direct activation of human neutrophil procollagenase by recombinant stromelysin.
Knauper V, Wilhelm SM, Seperack PK, DeClerck YA, Langley KE, Osthues A, Tschesche H., Biochem. J. 295 ( Pt 2)(), 1993
PMID: 8240261
Knauper V, Wilhelm SM, Seperack PK, DeClerck YA, Langley KE, Osthues A, Tschesche H., Biochem. J. 295 ( Pt 2)(), 1993
PMID: 8240261
AUTHOR UNKNOWN, 0
The C-terminal domain of 72 kDa gelatinase A is not required for catalysis, but is essential for membrane activation and modulates interactions with tissue inhibitors of metalloproteinases.
Murphy G, Willenbrock F, Ward RV, Cockett MI, Eaton D, Docherty AJ., Biochem. J. 283 ( Pt 3)(), 1992
PMID: 1317162
Murphy G, Willenbrock F, Ward RV, Cockett MI, Eaton D, Docherty AJ., Biochem. J. 283 ( Pt 3)(), 1992
PMID: 1317162
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