Membrane type 1 matrix metalloproteinase (MT1-MMP) cleaves the recombinant aggrecan substrate rAgg1(mut) at the 'aggrecanase' and the MMP sites - Characterization of MT1-MMP catabolic activities on the interglobular domain of aggrecan
Buttner FH, Hughes CE, Margerie D, Lichte A, Tschesche H, Caterson B, Bartnik E (1998)
BIOCHEMICAL JOURNAL 333: 159-165.
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Autor*in
Buttner, FH;
Hughes, CE;
Margerie, D;
Lichte, A;
Tschesche, HaraldUniBi;
Caterson, B;
Bartnik, E
Einrichtung
Abstract / Bemerkung
The recent detection of membrane type 1 matrix metallo-proteinase (MT1-MMP) expression in human articular cartilage [Buttner, Chubinskaya, Margerie, Huch, Flechtenmacher, Cole, Kuettner, and Bartnik (1997) Arthritis Rheum. 40, 704-709] prompted our investigation of MT1-MMP's catabolic activity within the interglobular domain of aggrecan. For these studies we used rAAg1(mut), a mutated form of the recombinant fusion protein (rAgg1) that has been used as a substrate to monitor 'aggrecanase' catabolism in vitro [Hughes, Buttner, Eidenmuller, Caterson and Bartnik (1997) J. Biol. Chem. 272, 20269-20274]. The rAgg1 was mutated (G(332) to A) to avoid the generation of a splice variant seen with the original genetic construct, which gave rise to heterogeneous glycoprotein products. This mutation yielded a homogeneous recombinant product. Studies in vitro with retinoic acid-stimulated rat chondrosarcoma cells indicated that the rAgg1(mut) substrate was cleaved at the 'aggrecanase' site equivalent to Glu(373)-Ala(374) (human aggrecan sequence enumeration) in its interglobular domain sequence segment. The differential catabolic activities of the recombinant catalytic domain (ed) of MT1-MMP and matrix metalloproteinases (MMPs) 3 and 8 were then compared by using this rAgg1(mut) as substrate. Coomassie staining of rAAg1(mut) catabolites separated by SDS/PAGE showed similar patterns of degradation with all three recombinant enzymes. However, comparative immunodetection analysis, with neoepitope antibodies BC-3 (anti-ARGS...) and BC-14 (anti-FFGV...) to distinguish between 'aggrecanase' and MMP-generated catabolites, indicated that the catalytic domain of MT1-MMP exhibited strong 'aggrecanase' activity, cdMMP-8 weak activity and cdMMP-3 no activity. In contrast, cdMMP-3 and cdMMP-8 led to strongly BC-14-reactive catabolic fragments, whereas cdMT1-MMP resulted in weak BC-14 reactivity. N-terminal sequence analyses of the catabolites confirmed these results and also identified other potential minor cleavage sites within the interglobular domain of aggrecan. These results indicate that MT1-MMP is yet another candidate for 'aggrecanase' activity in vivo.
Erscheinungsjahr
1998
Zeitschriftentitel
BIOCHEMICAL JOURNAL
Band
333
Seite(n)
159-165
ISSN
0264-6021
Page URI
https://pub.uni-bielefeld.de/record/1625197
Zitieren
Buttner FH, Hughes CE, Margerie D, et al. Membrane type 1 matrix metalloproteinase (MT1-MMP) cleaves the recombinant aggrecan substrate rAgg1(mut) at the 'aggrecanase' and the MMP sites - Characterization of MT1-MMP catabolic activities on the interglobular domain of aggrecan. BIOCHEMICAL JOURNAL. 1998;333:159-165.
Buttner, F. H., Hughes, C. E., Margerie, D., Lichte, A., Tschesche, H., Caterson, B., & Bartnik, E. (1998). Membrane type 1 matrix metalloproteinase (MT1-MMP) cleaves the recombinant aggrecan substrate rAgg1(mut) at the 'aggrecanase' and the MMP sites - Characterization of MT1-MMP catabolic activities on the interglobular domain of aggrecan. BIOCHEMICAL JOURNAL, 333, 159-165. https://doi.org/10.1042/bj3330159
Buttner, FH, Hughes, CE, Margerie, D, Lichte, A, Tschesche, Harald, Caterson, B, and Bartnik, E. 1998. “Membrane type 1 matrix metalloproteinase (MT1-MMP) cleaves the recombinant aggrecan substrate rAgg1(mut) at the 'aggrecanase' and the MMP sites - Characterization of MT1-MMP catabolic activities on the interglobular domain of aggrecan”. BIOCHEMICAL JOURNAL 333: 159-165.
Buttner, F. H., Hughes, C. E., Margerie, D., Lichte, A., Tschesche, H., Caterson, B., and Bartnik, E. (1998). Membrane type 1 matrix metalloproteinase (MT1-MMP) cleaves the recombinant aggrecan substrate rAgg1(mut) at the 'aggrecanase' and the MMP sites - Characterization of MT1-MMP catabolic activities on the interglobular domain of aggrecan. BIOCHEMICAL JOURNAL 333, 159-165.
Buttner, F.H., et al., 1998. Membrane type 1 matrix metalloproteinase (MT1-MMP) cleaves the recombinant aggrecan substrate rAgg1(mut) at the 'aggrecanase' and the MMP sites - Characterization of MT1-MMP catabolic activities on the interglobular domain of aggrecan. BIOCHEMICAL JOURNAL, 333, p 159-165.
F.H. Buttner, et al., “Membrane type 1 matrix metalloproteinase (MT1-MMP) cleaves the recombinant aggrecan substrate rAgg1(mut) at the 'aggrecanase' and the MMP sites - Characterization of MT1-MMP catabolic activities on the interglobular domain of aggrecan”, BIOCHEMICAL JOURNAL, vol. 333, 1998, pp. 159-165.
Buttner, F.H., Hughes, C.E., Margerie, D., Lichte, A., Tschesche, H., Caterson, B., Bartnik, E.: Membrane type 1 matrix metalloproteinase (MT1-MMP) cleaves the recombinant aggrecan substrate rAgg1(mut) at the 'aggrecanase' and the MMP sites - Characterization of MT1-MMP catabolic activities on the interglobular domain of aggrecan. BIOCHEMICAL JOURNAL. 333, 159-165 (1998).
Buttner, FH, Hughes, CE, Margerie, D, Lichte, A, Tschesche, Harald, Caterson, B, and Bartnik, E. “Membrane type 1 matrix metalloproteinase (MT1-MMP) cleaves the recombinant aggrecan substrate rAgg1(mut) at the 'aggrecanase' and the MMP sites - Characterization of MT1-MMP catabolic activities on the interglobular domain of aggrecan”. BIOCHEMICAL JOURNAL 333 (1998): 159-165.
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Lichte A, Kolkenbrock H, Tschesche H., FEBS Lett. 397(2-3), 1996
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Lichte A, Kolkenbrock H, Tschesche H., FEBS Lett. 397(2-3), 1996
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Arner EC, Decicco CP, Cherney R, Tortorella MD., J. Biol. Chem. 272(14), 1997
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Arner EC, Decicco CP, Cherney R, Tortorella MD., J. Biol. Chem. 272(14), 1997
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Expression of membrane type 1 matrix metalloproteinase in human articular cartilage.
Buttner FH, Chubinskaya S, Margerie D, Huch K, Flechtenmacher J, Cole AA, Kuettner KE, Bartnik E., Arthritis Rheum. 40(4), 1997
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Buttner FH, Chubinskaya S, Margerie D, Huch K, Flechtenmacher J, Cole AA, Kuettner KE, Bartnik E., Arthritis Rheum. 40(4), 1997
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Aggrecan degradation in human cartilage. Evidence for both matrix metalloproteinase and aggrecanase activity in normal, osteoarthritic, and rheumatoid joints.
Lark MW, Bayne EK, Flanagan J, Harper CF, Hoerrner LA, Hutchinson NI, Singer II, Donatelli SA, Weidner JR, Williams HR, Mumford RA, Lohmander LS., J. Clin. Invest. 100(1), 1997
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Expression of membrane-type 1 matrix metalloproteinase and activation of progelatinase A in human osteoarthritic cartilage.
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Imai K, Ohta S, Matsumoto T, Fujimoto N, Sato H, Seiki M, Okada Y., Am. J. Pathol. 151(1), 1997
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Utilization of a recombinant substrate rAgg1 to study the biochemical properties of aggrecanase in cell culture systems.
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Hughes CE, Buttner FH, Eidenmuller B, Caterson B, Bartnik E., J. Biol. Chem. 272(32), 1997
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The interglobular domain of cartilage aggrecan is cleaved by hemorrhagic metalloproteinase HT-d (atrolysin C) at the matrix metalloproteinase and aggrecanase sites.
Tortorella MD, Pratta MA, Fox JW, Arner EC., J. Biol. Chem. 273(10), 1998
PMID: 9488721
Tortorella MD, Pratta MA, Fox JW, Arner EC., J. Biol. Chem. 273(10), 1998
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Cleavage of structural proteins during the assembly of the head of bacteriophage T4.
Laemmli UK., Nature 227(5259), 1970
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Laemmli UK., Nature 227(5259), 1970
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Human skin fibroblast stromelysin: structure, glycosylation, substrate specificity, and differential expression in normal and tumorigenic cells.
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Wilhelm SM, Collier IE, Kronberger A, Eisen AZ, Marmer BL, Grant GA, Bauer EA, Goldberg GI., Proc. Natl. Acad. Sci. U.S.A. 84(19), 1987
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Prickett KS, Amberg DC, Hopp TP., BioTechniques 7(6), 1989
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Doege KJ, Sasaki M, Kimura T, Yamada Y., J. Biol. Chem. 266(2), 1991
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PMID: 2026585
Sandy JD, Neame PJ, Boynton RE, Flannery CR., J. Biol. Chem. 266(14), 1991
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Cleavage of cartilage proteoglycan between G1 and G2 domains by stromelysins.
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Fosang AJ, Neame PJ, Hardingham TE, Murphy G, Hamilton JA., J. Biol. Chem. 266(24), 1991
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Identification of a stromelysin cleavage site within the interglobular domain of human aggrecan. Evidence for proteolysis at this site in vivo in human articular cartilage.
Flannery CR, Lark MW, Sandy JD., J. Biol. Chem. 267(2), 1992
PMID: 1730630
Flannery CR, Lark MW, Sandy JD., J. Biol. Chem. 267(2), 1992
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Detection of stromelysin and collagenase in synovial fluid from patients with rheumatoid arthritis and posttraumatic knee injury.
Walakovits LA, Moore VL, Bhardwaj N, Gallick GS, Lark MW., Arthritis Rheum. 35(1), 1992
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Walakovits LA, Moore VL, Bhardwaj N, Gallick GS, Lark MW., Arthritis Rheum. 35(1), 1992
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Mechanism of catabolism of aggrecan by articular cartilage.
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Ilic MZ, Handley CJ, Robinson HC, Mok MT., Arch. Biochem. Biophys. 294(1), 1992
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The structure of aggrecan fragments in human synovial fluid. Evidence for the involvement in osteoarthritis of a novel proteinase which cleaves the Glu 373-Ala 374 bond of the interglobular domain.
Sandy JD, Flannery CR, Neame PJ, Lohmander LS., J. Clin. Invest. 89(5), 1992
PMID: 1569188
Sandy JD, Flannery CR, Neame PJ, Lohmander LS., J. Clin. Invest. 89(5), 1992
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Purification and characterization of the human stromelysin catalytic domain expressed in Escherichia coli.
Ye QZ, Johnson LL, Hupe DJ, Baragi V., Biochemistry 31(45), 1992
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Ye QZ, Johnson LL, Hupe DJ, Baragi V., Biochemistry 31(45), 1992
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