Chemistry: natural resins or derivatives; peptides or proteins; – Proteins – i.e. – more than 100 amino acid residues – Blood proteins or globulins – e.g. – proteoglycans – platelet...
Reexamination Certificate
2011-08-30
2011-08-30
Yu, Misook (Department: 1643)
Chemistry: natural resins or derivatives; peptides or proteins;
Proteins, i.e., more than 100 amino acid residues
Blood proteins or globulins, e.g., proteoglycans, platelet...
C530S391700
Reexamination Certificate
active
08008445
ABSTRACT:
Proteins that bind to matrix metalloproteinase 9 and methods of using such proteins are described.
REFERENCES:
patent: 2002/0159971 (2002-10-01), Houde et al.
patent: 2004/0115202 (2004-06-01), Chen
patent: 2004/0146499 (2004-07-01), Wood et al.
patent: 2005/0118632 (2005-06-01), Chen et al.
patent: 2006/0062777 (2006-03-01), Brooks et al.
patent: 2006/0063204 (2006-03-01), Valkirs et al.
patent: 2006/0142550 (2006-06-01), Chang
patent: 2007/0203209 (2007-08-01), Bartolini et al.
patent: 2007/0207184 (2007-09-01), Ruane et al.
patent: 2007/0258987 (2007-11-01), Francisco et al.
patent: 2009/0186031 (2009-07-01), Wood
patent: 2009/0203060 (2009-08-01), Wood
patent: 2009/0297449 (2009-12-01), Devy et al.
patent: 9957315 (1999-11-01), None
patent: 0190047 (2001-11-01), None
patent: 2009079581 (2009-06-01), None
patent: 2009079585 (2009-06-01), None
patent: 2009111508 (2009-09-01), None
patent: 2010048432 (2010-04-01), None
Ueda et al., “Surviving gene expression in endometrosis,” J. Clin. Endocr. Metab., 2002, vol. 87, pp. 3452-3459.
Vadillo-Ortega et al., “92-kd type IV collagenase (matrix metalloproteinase-9) activity in human amniochorion increases with labor,” Am. J. Pathol., Jan. 1995, vol. 146(1), pp. 148-156.
Van Den Steen et al., “Neutrophil gelatinase B poteniates interleukin-8 tenfold by aminoterminal processing, whereas it degrades CTAP-III, PF-4, and GRO-alpha and leaves RANTES and MCP-2 intact,” Blood, 2000, vol. 96, pp. 2673-2681.
Vu et al., “MMP-9/gelatinase B is a key regulator of growth plate angiogenesis and apoptosis o hypertrophic chondrocytes,” Cell, 1998, vol. 93, pp. 411-422.
Wang et al., “Lipoprotein receptor-mediated induction of matrix metalloproteinase by tissue plasminogen activator,” Nature Med., 2003, vol. 9, pp. 1313-1317.
Yan et al., “Repression of 92-kDa type IV collagenase expression by MTA1 is mediated through direct interactions with the promoter via a mechanism, which is both dependent on and independent of histone deacetylation,” J. Biol. Chem., 2003, vol. 278, pp. 2309-2316.
Yu et al., “Cell surface-localized matrix metalloproteinase-9 proteolytically activates TGF-beta and promotes tumor invasion and angiogenesis,” Genes Dev., 2000, vol. 14, pp. 163-176.
Zhao et al., “Activation of pro-gelatinase B by endometase/matrilysin-2 promotes invasion of human prostate cancer cells,” J. Biol. Chem., Apr. 25, 2003, vol. 278(17), pp. 15056-15064.
International Search Report and Written Opinion from corresponding International Application No. PCT/US09/35840, dated Jun. 1, 2009.
Bergers et al., “Extrinsic Regulators of Epithelial Tumor Progression: Metalloproteinases”, Current Opinion in Genetics and Development, 10:120-127, 2000.
Nagase et al., “Nomenclature and Glossary of the Matrix Metalloproteinases”, Matrix, Supplemental No. 1:421-424, 1992.
Itoh, “MT1-MMP: A Key Regulator of Cell Migration in Tissue”, IUBMB Life, 58(10):589-596, Oct. 2006.
Jiang et al., “Expression of Membrane Type-1 Matrix Metalloproteinase, MT1-MMP in Human Breast Cancer and its Impact on Invasiveness of Breast Cancer Cells”, Int. J. Mol. Med., 17:583-590, 2006.
Paquette et al., “In Vitro Irradiation of Basement Membrane Enhances the Invasiveness of Breast Cancer Cells”, British Journal of Cancer, 97:1505-1512, 2007.
Shinoda et al., “A Novel Matrix Metalloproteinase Inhibitor, FYK-1388 Suppresses Tumor Growth, Metastasis and Angiogenesis by Human Fibrosarcoma Cell Line”, Int'l Journal of Oncology, 22:281-288, 2003.
Choi et al., “Expression of Matrix Metalloproteinases in the Muscle of Patients with Inflammatory Myopathies”, Neurology, vol. 54, Issue 1, Jan. 2000.
Andrews et al., “Gelatinase B (MMP-9) is not essential in the normal kidney and does not influence progression of renal disease in a mouse model of Alport syndrome,” Am. J. Pathol., Jul. 2000, vol. 157(1), pp. 303-311.
Buisson-Legendre et al., “Relationship Between Cell-Associated Matrix Metalloproteinase 9 and Psoriatic Keratinocyte Growth,” Journal of Investigative Dermatology, 2000, vol. 115, pp. 213-218.
Collier et al., “On the structure and chromosome location of the 72- and 92-kDa human type IV collagenase genes,” Genomics, 1991, vol. 9, pp. 429-434.
Coussens et al., “MMP-9 supplied by bone marrow-derived cells contributes to skin carcinogenesis,” Cell, 2000, vol. 103, pp. 481, 490.
Davis et al., “Matrix metalloproteinase-1 and -9 activation by plasmin regulates a novel endothelial cell-mediated mechanism of collagen gel contraction and capillary tube regression in three-dimensional collagen matrices,” J. Cell. Sci., Mar. 2001, vol. 114(Pt. 5), pp. 917-930.
Di Carlo et al., “Urinary gelatinase activities (matrix metalloproteinases 2 and 9) in human bladder tumors,” Oncol. Rep., 2006, vol. 15, pp. 1321-1326.
Dubois et al., Resistance of young gelatinase B-deficient mice to experimental autoimmune encephalomyelitis and necrotizing tail lesions, 1999, J. Clin. Invest. vol. 104, pp. 1507-1515.
Gijbels et al., “Gelatinase in the cerebrospinal fluid of patients with multiple sclerosis and other inflammatory neurological disorders,” J. Neuroimmun. 1992, vol. 41, p. 29-34.
Gijbels et al., “Gelatinase B is present in the cerebrospinal fluid during experimental autoimmune encephalomyelitis and cleaves myelin basic protein,” J. Neurosci. Res., 1993, vol. 36, pp. 432-440.
Gu et al., “S-nitrosylation of matrix metalloproteinases: signaling pathway to neuronal cell death,” Science, 2002, vol. 297, pp. 1186-1190.
Gursoy-Ozdemir et al., Cortical spreading depression activates and upregulates MMP-9, J. Clin. Invest. 2004, vol. 113, pp. 1447-1455.
Graubert et al., “Cloning and Expression of the cDNA Encoding Mouse Neutrophil Gelatinase: Demonstration of Coordinate Secondary Granule Protein Gene Expression During Terminal Neutrophil Maturation,” Blood, Nov. 15, 1993, vol. 82, No. 10, pp. 3192-3197.
Hayashidani et al., “Targeted deletion of MMP-2 attenuates early LV rupture and late remodeling after experimental myocardial infarction,” 2003, Am. J. Physiol. Heart Circ. Physiol. vol. 285, pp. H1229-H1235.
Heymans et al., “Loss or inhibition of uPA or MMP-9 attenuates LV remodeling and dysfunction after acute pressure overload in mice,” 2005, Am. J. Pathol., vol. 166, pp. 15-25.
Heymans et al., “Inhibition of plasminogen activators or matrix metalloproteinases prevents cardiac rupture but impairs therapeutic angiogenesis and causes cardiac failure,” Nat. Med., 1999, vol. 5, pp. 1135-1142.
Heymans et al., “Inhibition of urokinase-type plasminogen activator or matrix metalloproteinases prevents cardiace injury and dysfunction during viral myocarditis,” 2006, Circulation, vol. 114, pp. 565-573.
Heissig et al., Recruitment of stem and progenitor cells from the bone marrow niche requires MMP-9 mediated release of Kit-ligand, Cell, 2002, vol. 109, pp. 625-637.
Huhtala et al., Complete structure of the human gene for 92-kDa type IV collagenase: divergent regulation of expression for the 92- and 72-kilodalton enzyme genes in HT-1080 cells, J. Biol. Chem., 1991, vol. 266, pp. 16485-16490.
Hudson et al., “Effects of selective matrix metalloproteinase inhibitor (PG-116800) to prevent ventricular remodeling after myocardial infarction: results of the PREMIER (Prevention of Myocardial Infarction Early Remodeling) trial,” J. Am. Coll. Cardiol., 2006, vol. 48, pp. 15-20.
Johnson et al., “Matrix metalloproteinase-2 and -9 differentially regulate smooth muscle cell migration and cell-mediated collagen organization,” Arterioscler Thromb Vasc. Biol., 2004, vol. 24, pp. 54-60.
Kaliski et al., “Angiogenesis and tumor growth inhibition by a matrix metalloproteinase inhibitor targeting radiation-induced invasion,” M
Buckler David
Cohen Edward H.
Devy Laetitia
Duffy Brad
Dyax Corp.
Lando & Anastasi LLP
Yu Misook
LandOfFree
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