Chemistry: molecular biology and microbiology – Measuring or testing process involving enzymes or... – Involving antigen-antibody binding – specific binding protein...
Reexamination Certificate
2007-01-30
2007-01-30
Spector, Lorraine (Department: 1646)
Chemistry: molecular biology and microbiology
Measuring or testing process involving enzymes or...
Involving antigen-antibody binding, specific binding protein...
C435S007920, C435S007100, C530S350000, C530S381000, C530S395000, C514S802000, C514S822000
Reexamination Certificate
active
10028741
ABSTRACT:
The assay of soluble endothelial protein C receptor (sEPCR) is useful to monitor effective thrombin levels and a hypercoagulable state. An assay for sEPCR is therefore useful to monitor ongoing effectiveness of anticoagulant therapy. A sEPCR ELISA assay is particularly useful for this purpose. A state of hypercoagulability in patients or normal individuals can also be identified by such an assay.
REFERENCES:
patent: 5804392 (1998-09-01), Esmon et al.
patent: 5935802 (1999-08-01), Lind
patent: 5981285 (1999-11-01), Carroll et al.
patent: 6037450 (2000-03-01), Esmon et al.
patent: WO 96/05303 (1996-02-01), None
Esmon et al., Endothelial protein C receptor, Thromb. Haemost. (Aug. 1999) 82(2):251-258.
Wu et al., Detection of soluble endothelial protein C receptor (sEPCR) in patients with CHD, DM, and SLE, Chung-Hua Hsueh Yeh Hsueh Tsa Chih [Chinese Journal of Hematology] (Sep. 2000) 21(9):472-474.
Esmon. CT, The endothelial cell protein C receptor, Thromb. Haemost. (May 2000) 83(5):639-643.
Stearns-Kurosawa et al., Plasma levels of endothelial protein C receptor respond to anticoagulant treatment, Hemost. Thromb. Vasc. Biol. (Jan. 15, 2002) 99(2):526-530.
Stearns-Kurosawa et al. Bimodal distribution of soluble endothelial protein C receptor levels in healthy populations, J. Thromb. Haemost (Apr. 2003) 1(4):855-856.
Debeir et al., (1997) Pharmacological characterization of protease-activated receptor (APR-1) in rat astrocytes, Eur. J. Pharm. 323:111-117.
Breckenridge, “Oral Anticoagulant Drugs: Pharmacokinetic Aspects,”Semin. Hematol., 15:19-26, 1978.
Esmon, “Natural Anticoagulants and Their Pathways,” inHandbook of Experimental Pharmacology, ed: Born et al., Springer-Verlag, New York; pp. 447-476, 1999.
Fukudome and Esmon, “Identification, cloning, and regulation of a novel endothelial cell protein C/activated protein C receptor,”J. Biol. Chem. 269:26486-26491, 1994.
Fukudome et al., “The endothelial cell protien C receptor. Cell surface expression and direct ligand binding by the soluble receptor,”J Biol Chem., 271(29):17491-17498, 1996.
Goldstein et al., “Is Glycohemoglobin Testing Useful in Diabetes Mellitis? Lessons from the Diabetes Control and Complications Trial,”Clin. Chem., 40:1637-1640, 1994.
Hrish et al., “Oral Anticoagulants: Mechanisms of Action, Clinical Effectiveness and Optimal Therapeutic Range,”Chest, 114 Supp. 445S-469S, 1998.
Kurosawa et al., “Identification of Functional Endothelial Protein C Receptor in Plasma,”J. Clin. Invest., 100:411-418, 1997.
Kurosawa et al., “Plasma Levels of Endothelial Protein C Receptor are Elevated in Patients with Sepsis and Systemic Lupus Erythmatosus: Lack of Correlation with Thrombomodulin Suggests Different Pathological Processes,”Blood, 91:725-727, 1998.
O'Reilly, “Vitamin K and the Oral Anticoagulant Drugs,”Annu. Rev. Med., 27:245-261, 1976.
Regan et al., “The endothelial cell protein C receptor,”J. Biol. Chem. 271:17499-17503, 1996.
Riley et al., “Clinical Utilization of the International Normalized Ratio (INR),”J. Clin. Lab. Anal., 14:101-114, 2000.
Stearns-Kurosawa et al., “Plasma levels of endothelial protein C receptor respond to anticoagulant treatment,”Blood, 99(2):526-530, 2002.
Stearns-Kurosawa et al., “The endothelial cell protein C receptor augments protein C activation by the thrombin-thrombomodulin complex,”Proc. Nat'l Acad. Sci. USA, 93:10212-10216, 1996.
Sutcliffe et al., “Aspects of Anticoagulant Action: A Review of the Pharmacology, Metabolism and Toxicology of Warfarin and Cogeners,”Rev. Drug Metabol. Drug Interact, 5:225-272, 1987.
Takahashi et al., “Circulating Thrombomodulin as a Novel Endothelial Cell Marker: Comparison of Its Behavior with von Willebrand Factor and Tissue-Type Plasminogen Activator,”Am. J. Hematol., 41:32-39, 1992.
Takano et al., “Plasma Thrombomodulin in Health and Diseases,”Blood, 76:2024-2029, 1990.
Wada et al., “Plasma Thrombomodulin as a Marker of Vascular Disorders in Thrombotic Thrombocytopenic Purpura and Disseminated Intravascular Coagulation,”Am. J. Hematol., 39:20-24, 1992.
Xu et al., “Metalloproteolytic Release of Endothelial Protein C Receptor,”J. Bio. Chem., 275:6038-6044, 2000.
Abraham et al., “Efficacy and safety of monoclonal antibody to human tumor necrosis factor alpha in patients with sepsis syndrome: a randomized, controlled, double-blind, multicenter clinical trial,”JAMA, 273(12):934-941, 1995.
Barthold, “‘Muromics’: genomics from the perspective of the laboratory mouse,”Comparative Medicine, 52(3):206-223, 2002.
Coughlin, “Protease-activated receptors in vascular biology,”Thromb. Haemost., 86:296-307, 2001.
Deitch, “Animal models of sepsis and shock: a review and lessons learned,”Shock, 9(1):1-11, 1998.
Fiedler et al., “Monoclonal antibody to tumor necrosis factor-α prevents lethal endotoxin sepsis in adult rhesus monkeys,”J. Lab. Clin. Med., 120:574-588, 1992.
Giudici et al., “Antithrombin replacement in patients with sepsis and septic shock,”Haematologica, 84:452-460, 1999.
Gu et al. “Endotoxin and thrombin elevate rodent endothelial cell protein C receptor mRNA levels and increase receptor shedding in vivo,”Blood, 95(5):1687-1693, 2000.
Hinshaw et al., “Survival of primates in LD100 septic shock following therapy with antibody to tumor necrosis factor (TNFα),”Circulatory Shock, 30:279-292, 1990.
McCloskey et al., “Treatment of septic shock with human monoclonal antibody HA-1A,”Ann. Intern. Med., 121:1-5, 1994.
Minnema et al., “Recombinant human antithromin III improves survival and attenuates inflammatory responses in baboons lethally challenged withEscherichia coli, ” Blood, 95(4):1117-1123, 2000.
Moayeri et al., “Bacillus anthracislethal toxin induces TNF-α-independent hypoxia-mediated toxicity in mice,”J. Clin. Invest., 112(5):670-682, 2003.
Taylor et al., “Antithrombin-III prevents the lethal effects ofEscherichia coliinfusion in baboons,”Circulatory Shock, 26:227-235, 1988.
Tracey et al., “Anti-cachectin/TNF monoclonal antibodies prevent septic shock during lethal bacteraemia,”Nature, 330:662-664, 1987.
Tracey et al., “Cachectin/tumor necrosis factor induces lethal shock and stress hormone responses in the dog,”Surg., Gynec., Obst., 164:415-422, 1987.
Vincent et al., “Clinical trials of immunomodulatory therapies in severe sepsis and septic shock,”CID, 34:1084-1093, 2002.
Zeni et al., “Anti-inflammatory therapies to treat sepsis and septic shock: a reassessment,”Critical Care Medicine, 25(7):1095-1110, 1997.
Kurosawa Shinichiro
Stearns-Kurosawa Deborah J.
Fulbright & Jaworski
Kaufman Claire M.
Oklahoma Medical Research Foundation
Spector Lorraine
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