Drug – bio-affecting and body treating compositions – Antigen – epitope – or other immunospecific immunoeffector – Amino acid sequence disclosed in whole or in part; or...
Reexamination Certificate
2007-12-11
2007-12-11
Chan, Christina (Department: 1644)
Drug, bio-affecting and body treating compositions
Antigen, epitope, or other immunospecific immunoeffector
Amino acid sequence disclosed in whole or in part; or...
C530S350000
Reexamination Certificate
active
11403387
ABSTRACT:
Recombinant plasminogen activator inhibitor-1 (PAI-1) isoforms which lack the reactive center loop and contain the complete heparin-binding domain or lack at least a portion of the heparin-binding domain are described. The rPAI-1 isoforms disclosed herein may be used to modulate angiogenesis through blocking release of VEGF from a VEGF-heparin complex. Furthermore, the rPAI-1 proteins may be used to inhibit cell proliferation and migration, induce apoptosis, and produce proteolytic fragments corresponding to angiostatin kringles 1-3 and kringles 1-4. A truncated proteolytic plasmin protein of 34 kDa is also provided.
REFERENCES:
patent: 5830880 (1998-11-01), Sedlacek et al.
Mulloy et al, Current opinion in Structural Biology 11: 623-628, 2001.
Asano et al., “An Anti-Human VEGF Monoclonal Antibody, MV833, That Exhibits Potent Anti-Tumor Activity In Vivo”, Hybridoma 1998 17(2) :185-190.
Aleshkov et al., “Biochemical and Biophysical Studies of Reactive Center cleaved Plasminogen Activator Inhibitor Type 1”, J. Biol. Chem. 1996 271 (35) :21231-21238.
Bijnens et al., “Expression and Characterization of Recombinant Porcine Plasminogen Activator Inhibitor-1”, Thrombosis and Haemostasis 1997 77(2) :350-356.
Blasi F., “Proteolysis, Cell Adhesion, Chemotaxis, and Invasiveness Are Regulated by the u-PA-u-PAR-PAI-1 System”, Thrombosis and Haemostasis 1999 82(2) :298-304.
Brem et al., Interstitial chemotherapy with drug polymer implants for the treatment of recurrent gliomas, J. Neurosurg 1991 74:441-446.
Bosma et al., “Human Plasminogen Activator Inhibitor-1 Gene”, J. Biol. Chem. 1988 162(19) :9129-9141.
Borgström et al., “Neutralizing Anti-Vascular Endothelial Growth Factor Antibody Completely Inhibits Angiogenesis and Growth of Human Prostate Carcinoma Micro Tumors In Vivo”, The Prostate 1998 35:1-10.
Borgström et al., “Importance of VEGF for Breast Cancer Angiogenesis in Vivo: Implications from Intravital Microscopy of Combination Treatments with an Anti-VEGF Neutralizing Monoclonal Antibody and Doxorubicin”, Anticancer Research 1999 19:4203-4214.
Cao et al., “Kringle Domains of Human Angiostatin”, J. Biol. Chem. 1996 271(46) :29461-29467.
Cao et al., “Suppression of angiogenesis and tumor growth by the inhibitor K1-5 generated by plasmin-mediated proteolysis”, Proc. Natl. Acad. Sci. USA 1999 96:5728-5733.
Chang et al., “Phenotypic expression inE. coliof a DNA sequence coding for mouse dihydrofolate reductase”, Nature 1978 275:617-624.
Chapman et al., “Macrophage Fibrinolytic Activity: Identification of Two Pathways of Plasmin Formation by Intact Cells and of a Plasminogen Activator Inhibitor”, Cell 1982 28(3) :653-662.
Chapman H., “Plasminogen activators, integrins, and the coordinated regulation of cell adhesion and migration”, Current Opinion in Cell Biology 1997 9:714-724.
Clowes et al., “Smooth Muscle Cells Express Urokinase During Mitogenesis and Tissue-Type Plasminogen Activator During Migration in Injured Rat Carotid Artery”, Circulation Research 1990 67:61-67.
Colbére-Garapin et al., “A New Dominant Hybrid Selective Marker for Higher Eukaryotic Cells”, J. Mol. Biol. 1981 150:1-14.
Collen D., “The Plasminogen (Fibrinolytic) System”, Thrombosis and Haemostasis 1999 82:165-270.
Debrock and Declerck, “Identification of a Functional Epitope in Plasminogen Activator Inhibitor-1, not Localized in the Reactive Center Loop”, Thrombosis and Haemostasis 1998 79:456-690.
De Boer et al., “Thetacpromoter: A functional hybrid derived from thetrpandlacpromoters”, Natl. Proc. Acad. Sci. USA 1983 80:32-36.
Declerck et al., “Identification of a Conformationally Distinct Form of Plasminogen Activator Inhibitor-1, Acting as a Non-inhibitory Substrate for Tissue-type Plasminogen Activator”, J. Biol. Chem. 1992 267(17) :11693-11696.
Deryugina et al., “Up-Regulation of Vascular Endothelial Growth Factor by Membrane-type 1 Matrix Metalloproteinase Stimulates Human Glioma Xenograft Growth and Angiogenesis1”, Cancer Research 2002 62(2) :580-588.
Dhanabal et al., “Endostatin Induces Endothelial Cell Apoptosis”, J. Biol. Chem. 1999 274(17) :11721-11726.
Egelund et al., “Type-1 plasminogen-activator inhibitor Conformational differences between latent, active, reactive-centre-cleaved and plasminogen-activator-complexed forms, as probed by proteolytic susceptibility”, Eur. J. Biochem. 1997 248(3) :775-785.
Ehrlich et al., “Elucidation of Structural Requirements on Plasminogen Activator Inhibitor 1 for Binding to Heparin”, J. Biol. Chem. 1992 267(16) :11606-11611.
Fiers et al., “Complete nucleotide sequence of SV40 DNA”, Nature 1978 273(5658) :113-120.
Folkman and Klagsbrun, “Angiogenic Factors”, Science 1987 235 :442-447.
Gitay-Goren et al., “The Binding of Vascular Endothelial Growth Factor to Its Receptors Is Dependent on Cell Surface-associated Heparin-like Molecules”, J. Biol. Chem. 1992 267(9) :6093-6098.
Goeddel et al., “Direct expression inEscherichia coliof a DNA sequence coding for human growth hormone”, Nature 1979 281:544-548.
Goeddel et al., “Synthesis of human fibroblast interferon byE. coli”, Nucleic Acids Research 1980 8(18) :4057-4074.
Gille et al., “Analysis of Biological Effects and Signaling Properties of Flt-1 (VEGFR-1) and KDR (VEGFR-2)”, J. Biol. Chem. 2001 276(5) :3222-3230.
Hanahan et al., “Patterns and Emerging Mechanism of the Angiogenic Switch during Tumorigenesis”, Cell 1996 86:353-364.
Hartman and Mulligan, “Two dominant-acting selectable markers for gene transfer studies in mammalian cells”, Proc. Natl. Acad. Sci. USA 1988 85(21) :8047-8051.
Houck et al., “The Vascular Endothelial Growth Factor Family :Identification of a Fourth Molecular Species and Characterization of Alternative Splicing of RNA”, Molecular Endocrinology 1991 5(12) :1806-1814.
Houck et al., “Dual Regulation of Vascular Endothelial Growth Factor Bioavailability of Genetic and Proteolytic Mechanisms”, J. Biol. Chem. 1992 267(36) :26031-26037.
Jones E., Proteinase Mutants ofSaccharomyces Cerevisiae1, Genetics 1977 85(1) :23-33.
Mulligan-Kehoe et al., “A Truncated Plasminogen Activator Inhibitor-1 Protein Induces and Inhibits Angiostatin (Kringles 1-3), a Plasminogen Cleavage Product”, J. Biol. Chem. 2001 276(11) :8588-8596.
Keijer et al., “The Interaction of Plasminogen Activator Inhibitor 1 With Plasminogen Activators (Tissue-Type and Urokinase-Type) and Fibrin :Localization of Interaction Sites and Physiologic Relevance” Blood 1991 78(2) :409-409.
Keyt et al., “The Carboxyl-terminal Domain (111-165) of Vascular Endothelial Growth Factor Is Critical for Its Mitogenic Potency”, J. Biol. Chem. 1996 271(13) :7788-7795.
Kim et al., “Inhibition of vascular endothelial growth factor-induced angiogenesis suppresses tumour growth in vivo”, Nature 1993 362:841-844.
Kjøller et al., “Conformational changes of the reactive-centre loop and βstrand 5A accompany temperature-dependent inhibitor-substrate transition of plasminogen-activator inhibitor 1”, Eur. J. Biochem. 1996 241(1) :38-46.
Kleinman et al., “Isolation and Characterization of Type IV Procollagen, Laminin, and Sulfate Proteoglycan from the EHS Sarcoma”, Biochemistry 1982 21:6188-6193.
Kroll et al., “A Multifunctional Prokaryotic Protein Expression System: Overproduction, Affinity Purification, and Selective Detection”, DNA and Cell Biology 1993 12(5) :441-453.
Laskowski et al., “Protein Inhibitors of Proteinases”, Ann. Rev. Biochem. 1980 49:593-626.
Lawrence et al., “Serpin Reactive Center Loop Mobility Is Requirement for Inhibitor Function but Not for Enzyme Recognition”, J
Chan Christina
Huynh Phuong
Licata & Tyrrell P.C.
Trustees of Dartmouth College
LandOfFree
Methods for modulating angiogenesis 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 for modulating angiogenesis, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Methods for modulating angiogenesis will most certainly appreciate the feedback.
Profile ID: LFUS-PAI-O-3836816