Selective substrates for matrix metalloproteinases

Details Selective substrates for matrix metalloproteinases Selective substrates for matrix metalloproteinases

2002-09-13

2008-10-21

Helms, Larry R. (Department: 1642)

Chemistry: natural resins or derivatives; peptides or proteins;

Peptides of 3 to 100 amino acid residues

C530S328000, C530S329000, C530S333000

Reexamination Certificate

active

07439319

ABSTRACT:
The invention provides isolated MMP-2, MMP-9 and MT1-MMP selective substrate polypeptides or functional peptidomimetics. The selective substrate polypeptides contain the following sequences: MMP-2 selective substrate polypeptides contain SEQ ID NOS:1-27, MMP-9 selective substrate polypeptides contain SEQ ID NOS:28-35, and MT1-MMP selective substrate polypeptide contain SEQ ID NOS:36-40. In addition, the invention provides a method of preferentially directing a moiety to a site of MMP-2 activity by administering to a subject an effective amount of an isolated MMP-2 selective substrate polypeptide containing SEQ ID NOS:45-47 linked to a moiety. Also provided is a method of preferentially directing a moiety to a site of MMP-9 activity by administering to a subject an effective amount of an isolated MMP-9 selective substrate polypeptide containing SEQ ID NO:44 linked to a moiety, and preferentially directing a moiety to a site of MT1-MMP activity by administering to a subject an effective amount of an isolated MT1-MMP selective substrate polypeptide containing SEQ ID NOS:36-40 linked to a moiety.

REFERENCES:
patent: 5518912 (1996-05-01), Zasloff et al.
patent: 6399075 (2002-06-01), Howley et al.
Burgess et al., J of Cell Bio. 111:2129-2138, 1990.
Lazar et al., Molecular and Cellular Biology 8:1247-1252, 1988.
Bowie et al., Science, 247:1306-1310, 1990.
PIR Database, Accession No. S54424, Apr. 1997.
PIR Database, Accession No. A45185, Sep. 1993.
PIR Database, Accession No. D71810, Feb. 12, 1999.
Simth et al., Chem Rev, vol. 97, p. 391-410.
Jain, Scientific American Jul. 1994.
Gura, Science, v278, 1997, pp. 1041-1042.
Simth et al., Chem Rev, vol. 97 p. 391-410, 1997.
Bergers et al., “Matrix metalloproteinase-9 triggers the angiogenic switch during carcinogenesis,”Nature Cell Biol. 2:737-744 (2000).
Birkendal-Hansen, “Proteolytic remodeling of extracellular matrix,”Curr. Opin. Cell Biol. 7:728-735 (1995).
Burger's Medicinal Chemistry and Drug DiscoveryEditor Manfred E. Wolff, Ch. 15, pp. 619-620, John Wiley & Sons Inc., New York, New York (1995).
Chen et al., “A Unique Substrate Recognition Profile for Matrix Metalloproteinase-2,”J. Biol. Chem. 277:4485-4491 (2002).
Coussens et al., “MMP-9 Supplied by Bone Marrow-Derived Cells Contributes to Skin Carcinogenesis,”Cell103:481-490 (2000).
DeFeo-Jones et al., “A peptide-doxorubicin ‘prodrug’ activated by prostate-specific antigen selectively kills prostate tumor cells positive for prostate-specific antigen in vivo,”Nature Med. 6:1248-1252 (2000).
Deng et al., “Substrate Specificity of Human Collagenase 3 Assessed Using a Phage-displayed Peptide Library,”J. Biol. Chem. 275:31422-31427 (2000).
Denmeade et al., “Enzymatic Activation of Doxorubicin-Peptide Prodrug by Prostate-Specific Antigen,”Cancer Res. 58:2537-2540 (1998).
Folkman, “Angiogenesis in cancer, vascular, rheumatoid and other disease,”Nature Med. 1:27-31 (1995).
Goldman et al., “Targeted Gene Delivery to Kaposi's Sarcoma Cellsviathe Fibroblast Growth Factor Receptor,”Cancer Res. 57:1447-1451 (1997).
Koivunen et al., “Tumor targeting with a selective gelatinase inhibitor,”Nature Biotech. 17:768-774 (1999).
Kridel et al., “Substrate Hydrolosis by Matrix Metalloproteinase-9,”J. Biol. Chem. 276:20572-20578 (2001).
Kridel et al., “A Substrate Phage Enzyme-Linked Immunosorbent Assay to Profile Panels of Proteases,”Anal. Biochem. 294:176-184 (2001).
Murphy and Crabbe, “Gelatinases A and B,”Methods Enzymol. 248:470-484 (1995).
NCBI Accession No. P28618 (Dec. 1992).
Netzel-Arnett et al., “Comparative Sequence Specificities of Human 72- and 92-kDa Gelatinases (Type IV Collagenases) and PUMP (Matrilysin),”Biochemistry32:6427-6432 (1993).
Netzel-Arnett et al., “Sequence Specificities of Human Fibroblast and Neutrophil Collagenases,”J. Biol. Chem. 266:6747-6755 (1991).
Ohkubo et al., “Identification of Substrate Sequences for Membrane Type-1 Matrix Metalloproteinase Using Bacteriophage Peptide Display Library,”Biochem. Biophys. Res. Comm. 266:308-313 (1999).
Ohuchi et al., “Membrane Type 1 Matrix Metalloproteinase Digests Interstitial Collagens and Other Extracellular Matrix Macromolecules,”J. Biol. Chem. 272:2446-2451 (1997).
Rak et al., “Consequences of angiogenesis for tumor progression, metastasis and cancer therapy,”Anti-Cancer Drugs6:3-18 (1995).
Schechter and Berger, “On the Size of the Active Site in Proteases. I. Papain,”Biochem. and Biophys. Res. Comm. 27:157-162 (1967).
Smith et al., “Rapid Identification of Highly Active and Selective Substrates for Stromelysin and Matrilysin Using Bacteriophage Peptide Display Libraries,”J. Biol. Chem. 270:6440-6449 (1995).
Smith et al., “Building Synthetic Antibodies as Adhesive Ligands for Integrins,”J. Biol. Chem. 269:32788-32795 (1994).
Weissleder et al., “In vivo imaging of tumors with protease-activated near-infrared fluorescent probes,”Nature Biotech. 17:375-378 (1999).

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