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.

Download
Es wurde kein Volltext hochgeladen. Nur Publikationsnachweis!
Zeitschriftenaufsatz | Veröffentlicht | Englisch
Autor
; ;
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.
Erscheinungsjahr
Zeitschriftentitel
FEBS LETTERS
Band
397
Zeitschriftennummer
2-3
Seite
277-282
ISSN
PUB-ID

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. doi:10.1016/S0014-5793(96)01206-9
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.

42 Zitationen in Europe PMC

Daten bereitgestellt von Europe PubMed Central.

Targeting Matrix Metalloproteinases in Cancer: Bringing New Life to Old Ideas.
Cathcart J, Pulkoski-Gross A, Cao J., Genes Dis 2(`1), 2015
PMID: 26097889
The microtubule stabilizer patupilone counteracts ionizing radiation-induced matrix metalloproteinase activity and tumor cell invasion.
Furmanova-Hollenstein P, Broggini-Tenzer A, Eggel M, Millard AL, Pruschy M., Radiat Oncol 8(), 2013
PMID: 23631818
Peptide-based selective inhibitors of matrix metalloproteinase-mediated activities.
Ndinguri MW, Bhowmick M, Tokmina-Roszyk D, Robichaud TK, Fields GB., Molecules 17(12), 2012
PMID: 23201642
Inhibition of matrix metalloproteinase 14 (MMP-14)-mediated cancer cell migration.
Zarrabi K, Dufour A, Li J, Kuscu C, Pulkoski-Gross A, Zhi J, Hu Y, Sampson NS, Zucker S, Cao J., J Biol Chem 286(38), 2011
PMID: 21795678
Biochemical characterization of the cellular glycosylphosphatidylinositol-linked membrane type-6 matrix metalloproteinase.
Radichev IA, Remacle AG, Shiryaev SA, Purves AN, Johnson SL, Pellecchia M, Strongin AY., J Biol Chem 285(21), 2010
PMID: 20308072
Internal cleavages of the autoinhibitory prodomain are required for membrane type 1 matrix metalloproteinase activation, although furin cleavage alone generates inactive proteinase.
Golubkov VS, Cieplak P, Chekanov AV, Ratnikov BI, Aleshin AE, Golubkova NV, Postnova TI, Radichev IA, Rozanov DV, Zhu W, Motamedchaboki K, Strongin AY., J Biol Chem 285(36), 2010
PMID: 20605791
Loss of intercellular adhesion activates a transition from low- to high-grade human squamous cell carcinoma.
Margulis A, Zhang W, Alt-Holland A, Pawagi S, Prabhu P, Cao J, Zucker S, Pfeiffer L, Garfield J, Fusenig NE, Garlick JA., Int J Cancer 118(4), 2006
PMID: 16152579
Expression of matrix metalloproteinases in benign and malignant follicular thyroid lesions.
Cho Mar K, Eimoto T, Tateyama H, Arai Y, Fujiyoshi Y, Hamaguchi M., Histopathology 48(3), 2006
PMID: 16430475
Catalytic- and ecto-domains of membrane type 1-matrix metalloproteinase have similar inhibition profiles but distinct endopeptidase activities.
Hurst DR, Schwartz MA, Ghaffari MA, Jin Y, Tschesche H, Fields GB, Sang QX., Biochem J 377(pt 3), 2004
PMID: 14533979
Characterization of expression of matrix metalloproteinases and tissue inhibitors of metalloproteinases in prostate cancer cell lines.
Daja MM, Niu X, Zhao Z, Brown JM, Russell PJ., Prostate Cancer Prostatic Dis 6(1), 2003
PMID: 12664060
Design, synthesis, and characterization of potent, slow-binding inhibitors that are selective for gelatinases.
Bernardo MM, Brown S, Li ZH, Fridman R, Mobashery S., J Biol Chem 277(13), 2002
PMID: 11790786
mRNA expression of matrix metalloproteases and their inhibitors differs in subtypes of renal cell carcinomas.
Hagemann T, Gunawan B, Schulz M, Füzesi L, Binder C., Eur J Cancer 37(15), 2001
PMID: 11576837
Secretion of gelatinases and activation of gelatinase A (MMP-2) by human rheumatoid synovial fibroblasts.
Smolian H, Aurer A, Sittinger M, Zacher J, Bernimoulin JP, Burmester GR, Kolkenbrock H., Biol Chem 382(10), 2001
PMID: 11727833
Activation of progelatinase B by membranes of human polymorphonuclear granulocytes.
Kolkenbrock H, Zimmermann J, Burmester GR, Ulbrich N., Biol Chem 381(1), 2000
PMID: 10722050
Production of active mammalian and viral proteases in bacterial expression systems.
Babé LM, Linnevers CJ, Schmidt BF., Biotechnol Genet Eng Rev 17(), 2000
PMID: 11255667
Type IV collagen and its degradation in paralyzed human muscle: effect of functional electrical stimulation.
Koskinen SO, Kjaer M, Mohr T, Sørensen FB, Suuronen T, Takala TE., Muscle Nerve 23(4), 2000
PMID: 10716770
Expression and purification of soluble and inactive mutant forms of membrane type 1 matrix metalloproteinase.
Valtanen H, Lehti K, Lohi J, Keski-Oja J., Protein Expr Purif 19(1), 2000
PMID: 10833392
Solitary lung tumors and their spontaneous metastasis in athymic nude mice orthotopically implanted with human non-small cell lung cancer.
Yamaura T, Murakami K, Doki Y, Sugiyama S, Misaki T, Yamada Y, Saiki I., Neoplasia 2(4), 2000
PMID: 11005566
Expression of human membrane type 1 matrix metalloproteinase in Pichia pastoris.
Roderfeld M, Büttner FH, Bartnik E, Tschesche H., Protein Expr Purif 19(3), 2000
PMID: 10910727
Increased expression of membrane type 1 matrix metalloproteinase and matrix metalloproteinase-2 with tumor dedifferentiation in hepatocellular carcinomas.
Ogata R, Torimura T, Kin M, Ueno T, Tateishi Y, Kuromatsu R, Shimauchi Y, Sakamoto M, Tamaki S, Sata M, Tanikawa K., Hum Pathol 30(4), 1999
PMID: 10208467
Matrix metalloproteinases and tissue inhibitors of metalloproteinases in joint fluid of the patients with loose artificial hip joints.
Takei I, Takagi M, Santavirta S, Ida H, Hamasaki M, Ishii M, Fukushima S, Ogino T, Konttinen YT., J Biomed Mater Res 45(3), 1999
PMID: 10397973
MMP inhibition and downregulation by bisphosphonates.
Teronen O, Heikkilä P, Konttinen YT, Laitinen M, Salo T, Hanemaaijer R, Teronen A, Maisi P, Sorsa T., Ann N Y Acad Sci 878(), 1999
PMID: 10415748
Increased secretion of basement membrane-degrading metalloproteinases in pig saphenous vein into carotid artery interposition grafts.
Southgate KM, Mehta D, Izzat MB, Newby AC, Angelini GD., Arterioscler Thromb Vasc Biol 19(7), 1999
PMID: 10397681
Biochemical characterization of the catalytic domain of membrane-type 4 matrix metalloproteinase.
Kolkenbrock H, Essers L, Ulbrich N, Will H., Biol Chem 380(9), 1999
PMID: 10543448
TIMP-2 promotes activation of progelatinase A by membrane-type 1 matrix metalloproteinase immobilized on agarose beads.
Kinoshita T, Sato H, Okada A, Ohuchi E, Imai K, Okada Y, Seiki M., J Biol Chem 273(26), 1998
PMID: 9632662
Activation of progelatinase A and progelatinase A/TIMP-2 complex by membrane type 2-matrix metalloproteinase.
Kolkenbrock H, Hecker-Kia A, Orgel D, Ulbrich N, Will H., Biol Chem 378(2), 1997
PMID: 9088534
Membrane type-1 matrix metalloproteinase in human ocular tissues.
Smine A, Plantner JJ., Curr Eye Res 16(9), 1997
PMID: 9288454

32 References

Daten bereitgestellt von Europe PubMed Central.

Matrix metalloproteinases: a review.
Birkedal-Hansen H, Moore WG, Bodden MK, Windsor LJ, Birkedal-Hansen B, DeCarlo A, Engler JA., Crit. Rev. Oral Biol. Med. 4(2), 1993
PMID: 8435466
Tumor cell interactions with the extracellular matrix during invasion and metastasis.
Stetler-Stevenson WG, Aznavoorian S, Liotta LA., Annu. Rev. Cell Biol. 9(), 1993
PMID: 8280471
Proteolytic remodeling of extracellular matrix.
Birkedal-Hansen H., Curr. Opin. Cell Biol. 7(5), 1995
PMID: 8573349

AUTHOR UNKNOWN, 0
The matrix-degrading metalloproteinases.
Matrisian LM., Bioessays 14(7), 1992
PMID: 1445287
Nature of the collagenous protein in a tumor basement membrane.
Timpl R, Martin GR, Bruckner P, Wick G, Wiedemann H., Eur. J. Biochem. 84(1), 1978
PMID: 648517

AUTHOR UNKNOWN, 0
Substrate specificities and activation mechanisms of matrix metalloproteinases.
Nagase H, Ogata Y, Suzuki K, Enghild JJ, Salvesen G., Biochem. Soc. Trans. 19(3), 1991
PMID: 1783204
Matrix metalloproteinase 2 from human rheumatoid synovial fibroblasts. Purification and activation of the precursor and enzymic properties.
Okada Y, Morodomi T, Enghild JJ, Suzuki K, Yasui A, Nakanishi I, Salvesen G, Nagase H., Eur. J. Biochem. 194(3), 1990
PMID: 2269296
Plasma membrane-dependent activation of the 72-kDa type IV collagenase is prevented by complex formation with TIMP-2.
Strongin AY, Marmer BL, Grant GA, Goldberg GI., J. Biol. Chem. 268(19), 1993
PMID: 8314771
A matrix metalloproteinase expressed on the surface of invasive tumour cells.
Sato H, Takino T, Okada Y, Cao J, Shinagawa A, Yamamoto E, Seiki M., Nature 370(6484), 1994
PMID: 8015608
Use of T7 RNA polymerase to direct expression of cloned genes.
Studier FW, Rosenberg AH, Dunn JJ, Dubendorff JW., Meth. Enzymol. 185(), 1990
PMID: 2199796
Detergent-activation of latent collagenase and resolution of its component molecules.
Birkedal-Hansen H, Taylor RE., Biochem. Biophys. Res. Commun. 107(4), 1982
PMID: 6291522
The complex between a tissue inhibitor of metalloproteinases (TIMP-2) and 72-kDa progelatinase is a metalloproteinase inhibitor.
Kolkenbrock H, Orgel D, Hecker-Kia A, Noack W, Ulbrich N., Eur. J. Biochem. 198(3), 1991
PMID: 1646720

AUTHOR UNKNOWN, 0
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

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
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
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
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
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

AUTHOR UNKNOWN, 0

Export

Markieren/ Markierung löschen
Markierte Publikationen

Open Data PUB

Web of Science

Dieser Datensatz im Web of Science®

Quellen

PMID: 8955363
PubMed | Europe PMC

Suchen in

Google Scholar