Drug – bio-affecting and body treating compositions – Designated organic active ingredient containing – Peptide containing doai
Reexamination Certificate
2003-06-04
2008-05-27
Monshipouri, Maryam (Department: 1656)
Drug, bio-affecting and body treating compositions
Designated organic active ingredient containing
Peptide containing doai
C530S380000, C530S350000, C435S013000
Reexamination Certificate
active
07378393
ABSTRACT:
Novel recombinant anticoagulation proteins, methods of their use and methods of their production are described. In particular, recombinant fusions of annexin V (ANV) and Kunitz protease inhibitors (KPI) that possess potent anticoagulant activity are provided. The fusions, abbreviated ANV:KPI, utilize ANV having high affinity for phosphatidyl-L-serine with various KPI's to target serine proteases in membrane-associated coagulation complexes in the blood coagulation cascade. ANV:KPIs are potentially useful antithrombotic drugs permitting localized passivation of thrombogenic vessel walls and associated thrombi.
REFERENCES:
patent: 0965597 (1999-12-01), None
patent: WO 88/07676 (1998-10-01), None
Kohler et al., Biochemisrty, 36(26), 8189-8194, 1997.
Bach et al., Expression of tissue factor procoagulant activity: Regulation by cytosolic calcium. Proc Natl Acad Sci USA 1990; 87: 6995-9.
Bevers et al., Generation of prothrombin-converting activity and the exposure of phosphotidylserine at the outer surface of platelets. Eur J Biochem 1982; 122: 429-36.
Bombeli et al., Apoptotic vascular endothelial cells become procoagulant. Blood 1997; 89: 2429-42.
Broze, Tissue factor pathway inhibitor and the current concept of blood coagulation. Blood Coagul Fibrinol 1995; 6: 7-13.
Chase et al., Titration of trypsin, plasmin, and thrombin withp-nitrophenylp′-guanidinobenzoate HCI. Methods Enzymol 1970; 19: 20-7.
Dachary-Prigent et al., Physiopathological significance of catalytic phospholipids in the generation of thrombin. Sem Thromb Hemost 1996; 22: 157-64.
Dennis et al., Kunitz domain inhibitors of tissue factor-factor VIIa. I. Potent inhibitors selected from libraries by phage display. J Biol Chem 1994; 269: 22129-36.
Dennis et al., Kunitz domain inhibitors of tissue factor-factor VIIa. II. Potent and specific inhibitors by competitive phage selection. J Biol Chem 1994; 269: 22137-44.
Diaz-Collier et al., Refold and characterization of recombinant tissue factor pathway inhibitor expressed inE. coli. Thromb Haemost 1994; 71: 339-46.
Franssen et al., Prothrombinase is protected from inactivation by tissue factor pathway inhibitor: competition between prothrombin and inhibitor. Biochem J 1997; 323: 33-7.
Gill et al., Calculation of protein extinction coefficients from amino acid sequence data. Anal Biochem 1989; 182: 319-26.
Girard et al., Inhibition of factor VIIa-tissue factor coagulation activity by a hybrid protein. Science 1990; 248: 1421-4.
Greeno et al., Apoptosis is associated with increased cell surface tissue factor procoagulant activity. Lab Invest 1996; 75: 281-9.
Hansen et al., Discordant expression of tissue factor and its activity in polarized epithelial cells. Asymmetry in anionic phospholipid availability as a possible explanation. Blood 1999; 94: 1657-64.
Haskel et al., Prevention of arterial reocclusion after thrombolysis with recombinant lipoprotein-associated coagulation inhibitor. Circulation 1991; 84: 821-7.
Hoffman et al., Factors IXa and Xa play distinct roles in tissue factor-dependent initiation of coagulation. Blood 1995; 86:1794-801.
Jang et al., Influence of blockade at specific levels of the coagulation cascade on restenosis in a rabbit atherosclerotic femoral artery injury model. Circulation 1995; 92: 3041-50.
Kinsky, Preparation of liposomes and a spectrometric assay for release of trapped glucose marker. Methods Enzymol. 1974; 32: 501-514.
Krishnaswamy et al., Role of the membrane surface in the activation of human coagulation factor X. J Biol Chem 1992; 267: 26110-20.
Le et al., Studies of the mechanism for enhanced cell surface factor VIIa/tissue factor activation of factor X on fibroblast monolayers after their exposure to N-ethylmaleimide. Thromb Haemost 1994; 72: 848-55.
Lefovits et al., Selection inhibition of factor Xa is more efficient that factor VIII tissue factor complex blockade at facilitating coronary thrombolysis in the canine model. J. Am. Coll. Cardiol. 1996; 28: 1858-65.
McGrath et al., Ecotin: lessons on survival in a protease-filled world. Protein Sci 1995; 4:141-8.
Mahdi et al., Protease nexin-2/amyloid beta-protein precursor inhibits factor Xa in the prothrombinase complex. J Biol Chem 1995; 270: 23468-74.
Mahdi et al., Protease nexin-2/amyloid □-protein precursor regulates factor VIIa and the factor VIIa-tissue factor complex. Thromb Res 2000; 99: 267-76.
Mann, Biochemistry and physiology of blood coagulation. Thromb Haemost 1999; 82: 165-74.
Mast et al., Physiological concentrations of tissue factor pathway inhibitor do not inhibit prothrombinase. Blood 1996; 87: 1845-50.
Monroe et al., The factor VII-platelet interplay: effectiveness of recombinant factor VIIa in the treatment of bleeding in severe thrombocytopathia. Sem Thromb Haemost 2000; 26: 373-7.
Morrisey, Tissue factor: An enzyme cofactor and a true receptor. Thromb Haemost 2001; 86: 66-74.
Neeper et al., Characterization of recombinant tick anticoagulant peptide. J. Biol. Chem. 1990; 265: 17446-52.
Petersen et al., Inhibitory properties of separate recombinant Kunitz-type-protease-inhibitor domains from tissue factor pathway inhibitor. Eur J Biochem 1996; 235, 310-6.
Rand et al., Blood clotting in minimally altered whole blood. Blood 1996; 88: 3432-45.
Reutelingsperger et al., Annexin V, the regulator of phosphatidylserine-catalyzed inflammation and coagulation. during apoptosis. Cell Mol Life Sci 1997; 53: 527-32.
Romisch et al., In vivo antithrombotic potency of placenta protein 4 (annexin V). Thromb Res 1991; 61: 93-104.
Schmaier et al., Factor IXa inhibition by protease nexin-2/amyloid beta-protein precursor on phospholipid vesicles and cell membranes. Biochemistry 1995; 34: 1171-8.
Schmaier et al., Protease Nexin-2/Amyloid β protein precursor. A tight-binding inhibitor of coagulation factor IXa. J Clin Invest 1993; 2540-5.
Scorer et al., Rapid selection using G418 of high copy number transformants ofPichia pastorisfor high-level foreign gene expression. Biotechnology 1994; 12: 181-4.
Shi, Lactadherin inhibits enzyme complexes of blood coagulation by competing for phospholipid-binding sites. Blood 2003; 101:2628-36.
Sims et al., Unraveling the mysteries of phospholipid scrambling. Thromb Haemost 2001; 86: 266-75.
Smith, Titration of activated bovine factor X. J Biol Chem 1973; 248: 2418-23.
Smith et al., Platelet coagulation factor XIa inhibitor, a form of Alzheimer amyloid precursor protein. Science 1990; 248: 1126-8.
Stanssens et al., Anticoagulant repertoire of the hookwormAncylostoma caninum. Proc Natl Acad Sci USA 1996; 93: 2149-54.
Stassen et al., Characterization of a novel series of aprotinin-derived anticoagulants. I. In vitro and pharmacological properties. Thromb Haemost 1995; 74: 646-54.
Stassen et al., Characterization of a novel series of aprotinin-derived anticoagulants. II. Comparative antithrombotic effects on primary thrombus formation in vivo. Thromb Haemost 1995; 74: 655-59.
Tait et al., Evaluation of annexin V as a platelet-directed thrombus targeting agent. Thromb Res 1994; 75: 491-501.
Thiagarajan et al., Inhibition of arterial thrombosis by recombinant annexin V in a rabbit carotid artery injury model. Circulation 1997; 96: 2339-47.
Tuszynski et al., Isolation and characterization of antistasin. J Biol Chem 1987: 262: 9718-23.
Van Ryn et al., The effect of heparin and annexin V on fibrin accretion after injury in the jugular vein of rabbit. Thromb Haemost 1993; 69: 227-30.
Waxman et al., Tick anticoagulant peptide is a novel inhibitor of blood coagulation facter Xa. Science 1990; 248: 593-6.
Wun et al., Comparison of recombinant tissue factor pathway inhibitors expressed in human SK hepatoma, mouse C127, baby hamster kidney, and Chinese hamster ovary cells. Thromb Haemost 1992; 68: 54-9.
Zwaal et al., Lipid-protein interactions in blood coagulation. Biochim Biophys Acta 1998; 1376: 433-53.
Zwaal et al., Pathophysiological implications of membrane phospholipid asymmetry in blood cells. Blood 1997; 89: 1121-32.
EMBL Database No. A01769 for “DNA Sequence (gaa) for Vascular Anticoagulating Protein,” 1993, 2 pages retriev
Monshipouri Maryam
Sonnenschein Nath and Rosenthal LLP
LandOfFree
Recombinant anticoagulant proteins does not yet have a rating. At this time, there are no reviews or comments for this patent.
If you have personal experience with Recombinant anticoagulant proteins, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Recombinant anticoagulant proteins will most certainly appreciate the feedback.
Profile ID: LFUS-PAI-O-3981905