Aggrecanase-1 and -2 peptide substrates and methods

Details Aggrecanase-1 and -2 peptide substrates and methods Aggrecanase-1 and -2 peptide substrates and methods

2007-12-25

2007-12-25

Prouty, Rebecca E. (Department: 1652)

Chemistry: molecular biology and microbiology

Measuring or testing process involving enzymes or...

Involving hydrolase

C435S226000, C530S327000, C530S300000

Reexamination Certificate

active

11012797

ABSTRACT:
The present invention describes synthetic peptide substrates of the metalloproteases, aggrecanase-1 and/or -2 suitable for assays of enzyme activity. The invention also describes methods using these peptides to discover pharmaceutical agents that modulate these proteases.

REFERENCES:
Tortorella et al. The trombospondin motif of aggrecanase-1 (ADAMTS-4) is critical for aggrecan substrate recognition and cleavage, J. Biol. Chem. Aug. 18, 2000, 275/33, pp. 25791-25797.
Supplementary Partial European Search Report dated Nov. 15, 2005 for corresponding Appln. No. 03 70 2145.
Horber C. et al.“Truncation of the Amino-Terminus of the Recombinant Aggrecan rAgg1mut Leads to Reduced Cleavage at the Aggrecanase Site. Efficient Aggrecanase Catabolism May Depend on Multiple Subtrate Interactions.” Matrix Biology: Journal of the International Society for Matrix Biology Nov. 2000, vol. 19, No. 6, Nov. 2000 pp. 533-543, XP002350412.
Mercuri F.A. et al.“Mutations in the Interglobular Domain of Aggrecan Alter Matrix Metalloproteinase and Aggrecanase Cleavage Patterns. Evidence that Matrix Metalloproteinase Cleavage Interferes with Aggrecanase Activity” The Journal of Biological Chemistry, Oct. 20, 2000, vol. 275, No. 42, XP002350413.
Fosang A.J. et al.: Aggrecan is Degraded By Matrix Metalloproteinases in Human Arthiritis: Evidence That Matrix Metalloproteinase and Aggrecanase Activities Can Be Independent Journal of Clinical Investigation, New York, NY USA, vol. 98, No. 10, Nov. 1996 XP001183906.

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