Organic compounds -- part of the class 532-570 series – Organic compounds – Carbohydrates or derivatives
Reexamination Certificate
2006-04-18
2006-04-18
Helms, Larry R. (Department: 1642)
Organic compounds -- part of the class 532-570 series
Organic compounds
Carbohydrates or derivatives
C435S320100, C435S325000, C435S069100
Reexamination Certificate
active
07030231
ABSTRACT:
This invention provides a novel membrane-type serine protease (designated MT-SP1) elevated expression of which is associated with cancer. In one embodiment, this invention provides a method obtaining a prognosis or of detecting or staging a cancer in an organism. The method involves providing a biological sample from the organism and detecting the level of a membrane type serine protease 1 (MT-SP1) in the sample, where an elevated level of the membrane-type serine protease, as compared to the level of the protease in a biological sample from a normal healthy organism indicates the presence or stage of the cancer.
REFERENCES:
patent: 5482848 (1996-01-01), Dickson et al.
patent: 5972616 (1999-10-01), O'Brien et al.
patent: WO-99/42120 (1999-08-01), None
Perona and Craik “Structural basis of substrate specificity in the serine proteases”Protein Science(1995) 4:337-360.
Bork and Beckmann “A Widespread Module in Developmentally Regulated Proteins”J. Mol. Biol.(1993) 231:539-545.
Ishibashi, et al. “Sp1 Decoy Transfected to Carcinoma Cells Suppresses the Expression of Vascular Endothelial Growth Factor, Transforming Growth Factor β1, and Tissue Factor and Also Cell Growth and Invasion Activities”Cancer Res.(2000) 60(20):6531-6536.
Kang, et al. “Identification of cDNAs encoding two novel rat pancreatic serine proteases”Gene(1992) 110:181-187.
Kim, et al. “Cloning and chromosomal mapping of gene isolated from thymic stromal cells encoding a new mouse type II membrane serine protease, epithin, containing four LDL receptor modules and two CUB domains”Immunogenetics(1999) 49:420-428.
Kitamoto, et al. “Enterokinase, the initiator of intestinal digestion, is a mosaic protease composed of a distinctive assortment of domains”Proc. Natl. Acad. Sci. (1994) 91:7588-7592.
Krieger and Herz “Structures and Functions of Multiligand Liprotein Receptors: Macrophage Scavenger Receptors and LDL Receptor-Related Protein (LRP)”Annu. Rev. Biochem. (1994) 63:601-637.
Leytus, et al. “A Novel Trypsin-like Serine Protease (Hepsin) with a Putative Transmembrane Domain Expressed by Human Liver and Hepatoma Cells”Biochemistry(1988) 27:1067-1074.
Paoloni-Giacobino, et al. “Cloning of the TMPRSS2 Gene, Which Encodes a Novel Serine Protease with Transmembrane LDLRA, and SRCR Domains and Maps to 21q22.3”Genomics(1997) 44:309-320.
Perona and Craik “Evolutionary Divergence of Substrate Specificity within the Chymotrypsin-like Serine Protease Fold”J. Biol. Chem. (1997) 272:29987-29990.
Sakanari, et al. “Serine proteases from nematode and protozoan parasites: Isolation of sequence homologs using generic molecular probes”Proc. Natl. Acad. Sci. (1989) 86:4863-4867.
Takeuchi, et al. “Reverse biochemistry: Use of macromolecular protease inhibitors to dissect complex biological processes and identify a membrane-type serine protease in epithelial cancer and normal tissue”Proc. Natl. Acad. Sci. (1999) 96(20):11054-11061.
Takeuchi, et al. “Cellular Localization of Membrane-type Serine Protease 1 and Identification of Protease-activated receptor-2 and Single-chain Urokinase-type Plasminogen Activator as Substrates”J. Biol. Chem. (2000) 275(34):26333-26342.
Wiegand, et al. “Cloning of cDNA encoding human brain trypsinogen and characterization of its product”Gene(1993) 136:167-175.
Yamada, et al. “Isolation and characterization of three novel serine protease genes fromXenopus laevis” Gene(2000) 252:209-216.
Yamaoka, et al. “Cloning and Characterization of the cDNA for Human Airway Trypsin-like Protease”J. Biol. Chem. (1998) 273:11895-11901.
Lin, et al. “Purification and Characterization of a Complex Containing Matriptase and a Kunitz-type Serine Protease Inhibitor from Human Milk”J. Biol. Chem. (1999) 274:18237-18242.
EST Accession No. aa459076.
EST Accession No. aa219372.
EST Accession No. w39209.
GenBank Accession No. U20428.
Lin et al. “Purification and Characterization of a Complex Containing Matriptase and a Kunitz-type Serine Protease Inhibitor from Human Milk”, J. Biol. Chem. vol. 274, No. 28, pp. 18237-18242 Jun. 1999.
Yamaoka et al. “Cloning and Characterization of the cDNA for Human Airway Trypsin-like Protease”, J. Biol. Chem. vol. 273, No. 19, pp. 11895-11901 May 1998.
Perona et al. “Structural Basis of Substrate Specificity in the Serine Proteases”, Protein Science, Cambridge University Press, No. 4, pp. 337-360 (1995).
Bork et al. “The CUB Domain: A Widespread Module in Developmentally Regulated Proteins”, J. Med. Biol. pp. 539-545 (1993).
Ishibashi et al. “Sp1 Decoy Transfected to Charcinoma Cells Suppresses the Expression of Vascular Endothelial Growth Factor, Transforming Growth Factor B1, and Tissue Factor and Also Cell Growth and Invasion Activities” Cancer Research No. 60, pp. 6531-6536 Nov. 2000.
Kang et al. “Identification of cDNAs Encoding Two Novel Rat Pancreatic Serine Proteases”, Gene, No. 110, pp. 181-187, (1992).
Kim et al. “Cloning and Chromosomal Mapping of a Gene Isolated from Thymic Stromal Cells Encoding a New Mouse Type II Membrane Serine Protease, Epithin, Containing Four LDL Receptor Modules and Two CUB Domains”, Immunogenetics (1999) 49: 420-428.
Kitamoto et al. “Enterokinase, the Initiator of Intestinal Digestion , is a Mosaic Protease Composed of a Distinctive Assorment of Domains”, Proc. Natl. Acad. Sci. (1994) 91: 7588-7592.
Kreiger et al. Structures and Functions of Multiligand Lipoprotein Receptors: Macrophase Scavenger Receptors and LDL Receptor-Related Protein (LRP) Annu. Rev. Biochem. (1994) 63: 601-637.
Leytus et al. “A Novel Trypsin-like Serine Protease (Hepsin) with a Putative Transmembrane Domain Expressed by Human Liver and Hepatoma Cells”, Biochemistry (1988) 27: 1067-1074.
Paoloni-Giacobino et al. “Cloning of the TMPRSS2 Gene, Which Encodes a Novel Serine Protease with Transmembrane, LDLRA, and SRCR Domains And Maps to 21q22.3” Genomics (1997) 44: 309-320.
Perona et al. “Evolutionary Divergence of Substrate Specificity within the Chymotrypsin-like Serine Protease Fold”, J. Biol. Chem. (1997) 272: 29987-29990.
Sakanari et al. “Serine Proteases from Nematode and Protozoan Parasites: Isolation of Sequence Homologs Using Generic Molecular Probes”, Proc. Natl. Acad. Sci. (1989) 86: 4863-4867.
Takeuchi et al. “Reverse Biochemisrty: Use of Macromolecular Protease Inhibitors to Dissect Complex Biological Processes and Identify a Membrane-Type Serine Protease in Epithelial Cancer and Normal Tissue”, Proc. Natl. Acad. Sci. (1999) 96: 11054-11061.
Takeuchi et al. “Cellular Localization of Membrane-type Serine Protease 1 and Identification of Protease-activated Receptor-2 and Single-chain Urokinase-type Plasminogen Activator as Substrates”, J. Biol. Chem. (2000) 275: 34: 26333-26342.
Wiegand et al. “Cloning of the cDNA Encoding Human Brain Trysinogen and Characterization of its Product”, Gene (1993) 136: 167-175.
Yamada et al. “Isolation and Charaterization of Three Novel Serine Protease Genes From Xenopus Laevis”, Gene (2000) 209-216.
Lin et al. “Molecular Cloning of cDNA for Matriptase, a Metrix-degrading Serine Protease with Trypsin-like Activity”, J. Biol. Chem. (1999) 274: 26: 18231-18236.
Craik Charles S.
Shuman Marc
Takeuchi Toshihiko
Catalyst Biosciences, Inc.
Helms Larry R.
Wilson Sonsini Goodrich & Rosati
Yu Misook
LandOfFree
Membrane type serine protease 1 (MT-SP1) and uses thereof does not yet have a rating. At this time, there are no reviews or comments for this patent.
If you have personal experience with Membrane type serine protease 1 (MT-SP1) and uses thereof, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Membrane type serine protease 1 (MT-SP1) and uses thereof will most certainly appreciate the feedback.
Profile ID: LFUS-PAI-O-3528822