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Science 4 June 1999:
Vol. 284. no. 5420, pp. 1664 - 1666
DOI: 10.1126/science.284.5420.1664
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Reports

Purification and Cloning of Aggrecanase-1: A Member of the ADAMTS Family of Proteins

M. D. Tortorella, 1 T. C. Burn, 2 M. A. Pratta, 1 I. Abbaszade, 2 J. M. Hollis, 2 R. Liu, 1 S. A. Rosenfeld, 2 R. A. Copeland, 3 C. P. Decicco, 4 R. Wynn, 2 A. Rockwell, 4 F. Yang, 3 J. L. Duke, 2 K. Solomon, 1 H. George, 2 R. Bruckner, 1 H. Nagase, 5 Y. Itoh, 5* D. M. Ellis, 2 H. Ross, 2 B. H. Wiswall, 2 K. Murphy, 2 M. C. Hillman Jr., 2 G. F. Hollis, 2 R. C. Newton, 1 R. L. Magolda, 1 J. M. Trzaskos, 1 E. C. Arner 1dagger

We purified, cloned, and expressed aggrecanase, a protease that is thought to be responsible for the degradation of cartilage aggrecan in arthritic diseases. Aggrecanase-1 [a disintegrin and metalloproteinase with thrombospondin motifs-4 (ADAMTS-4)] is a member of the ADAMTS protein family that cleaves aggrecan at the glutamic acid-373-alanine-374 bond. The identification of this protease provides a specific target for the development of therapeutics to prevent cartilage degradation in arthritis.

1 Department of Inflammatory Diseases Research,
2 Department of Applied Biotechnology,
3 Department of Enzymology,
4 Department of Chemical and Physical Sciences, DuPont Pharmaceuticals Company, Wilmington, DE 19880-0400, USA.
5 Department of Biochemistry and Molecular Biology, University of Kansas School of Medicine, Kansas City, KS 66160, USA.
*   Present address: Department of Cancer Cell Research, Institute of Medical Science, University of Tokyo, Minato-ku, Tokyo 108-8639, Japan.

dagger    To whom correspondence should be addressed. E-mail: elizabeth.c.arner{at}dupontpharma.com

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Characterization of ADAMTS-9 and ADAMTS-20 as a Distinct ADAMTS Subfamily Related to Caenorhabditis elegans GON-1.
R. P. T. Somerville, J.-M. Longpre, K. A. Jungers, J. M. Engle, M. Ross, S. Evanko, T. N. Wight, R. Leduc, and S. S. Apte (2003)
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Chest 117, 295S-299S
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J. D. Mott, C. L. Thomas, M. T. Rosenbach, K. Takahara, D. S. Greenspan, and M. J. Banda (2000)
J. Biol. Chem. 275, 1384-1390
   Abstract »    Full Text »    PDF »
The Four Terminal Components of the Complement System Are C-Mannosylated on Multiple Tryptophan Residues.
J. Hofsteenge, M. Blommers, D. Hess, A. Furmanek, and O. Miroshnichenko (1999)
J. Biol. Chem. 274, 32786-32794
   Abstract »    Full Text »    PDF »
Recombinant Human Aggrecan G1-G2 Exhibits Native Binding Properties and Substrate Specificity for Matrix Metalloproteinases and Aggrecanase.
F. A. Mercuri, K. J. Doege, E. C. Arner, M. A. Pratta, K. Last, and A. J. Fosang (1999)
J. Biol. Chem. 274, 32387-32395
   Abstract »    Full Text »    PDF »
Cloning and Characterization of ADAMTS11, an Aggrecanase from the ADAMTS Family.
I. Abbaszade, R.-Q. Liu, F. Yang, S. A. Rosenfeld, O. H. Ross, J. R. Link, D. M. Ellis, M. D. Tortorella, M. A. Pratta, J. M. Hollis, et al. (1999)
J. Biol. Chem. 274, 23443-23450
   Abstract »    Full Text »    PDF »
Metalloprotease-disintegrins: modular proteins capable of promoting cell-cell interactions and triggering signals by protein-ectodomain shedding.
J Schlondorff and C. Blobel (1999)
J. Cell Sci. 112, 3603-3617
   Abstract »    PDF »
TIMP-3 Is a Potent Inhibitor of Aggrecanase 1 (ADAM-TS4) and Aggrecanase 2 (ADAM-TS5).
M. Kashiwagi, M. Tortorella, H. Nagase, and K. Brew (2001)
J. Biol. Chem. 276, 12501-12504
   Abstract »    Full Text »    PDF »
Structure of von Willebrand Factor-cleaving Protease (ADAMTS13), a Metalloprotease Involved in Thrombotic Thrombocytopenic Purpura.
X. Zheng, D. Chung, T. K. Takayama, E. M. Majerus, J. E. Sadler, and K. Fujikawa (2001)
J. Biol. Chem. 276, 41059-41063
   Abstract »    Full Text »    PDF »
The Thrombospondin Motif of Aggrecanase-1 (ADAMTS-4) Is Critical for Aggrecan Substrate Recognition and Cleavage.
M. Tortorella, M. Pratta, R.-Q. Liu, I. Abbaszade, H. Ross, T. Burn, and E. Arner (2000)
J. Biol. Chem. 275, 25791-25797
   Abstract »    Full Text »    PDF »
Properdin, the Positive Regulator of Complement, Is Highly C-Mannosylated.
S. Hartmann and J. Hofsteenge (2000)
J. Biol. Chem. 275, 28569-28574
   Abstract »    Full Text »    PDF »
Characterization of METH-1/ADAMTS1 Processing Reveals Two Distinct Active Forms.
J. C. Rodriguez-Manzaneque, A. B. Milchanowski, E. K. Dufour, R. Leduc, and M. L. Iruela-Arispe (2000)
J. Biol. Chem. 275, 33471-33479
   Abstract »    Full Text »    PDF »
Brevican Is Degraded by Matrix Metalloproteinases and Aggrecanase-1 (ADAMTS4) at Different Sites.
H. Nakamura, Y. Fujii, I. Inoki, K. Sugimoto, K. Tanzawa, H. Matsuki, R. Miura, Y. Yamaguchi, and Y. Okada (2000)
J. Biol. Chem. 275, 38885-38890
   Abstract »    Full Text »    PDF »
Age-related Changes in Aggrecan Glycosylation Affect Cleavage by Aggrecanase.
M. A. Pratta, M. D. Tortorella, and E. C. Arner (2000)
J. Biol. Chem. 275, 39096-39102
   Abstract »    Full Text »    PDF »
Cysteine Array Matrix Metalloproteinase (CA-MMP)/MMP-23 Is a Type II Transmembrane Matrix Metalloproteinase Regulated by a Single Cleavage for Both Secretion and Activation.
D. Pei, T. Kang, and H. Qi (2000)
J. Biol. Chem. 275, 33988-33997
   Abstract »    Full Text »    PDF »
Versican V1 Proteolysis in Human Aorta in Vivo Occurs at the Glu441-Ala442 Bond, a Site That Is Cleaved by Recombinant ADAMTS-1 and ADAMTS-4.
J. D. Sandy, J. Westling, R. D. Kenagy, M. L. Iruela-Arispe, C. Verscharen, J. C. Rodriguez-Mazaneque, D. R. Zimmermann, J. M. Lemire, J. W. Fischer, T. N. Wight, et al. (2001)
J. Biol. Chem. 276, 13372-13378
   Abstract »    Full Text »    PDF »
Identification, Characterization, and Intracellular Processing of ADAM-TS12, a Novel Human Disintegrin with a Complex Structural Organization Involving Multiple Thrombospondin-1 Repeats.
S. Cal, J. M. Arguelles, P. L. Fernandez, and C. Lopez-Otin (2001)
J. Biol. Chem. 276, 17932-17940
   Abstract »    Full Text »    PDF »
Sites of Aggrecan Cleavage by Recombinant Human Aggrecanase-1 (ADAMTS-4).
M. D. Tortorella, M. Pratta, R.-Q. Liu, J. Austin, O. H. Ross, I. Abbaszade, T. Burn, and E. Arner (2000)
J. Biol. Chem. 275, 18566-18573
   Abstract »    Full Text »    PDF »
Brain-enriched Hyaluronan Binding (BEHAB)/Brevican Cleavage in a Glioma Cell Line Is Mediated by a Disintegrin and Metalloproteinase with Thrombospondin Motifs (ADAMTS) Family Member.
R. T. Matthews, S. C. Gary, C. Zerillo, M. Pratta, K. Solomon, E. C. Arner, and S. Hockfield (2000)
J. Biol. Chem. 275, 22695-22703
   Abstract »    Full Text »    PDF »
Generation and Novel Distribution of Matrix Metalloproteinase-derived Aggrecan Fragments in Porcine Cartilage Explants.
A. J. Fosang, K. Last, H. Stanton, D. B. Weeks, I. K. Campbell, T. E. Hardingham, and R. M. Hembry (2000)
J. Biol. Chem. 275, 33027-33037
   Abstract »    Full Text »    PDF »
Mutations in the Interglobular Domain of Aggrecan Alter Matrix Metalloproteinase and Aggrecanase Cleavage Patterns. EVIDENCE THAT MATRIX METALLOPROTEINASE CLEAVAGE INTERFERES WITH AGGRECANASE ACTIVITY.
F. A. Mercuri, R. A. Maciewicz, J. Tart, K. Last, and A. J. Fosang (2000)
J. Biol. Chem. 275, 33038-33045
   Abstract »    Full Text »    PDF »


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