Chemistry: molecular biology and microbiology – Micro-organism – tissue cell culture or enzyme using process... – Recombinant dna technique included in method of making a...
Reexamination Certificate
2006-04-18
2006-04-18
Wax, Robert A. (Department: 1653)
Chemistry: molecular biology and microbiology
Micro-organism, tissue cell culture or enzyme using process...
Recombinant dna technique included in method of making a...
C435S007100, C530S350000
Reexamination Certificate
active
07029877
ABSTRACT:
There is provided a protease inhibitor and a method of inhibiting a protease selected from the group consisting of thrombin, chymotrypsin and neuropsin, by contacting the protease with an effective amount of a member of the phosphoethanolamine binding protein (PEBP) family.
REFERENCES:
patent: 0 628 631 (1994-12-01), None
patent: 0 965 597 (1999-12-01), None
patent: 5 092 993 (1993-04-01), None
patent: WO 96 29347 (1996-09-01), None
Matsukkawa et al., “Increased Expression of Hippocampal Cholinergic Neurostimulating Peptide-Related Components and their Messenger RNAS in the Hippocampus of Aged Senescence-Accelerated Mice”, Neuroscience, vol. 88, No. 1, pp. 79-92, (1999).
Section Ch, Week 199320, Derwent Publications Ltd., London, GB; Class BO4, An 1993-162126 XP002201326 & JP 05 092993 A (Tosoh Corp, 1993—Abstract).
EBI; Sequence ID PEBP—MOUSE, (1997), Lin and Frischauf, Database accession No. P70296 XP002201325—Abstract.
Bruun et al.,, “A high-Affinity Inhibitor of Yeast Carboxypeptidase Y is Encoded by TFS1 and Shows Homology to a Family of Lipid Binding Proteins”, Biochemistry, vol. 37, No. 10, pp. 3351-3357, (1998).
Banfield et al., “Function from Structure? The Crystal Structure of Human Phosphatidylethanolamine-binding protein Suggests a Role in Membrane Signal Transduction”, Structure, vol. 6, No. 10, pp. 1245-1254, (1998).
Hengst Ulrich et al., “The Phosphatidylethanolamine-Binding Protein is a Prototype of a Novel Family of Serine Protease Inhibitors”, Journal of Biological Chemistry, vol. 276, No. 1, pp. 535-540, (2001).
Turgeon et al., “The Role of Thrombin-Like (serine) Proteases in the Development, Plasticity and Pathology of the Nervous System”, Brain Research Reviews, vol. 25, pp. 85-95, (1997).
Wagner et al., “Protease Nexin-1, an Antithrombin with Neurite Outgrowth Activity, is Reduced in Alzheimer Disease”, Proc. Natl. Acad. Sci. USA, vol. 86, pp. 8284-8288, (1989).
Davies et al., “Serine Proteases in Rodent Hippocampus”, The Journal of Biological Chemistry, vol. 273, No. 36, pp. 23044-23011, (1998).
Gloor et al., “A Gilla Derived Neurite Promoting Factor with Protease Inhibitory Activity Belongs to the Protease.Nexins”, Cell, vol., 47, pp. 687-693, (1986).
Stone et al., “Glial-Derived Neurite-Promoting Factor is a Slow-Binding Inhibitor of Trypsin, Thrombin and Urokinase”, Archives of Biochemistry and Biophysics, vol. 252, No. 1, pp. 237-244, (1987).
Monard et al., “Inhibition of Protease Activity Can Lead to Neurite Extension in Neuroblastoma Cells”, Friedrich Miescher-Institut and Department of Biology and Center for Cancer Research, pp. 359-364.
Gurwitz et al., “Thrombin Modulates and Reverses Neuroblastoma Neurite Outgrowth”, Proc. Natl. Acad. Sci. USA, vol. 85, pp. 3440-3444, (1988).
Zurn et al., “A Glia-Derived Nexin Promotes Neurite Outgrowth in Cultured Chick Sympathetic Neurons”, Dev. Neurosci., vol. 10, pp. 17-24, (1988).
Farmer et al., “Glia-Derived Nexin Potentiates Neurite Extension in Hippocampal Pyramidal Cells in Vitro”, Dev. Neurosci., vol., 12, pp. 73-80. (1990).
Cavanaugh et al., “Reciprocal Modulationof Astrocyte Stellation by Thrombin and Protease Nexin-1”, Journal of Neurochemistry, vol., 54, No. pp. 1735-1743, (1990).
Meier et al., “Induction of Glia-Derived Nexin After Lesion of a Peripheral never”, Letters to Nature, vol. 342, pp. 548-550, (1989).
Hoffmann et al., “The Prolonged Presence of Glia-Derived Nexin, an Endogenous Protease Inhibitor, in the Hippocampus after Ischemia-Induced Delayed Neuronal Death”, Neuroscience, vol. 49, No. 2, pp. 397-408, (1992).
Luthi et al, “Endogenous Serine Protease Inhibitor Modulates Epileptic Activity and Hippocampal Long-Term Potentiation”, The Journal of Neuroscience, vol. 17, No. 12, pp. 4688-4699, (1997).
Wolfgang J. Rettig, “Carboxypeptidase C Including Carboxypeptidase Y”, Oncology Research, pp. 389-393.
Schoentgen et al., “From Structure to Function: Possible Biological Roles of a new Widespread Protein Family Binding Hydrophobic Ligands and Displaying a Nucleotide Binding Site”, FEBS Letters, vol. 369, pp. 22-26, (1995).
Bernier et al., “Purification and Characterization of Basic 23 kDa Cytosolic Protein From Bovine Brain”, Biochemica et Biophysica Acta., vol. 790, pp. 174-181, (1984).
Bernier et al., “Ligand Binding Studies with a 23 kDa Protein Purified from Bovine Brain Cytosol”, Biochemica et Biophysica Acta, vol. 871, pp. 19-23, (1986).
Bucquoy et al., “Relationships between Molecular Interactions (Nucleotides, Lipids and Proteins) and Structural Features of the Bovine Brain 21-kDa Protein”, Eur. J. Biochem, vol. 225, pp. 1203-1210, (1994).
Bollengier et al., “Isolation and Partial Biochemical characterization of an Unknown Polypeptide from White and Grey Brain Material”, Neuropeptides, vol. 1, pp. 119-135, (1980).
Seddiqi et al, “Amino Acid Sequence of the Homo Sapiens Brain 21-23 kDa Protein (Neuropolypeptide h3), Comparison with its Counterparts fromRattus NorvegicusandBos TeurusSpecies, and Expression of its mRNA in Different Tissues”, J. Mol. Evol. vol. 39, pp. 655-660, (1994).
Schoentgen et al., “Complete Amino Acid Sequence of Basic 21-kDa Proteins from Bovine Brian Cytosol”, Eur. J. Biochem, vol. 166, pp. 333-338, (1987).
Grandy et al., “Purification, Cloning, and Tissue Distribution of a 23-kDa Rat Protein Isolated by Morphine Affinity Chromatography”, Molecular Endocrinology, vol. 4, No. 9, pp. 1370-1376, (1990).
Araki et al., “Isolation and Characterization of a 25-Kilodalton Protein from Mouse Testis: Sequence Homology with a Phospholipid-Biding Protein”, Biology of Reproduction, vol. 47, pp. 832-843, (1992).
Perry et al., “Sequence Analysis of a Mammalian Phospholipid-Binding Protein from Testis and Epididymis and Its Distribution Between Spermatozoa and Extracellular Secretions”, Biochem. J., vol. 301, pp. 235-242, (1994).
Pikielny et al., “Members of a Family of Drosphila Putative Odorant-Binding Proteins are Expressed in Different Subsets of Olfactory Hairs”, Neuron, vol. 12, pp. 35-49, (1994).
Trottein et al., “The Primary Structure of a Putative Phosphatidylethanolamine-Binding Protein fromPlasmodium Falciparum”, Molecular and Biochemical Parasitology, vol. 70, pp. 235-239, (1995).
Lobos et al., “Identification of anOnchocerca volvuluscDNA Enconding a Low-Molecular-Weight Antigen Uniquely Recognized by Onchocerciasis Patient Sera”, Molecular and Biochemical Parasitology, vol. 39, pp. 135-146, (1990).
Gems et al., “An Abundant, Trans-Spliced mRNA from Toxocara Canis Infective Larvae Encodes a 26-kDa Protein with Homology to Phosphatidylethanolamine-Binding Proteins”, The Journal of Biological Chemistry, vol. 270, No. 31, pp. 18517-18522, (1995).
Robinson et al., “TFS1: A Suppressor ofcdc25Mutations onSaccharomyces cerevisiae”, Mol Gen Genet, vol. 230, pp. 241-250, (1991).
Ohshima et al., “Cloning and Molecular Analysis of the Arabidopsis Gene Terminal Flower 1”, vol. 254, pp. 186-194, (1997).
Kardailsky et al., “Activation Tagging of the Floral InducerFT”, vol. 286, pp. 1962-1965, (1999).
Kobayashi et al., “A Pair of Related Genes with Antagonistic Roles in Mediating Flowering Signals”, vol. 286, pp. 1960-1962, (1999).
Bradley et al., “Crontrol of Inflorescence Architecture in Antirrhinum”, Nature, vol. 379, pp. 791-797, (1996).
Serre et al., “Crystal Structure of the Phosphatidylethanolamine-Binding Protein from Bovine Brain: A Novel Structural Class of Phospholipid-Binding Proteins”, Structure, vol. 6, pp. 1255-1265, (1998).
Ojika et al., “Hippocampal cholinergic Neurostimulating Peptides (HCNP)”, Progre
Albrecht Hugo
Hengst Ulrich
Monard Denis
Mayer Suzanne M.
Novartis Forschungsstiftung Zweigniederlassung Friedrich Miesche
Prince John
LandOfFree
Methods and reagents for protease inhibition does not yet have a rating. At this time, there are no reviews or comments for this patent.
If you have personal experience with Methods and reagents for protease inhibition, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Methods and reagents for protease inhibition will most certainly appreciate the feedback.
Profile ID: LFUS-PAI-O-3599949