Drug – bio-affecting and body treating compositions – Designated organic active ingredient containing – Peptide containing doai
Reexamination Certificate
2008-09-23
2008-09-23
Saunders, David A (Department: 1644)
Drug, bio-affecting and body treating compositions
Designated organic active ingredient containing
Peptide containing doai
C514S885000, C424S810000
Reexamination Certificate
active
10913045
ABSTRACT:
Methods and products for suppressing a class II MHC-restricted immune response in a mammal, or in mammalian cells, are described. The methods depend upon inhibiting invariant chain proteolysis by cathepsin S from class II MHC/invariant chain complexes, thereby reducing the competency of class II MHC molecules for binding antigenic peptides, reducing presentation of antigenic peptides by class II MHC molecules, and suppressing immune responses. The methods may be employed in the treatment of autoimmune diseases, allergic responses, and organ or tissue graft rejection. Pharmaceutical and therapeutic compositions which are peptide based inhibitors of cathepsin S are also described.
REFERENCES:
patent: 5422359 (1995-06-01), Ando et al.
patent: 5501969 (1996-03-01), Hastings et al.
patent: 5510333 (1996-04-01), Angelastro et al.
patent: 5559028 (1996-09-01), Humpreys
patent: WO-94/04557 (1994-03-01), None
patent: WO-95/23222 (1995-08-01), None
patent: WO-96/30353 (1996-10-01), None
Ahmed N.K. et al. “Peptidyl Fluoromethyl Ketones as Inhibitors of Cathepsin B: Implication for Treatment of Rheumatoid Arthritis”, Biochemical Pharmacology 44(6):1201-1207 (1992).
Bromme, D. et al. “Peptidyl vinyl sulphones: a new class of potent and selective cysteine protease inhibitors”, Biochem J. 315:85-89 (1996).
Bromme, D. et al. “N-Peptidyl-o-carbamoyl amino acid hydroxamates: Irreversible inhibitors for the study of the S2′ specificity of cysteine proteinases”, FEBS 12414 322(3):211-214 (1993).
Bromme, D. et al. “Potent Inactivitation of Cathepsins S and L by Peptidyl (Acyloxy)methyl Ketones”, Biol. Chem. Hoppe-Seyler 375:343-347 (1994).
Bromme, D. et al. “The Specificity of Bovine Spleen Cathepsin S: A comparison with rat liver cathepsins L and B”, Biochem J. 264:475-481 (1989).
Carmona, E. et al. “Potency and Selectivity of the Cathepsin L Propeptide as an Inhibitor of Cysteine Protease”, Biochemistry 35:8149-8157 (1996).
Demuth, H.U., et al. “N-peptidyl, O-acyl hydroxamates: comparison of the selective inhibition of serine and cystein proteinases”, Biochimica et Biophysica Acta, 1295:179-186 (1996).
Gour-Salin, B.J. “E-64 Analogs as Inhibitors of Cathepsin L and Cathepsin S: Importance of the S2-P2 Interactions for Potency and Selectivity”, Bioorganic Chemistry 22:227-241 (1994).
Hanzlik et al., “Vinylogous Amino Acid Esters: A New Class of Inactivators of Thiol Proteases”, Journal of Medicinal Chemistry, 27(6):711-712 (1984).
Hughes, E.A. et al. “The Protease Inhibitor, N-Acetyl-L-Leucyl-L-Leucyl- L-Norleucinal, Decreases the Pool of Major Histocompatibility Complex Class I-binding Peptides and Inhibits Peptide Trimming in the Endoplasmic Reticulum”, J. Exp. Med. 183:1569-1578 (1996).
Kirschke, H. et al. “Cathepsin S and Related Lysosomal Endopeptidases” Cysteine Peptidases Academic Press, Inc. 34:500-511 (1994).
Valderrama, et al., J. Neurological Sciences, 82 (1-3): 133-143 (1987).
McDonald et al., Arch. Biochem. Biophys., 305 (1): 1-8 (1993).
Takei et al., Transplantation, 50 (1): 14-20 (1990).
Eisenbarth et al., New England Journal of Medicine, 298 (2): 93 (1978).
Lenarcic et al., “Pig leukocyte cysteine proteinase inhibitor (PLCPI), a new memeber of the stefin family”, FEBS 13443 336(2):289-292 (1993).
Morton, P. et al. “Delivery of Nascent MHC Class II-Invariant Chain Complexes to Lysosomal Compartments and Proteolysis of Invariant Chain by Cysteine Proteases Precedes Peptide Binding in B-Lymphoblastoid Cells”, The Journal of Immunology 154:137-150 (1995).
Okamoto, K. et al. “The Characterization of the Inhibition of Mature Cysteine Proteases By Their Proregions”, J. of Cellular Biochemistry Suppl. 0(1913):254 (1995).
Palmer, J.T., et al. “Vinyl Sulfones as Mechanism-Based Cysteine Protease Inhibitors”, J.Med.Chem. 38:3193-3196 (1995).
Petanceska, S. et al. “Expression of Rat Cathepsin S in Phagocytic Cells”, The Journal of Biological Chemistry 271 (8):4403-4409 (1996).
Pohl, J. et al. “Chromophoric and Fluorophoric Peptide Substrates Cleaved through the Dipeptidyl Carboxypeptidase Activity of Cathepsin B”, Analytical Biochemistry 165:96-101 (1987).
Riese, R.J., et al. “Essential Role for Cathepsin S in MHC Class II-Associated Invariant Chain Processing and Peptide Loading”, Immunity 4:357-366 (1996).
Shaw, E. et al. “The affinity-labelling of cathepsin S with peptidyl diazomethyl ketones: Comparison with the inhibition of cathespin L and calpain”, FEBS 13268 334(3):340-342 (1993).
Shi, G.P. et al. “Human Cathepsin S: Chromosomal Localization, Gene Structure, and Tissue Distribution”, The Journal of Biological Chemistry 269(15):11530-11536 (1994).
Turk, V., et al. “Human Cysteine Proteinases and Their Inhibitors, Stefins and Cystatins” in Biological Functions of Proteases and Inhibitors, N. Katunuma et al., eds. Japanese Scientific Press, Tokyo Japan, Chap. 4:47-59 (1994).
Bogyo Matthew S.
Bryant Paula R.
Chapman Harold A.
Ploegh Hidde L.
Riese Richard J.
Brigham and Women's Hospital
Massachusetts Institute of Technology
Ropes & Gray LLP
Saunders David A
VanderVegt F. Pierre
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