Human osteoclast derived cathepsin

Details Human osteoclast derived cathepsin Human osteoclast derived cathepsin

2006-02-07

2006-02-07

Chan, Christina (Department: 1644)

Chemistry: molecular biology and microbiology

Measuring or testing process involving enzymes or...

Involving antigen-antibody binding, specific binding protein...

C530S389100, C530S388100, C530S391100

Reexamination Certificate

active

06994978

ABSTRACT:
Disclosed is a human osteoclast-derived cathepsin (Cathepsin O) polypeptide and DNA(RNA) encoding such cathepsin O polypeptides. Also provided is a procedure for producing such polypeptide by recombinant techniques. The present invention also discloses antibodies, antagonists and inhibitors of such polypeptide which may be used to prevent the action of such polypeptide and therefore may be used therapeutically to treat bone diseases such as osteoporosis and cancers, such as tumor metastases.

REFERENCES:
patent: 5223408 (1993-06-01), Goeddel et al.
patent: 5312816 (1994-05-01), Spielvogel et al.
patent: 5374623 (1994-12-01), Zimmerman et al.
patent: 5486623 (1996-01-01), Zimmerman et al.
patent: 5501969 (1996-03-01), Hastings
patent: 5552281 (1996-09-01), Stashenko et al.
patent: 5624801 (1997-04-01), Stashenko et al.
patent: 5656728 (1997-08-01), Stashenko et al.
patent: 5736357 (1998-04-01), Bromme
patent: 0 104 920 (1984-04-01), None
patent: 0 110674 (1987-04-01), None
patent: 0 504 938 (1992-09-01), None
patent: 0 520 427 (1994-12-01), None
patent: 0 111 129 (1998-09-01), None
patent: 0 525420 (1999-05-01), None
patent: WO-91/01378 (1991-02-01), None
patent: WO-94/23033 (1994-10-01), None
patent: WO-95/24182 (1995-09-01), None
patent: WO-96/13523 (1996-05-01), None
patent: WO-97/35971 (1997-10-01), None
patent: WO-97/47642 (1997-12-01), None
patent: WO-98/00716 (1998-01-01), None
patent: WO-98/03651 (1998-01-01), None
patent: WO-98/08494 (1998-01-01), None
patent: WO-98/20024 (1998-05-01), None
patent: WO-98/20156 (1998-05-01), None
patent: WO-98/34117 (1998-08-01), None
Barrett, et al., “L-trans-Epoxysuccinyl-leucylamido(4-guanidino)butane (E-64) and its analogues as inhibitors of cysteine proteinases including cathepsins B, H and L,”Biochem. J., 201:189 (1982).
Bossard, et al., “Proteolytic activity of human osteoclast cathepsin K,”J. Biol. Chem., 271:12517-12524 (1996).
Bromme, et al., “Human cathepsin 02, a novel cysteine protease highly expressed in osteoclastomas and ovary molecular cloning, sequencing and tissue distribution,”J. Biol. Chem., 376(6):379-384 (1995).
Bromme, et al., “Peptide methyl ketones as reversible inhibitors of cysteine proteinases,”J. Enzyme Inhibition, 3:13-21 (1989).
Bromme, et al., “Functional expression of human cathepsin S inSaccharomyces cerevisiae,”J. Biol. Chem., 268:4832-4838 (1993).
Bromme, et al., “Potent inactivation of cathepsins S and L by peptidyl (Acyloxy)methyl ketonesa.b,”J. Biol. Chem., 375:343-347 (1994).
Bromme, et al., “Peptide vinyl sulphones: a new class of potent and selective cysteine protease inhibitors,”Biochem. J., 315:85-89 (1996).
Bromme, et al., “Human cathepsin 02, a matrix protein-degrading cysteine protease expressed in osteoclasts,”J. Biol. Chem., 271:2126-2132 (1996).
Brown, et al., “Lymphopain, a cytotoxic T and natural killer cell-associated cysteine proteinase,”Leukemia, 12:1771-1781 (1998).
Carmona, et al., “Potency and selectivity of the cathepsin L propeptide as an inhibitor of cysteine proteases,”Biochem. J., 35:8149-8157 (1996).
Chagas, et al., “Inhibition of cathepsin B by its propeptide: use of overlapping peptides to identify a critical segment,”FEBS LETTS., 392:233-236 (1996).
Cygler, et al., “Proregion structure of members of the papain superfamily. Mode of inhibition of enzymatic activity,”Biochemie, 79:645-652 (1997).
Cygler, et al., “Structure of rat procathepsin B: mode for inhibition of cysteine protease activity by the proregion structure,”Structure, 4:405-416 (1996).
D'Alessio, et al., “Expression inEscherichia coli, refolding, and purification of human procathepsin K, an osteoclast-specific protease,”Protein Expression and Purification, 15:213-220 (1999).
Delaisse, et al., “Inhibition of bone resorption in culture by inhibitors of thiol proteinases,”J. Biochem., 192:365-368 (1980).
Delaisse, et al., “In vivo and in vitro evidence for the involvement of cysteine proteinases in bone resorption,”Biochem. Biophys. Res. Comm., 125:441-447 (1984).
Delaisse, et al., “The effects of inhibitors of cysteine—proteinases and collagenase on the resorptive activity of isolated osteoclasts,”Bone, 8:305-313 (1987).
Delaisse, et al., “Collagenolytic cysteine proteinases of bone tissue,”Biochem. J., 279:167-174 (1991).
Drake, et al., “Identification of a novel osteoclast selective human cysteine proteinase,”J. Bone Mineral Research, 9:5177 (A110) (1994).
Drake, et al., “Cathepsin K., but not Cathepsins B, L, or S, is abundantly expressed in human osteoclasts,”J. Biol. Chem., 271:12511-12516 (1996).
Duffy, et al., “Design and synthesis of diaminopyrrolidinone inhibitors of human osteoclast cathepsin K,”Bioorganic&Medicinal Chemistry, 9:1907-1910 (1999).
Fox, et al., “Potent slow-binding inhibition of cathepsin B by its propeptide,”Biochem, J., 31:12571-12576 (1992).
Gelb, et al., “Pycnodysostosis, a lysosomal disease caused by cathepsin K deficiency,”Science, 273:1236-1238 (1996).
Gelb, et al., “Structure and chromosomal assignment of the human cathepsin K Gene,”Genomics, 41:258-262 (1997).
Gelb, et al., “Cathepsin K: isolation and characterization of the murine cDNA and genomic sequence, the homolog of the human pycnodysostosis gene,”Biochem. and Mol. Med., 59:200-206 (1996).
Goto, et al., “Immunohistochemical localization of cathepsins B, D and L in the rat osteoclast,”Histochemistry, 99:411-414 (1993).
Goto, et al., “Localization of cathepsins B, D, and L in the rat osteoclast by immuno-light and -electron microscopy,”Histochemistry, 101:33-40 (1994).
Guay, et al., “Cloning and expression of Rhesus Monkey cathepsin K,”Bone, 25:204-209 (1999).
Hill, et al., “Inhibition of bone resorption by selective inactivators of cysteine proteinases,”J. Cell Biochem., 56:118-130 (1994).
Hudecki, et al., “Limited benefit to genetically dystrophic chickens from a synthetic proteinase inhibitor: Ep475,”Chemical Abstracts., 99:82493u (1983).
Hudecki, et al., “Limited benefit to genetically dystrophic chickens from a synthetic proteinase inhibitor: Ep475,”J. Neurol. Sci., 60:55-66 (1983).
Inaoka, et al., “Molecular cloning of human cDNA for cathepsin K: novel cysteine proteinase predominantly expressed in bone,”Biochem.&Biophys. Res. Comm., 206(1):89-96 (1995).
James, et al., “Development and characterization of a human in vitro resorption assay: demonstration of utility using novel antiresorptive agents,”J. Bone&Mineral Research, 14:1562-1569 (1999).
Kakegawa, et al., “Participation of cathepsin L on bone resorption,”FEBS LETTS., 321:247-250 (1993).
Kane, et al., “The role of cathepsin L in malignant transformation,”Seminars in Cancer Biol., 1:127-136 (1990).
Lalonde, et al., “The crystal structure of human procathepsin K.,”Biochem., 38:862-869 (1999).
Lee, et al., “Generation of cDNA probes directed by amino acid sequence: cloning of urate oxidase,”Science, 239:1288-1291 (1988).
Lehninger, A., “Biochemistry” 2nded.; Worth Publishers, Inc., New York, pp. 141 and 150 (1975).
Lerner, et al., “Human cystatin C, a cysteine proteinase inhibitor, inhibits bone resorption in vitro stimulated by a parathyroid hormone and parathyroid hormone related peptide of malignancy,”J. Bone&Mineral Research, 4:433-439 (1992).
Lerner, R.A., “Tapping the immunological repertoire to produce antibodies of predetermined specificity,”Nature, 299:592-596 (1982).
Li, et al., “Characterization of mouse cathepsin K gene, the gene promoter, and the gene expression,”J. Bone&Mineral Research, 14:487-499 (1992).
Li, et al., “Cloning and complete coding s

Affiliated with

Also associated with

Rating

Human osteoclast derived cathepsin does not yet have a rating. At this time, there are no reviews or comments for this patent.

If you have personal experience with Human osteoclast derived cathepsin, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Human osteoclast derived cathepsin will most certainly appreciate the feedback.

Rate now

Comments { 0 }

Profile ID: LFUS-PAI-O-3661011