Method of determining chymase activity with secretory...

Chemistry: molecular biology and microbiology – Measuring or testing process involving enzymes or... – Involving hydrolase

Reexamination Certificate

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Reexamination Certificate

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07892779

ABSTRACT:
It is now discovered that human chymase cleaves human SLPI at a specific site and that this cleavage can be used as an indicator of chymase activity. The present invention provides methods of diagnosing a chymase-associated disease or evaluating the efficiency of a treatment of a chymase-associated disease in a human subject by measuring SLPI processing, as well as other related methods and compositions.

REFERENCES:
patent: 4376110 (1983-03-01), David
patent: 4486530 (1984-12-01), David
patent: 5223409 (1993-06-01), Ladner
patent: 5567602 (1996-10-01), Clark et al.
patent: 5571698 (1996-11-01), Ladner
patent: 5633227 (1997-05-01), Muller et al.
patent: 5861264 (1999-01-01), Elrod et al.
patent: 7247704 (2007-07-01), Barr
patent: 7575888 (2009-08-01), Belkowski et al.
patent: 2002/0010318 (2002-01-01), Niven
patent: 2003/0195172 (2003-10-01), Greco
patent: 2004/0110811 (2004-06-01), Sakai
patent: 2005/0176769 (2005-08-01), Hawkins
Westin U. et al. The Effect of Immediate Hypersensitivity Reactions . . . Allergy (Copenhagen) 54(8)857-865, 1999.
Belkowski S. et al. Cleaved Secretory Leucocyte Protease Inhibitor . . . Clinical & Experimental Allergy 39(8)1179-1186, 2009.
Pemberton, “Differential Inhibition of Mast Cell Chymases by Secretory Leukocyte Protease Inhibitor”, Biochimica et Biophysica Acta., 1998, vol. 1379, pp. 29-34, abstract.
Grutter et al., Embo J 1988; 7:345-51.
Bitter et al., “Expression and Secretion Vectors for Yeast”, Methods in Enzymology, (1987), vol. 153, pp. 516-544.
Cull et al., “Screening for Receptor Ligands Using Large Libraries of Peptides Linked to the C Terminus of the Lac Repressor”, Proceedings of the National Academy of Sciences of the United States of America, (1992), vol. 89, pp. 1865-1869.
Dell'Italia et al., “Dissecting the Role of Chymase in Angiotensin II Formation and Heart and Blood Vessel Diseases”, Current Opinion in Cardiology, (2003) vol. 17, issue 5, pp. 374-379.
Doggrell et al., “Cardiac Chymase: Pathophysiological Role and Therapeutic Potential of Chymase Inhibitors”, Canadian Journal of Physiology and Pharmacology, (2005), vol. 83, issue 2, pp. 123-130.
Fink et al., “Inhibition of Mast Cell Chymase by Eglin c and Antileukoprotease (HUSI-I). Indications for Potential Biological Functions of these Inhibitors”, Biological Chemistry , Hoppe-Seyler, (1986), vol. 367, issue 7, pp. 567-571.
Fodor, “Multiplexed Biochemical Assays with Biological Chips”, Nature, (1993), vol. 364, pp. 555-556.
Fryksmark et al., “Distribution of Antileukoprotease in Upper Respiratory Mucosa, The Annals of Otology”, Rhinology Laryngology, (1982), vol. 91, issue 3, part 1, pp. 268-271.
Garavilla et al., “A Novel, Potent Dual Inhibitor of the Leukocyte Proteases Cathepsin G and Chymase”, Biochemistry (Easton), (2005), vol. 280, pp. 18001-18007.
Gordon et al., “Applications of Combinatorial Technologies to Drug Discovery. 2. Combinatorial Organic Synthesis, Library Screening Strategies, and Future Directions”, Journal of Medicinal Chemistry, (1994), vol. 37, issue 10, pp. 1385-1401.
Grutter et al., “The 2.5 A X-ray Crystal Structure of the Acid-Stable Proteinase Inhibitor from Human Mucous Secretions Analysed in it Complex with Bovine Alpha-Chymotrypsin”, The EMBO Journal, (1988); vol. 7, issue 2, pp. 345-351.
Houghten et al., “The Use of Synthetic Peptide Combinatorial Libraries for the Identification of Bioactive Peptides”, BioTechniques, (1992), vol. 13, issue 3, pp. 412-421.
Huang et al., “Chymase is Upregulated in Diabetic Nephropathy: Implications for an Alternative Pathway of Angiotensin II-mediated Diabetic Renal and Vascular Disease”, Journal of the American Society of Nephrology, (2003), vol. 14, issue 7, pp. 1738-1747.
Kanazawa et al., “A Case-Control Study of Bronchial Asthma Associated with Ulcerative Colitis: Role of Airway Microvascular Permeability”, Clinical & Experimental Allergy, (2005), vol. 35, issue 11, pp. 1432-1436.
Kobayashi et al., “Mast Cells as a Target of Rheumatoid Arthritis Treatment”, Japanese Journal of Pharmacology, (2002) vol. 90, issue 1, pp. 7-11.
Kramps et al., “Localization of Low Molecular Weight Protease Inhibitor in Serous Secretory Cells of the Respiratory Tract”, The Journal of Histochemistry and Cytochemistry, (1981), vol. 29, issue 6, pp. 712-719.
Kramps et al., “ELISA for Quantitative Measurement of Low-Molecular-Weight Bronchial Protease Inhibitor in Human Sputum”, The American Review of Respiratory Disease, (1984), vol. 129, issue 6, pp. 959-963.
Lam, “Application of Combinatorial Library Methods in Cancer Research and Drug Discovery”, Anticancer Drug Design, (1997), vol. 12, pp. 145-167.
Lam, “A New Type of Synthetic Peptide Library for Identifying Ligand-Binding Activity”, Nature, (1991), vol. 354, pp. 82-84.
Lee et al., “Distribution of Secretory Leukoprotease Inhibitor in the Human Nasal Airway”, The American Review of Respiratory Disease, (1993), vol. 147, issue 3, pp. 710-716.
Mooren et al., “Ultrastructural Localization of the Low Molecular Weight Protease Inhibitor in Human Bronchial Glands”, The Journal of Histochemistry and Cytochemistry, (1982), vol. 30, issue 11, pp. 1130-1134.
Muto et al., “Recent Chymase Inhibitors and Their Effects in in Vivo Models”, IDrugs: The Investigational Drugs Journal, (2002), vol. 5, issue 12, pp. 1141-1150.
Needleman & Wunsch, “A General Method Applicable to the Search for Similarities in the Amino Acid Sequence of Two Protein”, Journal of Molecular Biology, (1970) vol. 48, pp. 443-453.
Ota et al., “The Expression of Secretory Leukocyte Protease Inhibitor (SLPI) in the Fallopian Tube: SLPI Protects the acrosome Reaction of Sperm for Inhibitory Effects of Elastase”, Human Reproduction, (2002), vol. 17, issue 10, pp. 2517-2522.
Pemberton et al., “Differential Inhibition of Mast Cell Chymase by Secretory Leukocyte Protease Inhibitor”, Biochimica et Biophysica Acta, (1998); vol. 1379, issue 1, pp. 29-34.
Vogelmeier, “Anti-Neutrophil Elastase Defense of the Normal Human Respiratory Epithelial Surface Provided by the Secretory Leukoprotese Inhibitor”, The Journal of Clinical Investigation (1991), vol. 87, pp. 482-488.
Scott and Smith, “Searching for Peptide Ligands with an Epitope Library”, Science, (1990), vol. 249, issue 4967, pp. 386-390.
Takai et al., “Inhibition of Chymase Reduces Vascular Proliferation in Dog Grafted Veins”, FEBS Letters, (2000), vol. 467, issue 2-3, pp. 141-144.
Thompson et al., “Isolation, Properties, and Complete Amino Acid Sequence of Human Secretory Leukocyte Protease Inhibitor, a Potent Inhibitor of Leukocyte Elastase”, Proceedings of the National Academy of Sciences of the United States of America, (1986), vol. 83, issue 18, pp. 6692-6696.
Walter et al., “Inhibition of Human Mast Cell Chymase by Secretory Leukocyte Proteinase Inhibitor: Enhancement of the Interaction by Heparin”, Archives of Biochemistry and Biophysics, (1996), vol. 327, issue 1, pp. 81-88.
Westin et al., “Identification of SLPI (Secretory Leukocyte Protease Inhibitor) in Human Mast Cells Using Immunohistochemistry and in Situ Hybridisation”, Biological Chemistry, (1999), vol. 380, issue 4, pp. 489-493.
Willems et al., “Antileukoprotease-Containing Bronchiolar Cells. Relationship with Morphologic Disease of Small Airways and Parenchyma”, The American Review of Respiratory Disease, (1989), vol. 139, issue 5, pp. 1244-1250.
Zuckermann et al., “Discovery of Nanomolar Ligands for 7-Transmembrane G-Protein-Coupled Receptors from a Diverse N-(Substituted) Glycine Peptoid Library”, Journal of Medicinal Chemistry, (1994), vol. 37, pp. 2678-2685.

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