Drug – bio-affecting and body treating compositions – Designated organic active ingredient containing – Peptide containing doai
Patent
1995-05-03
2000-07-04
Kemmerer, Elizabeth
Drug, bio-affecting and body treating compositions
Designated organic active ingredient containing
Peptide containing doai
514 12, 435 691, 4352523, 435325, 530382, 536 235, 536 231, A61K 3816, C07K 14435, C12N 510, C12N 121
Patent
active
060839023
ABSTRACT:
The invention is directed to fibrin materials for use in fibrin compositions and methods that avoid the need to use thrombin as an activating agent for fibrin monomer-based sealants. The invention provides for substantially pure fibrin chains, fibrin chain precursors, fibrin chains with other N-terminal extensions, fibrin monomer, fibrin-homolog and fibrin-analog. The invention further provides for variant fibrin .gamma.-chains. The variant gamma-chain contains one or more mutations and/or deletions in the C-terminal region following the coiled-coil forming region such that, when incorporated into fibrin-homolog, the homolog lacks the ability to self-polymerize but has the ability to form non-covalent bonds, and thereby form mixed polymers useful as sealants, with fibrinogen. The invention also provides nucleotide sequences encoding fibrin chains or fibrin chain variants and cells expressing fibrin chains, fibrin chain variants, fibrin monomer, fibrin precursor or fibrinogen-analog. The invention further provides a method of forming fibrin-related proteins in vitro from their component fibrin chains. The invention additionally provides a method for forming a fibrin sealant by a reacting a first fibrin-related protein that is incapable of self-polymerizing with a second fibrin-related protein that is incapable of self-polymerizing. Fibrin chains produced by methods of the present invention may be used as sources of substantially pure starting material for the production of important fibrin-derived factors that regulate angiogenesis, platelet aggregation, and other physiological processes.
REFERENCES:
patent: 4902281 (1990-02-01), Avoy
patent: 5120834 (1992-06-01), Gargan et al.
patent: 5124439 (1992-06-01), Nieuwenhuizen
patent: 5292362 (1994-03-01), Bass et al.
patent: 5330974 (1994-07-01), Pines et al.
patent: 5453359 (1995-09-01), Gargan et al.
patent: 5510102 (1996-04-01), Cochrum
patent: 5631011 (1997-05-01), Wadstrom
patent: 5639940 (1997-06-01), Garner et al.
Bolyard and Lord, "Expression in Escherichia coli of the Human Fibrinogen B.beta. Chain and Its Cleavage by Thrombin," Blood, Apr. 1989, vol. 73, No. 5, pp 1202-1206.
Bolyard and Lord, "High-level expression of a functional human fibrinogen gamma chain in Escherichia coli," Gene, (1988), 66:183-192.
Brennan, "Fibrin Glue," Blood Reviews, (1991), 5:240-244.
Chevalet et al., "Genetic Improvements of an Industrial Strain of Aspergillus flavus for Urate Oxidase Production," Journal of Biotechnology, (1993) 27:239-247.
Chung et al., "Characterization of Complementary Deoxyribonucleic Acid and Genomic Deoxyribonucleic Acid for the .beta. Chain of Human Fibrinogen," Biochemistry, (1983), 22:3244-3250.
Chung et al., "Characterization of a cDNA Clone Coding for the .beta.Chain of Bovine Fibrinogen," Proc. Natl. Acad. Sci. U.S.A., Mar. 1981, vol. 78, No. 3, pp 1466-1470.
Chung et al., "Cloning of Fibrinogen Genes and Their cDNA," Ann. N.Y. Acad. Sci., (1983), 408:449-456.
Chung et al., "Characterization of a Complementary Deoxyribonucleic Acid Coding for the .gamma. Chain of Human Fibrinogen," Biochemistry, (1983), 22:3250-3256.
Danishefsky et al., "Intracellular Fate of Fibrinogen B.beta. Chain Expressed in COS Cells," Biochemica et Biophysica Acta, (1990), 1048:202-208.
Emr, "Heterologous Gene Expression in Yeast," Methods in Enzymology, (1990), 185:231-233.
Farrell et al., "Processing of the Carboxyl 15-Amino Acid Extension in the .alpha.-Chain of Fibrinogen," The Journal of Biological Chemistry, May 15, 1993, vol. 268, No. 14, pp 10351-10355.
Farrell et al., "Recombinant human fibrinogen and sulfation of the .gamma.' chain," Biochemistry, (1991), 30:9414-9420.
Fischer et al., "Renaturation of Lysozyme--Temperature Dependency of Renaturation Rate, Renaturation Yield, and Aggregation: Identification of Hydrophobic Folding Intermediates," Archives of Biochemistry and Biophysics, Oct. 1993, vol. 306, No. 1, pp 183-187.
Gan et al., "Reconstitution of Catalytically Compotent Human .zeta.-Thrombin by Combination of .zeta.-Thrombin Residues A1-36 and B1-148 and an Escherichia coli Expressed Polypeptide Corresponding to .zeta.-Thrombin Residues B149-259," Biochemistry, (1991), 30:11694-11699.
Grunfeld et al., "Effector-Assisted Refolding of Recombinant Tissue-Plasminogen Activator Produced in Escherichia coli," Applied Biochemistry and Biotechnology, (1992), 33:117-138.
Hartwig and Danishefsky, "Studies on the Assembly and Secretion of Fibrinogen," The Journal of Biological Chemistry, Apr. 5, 1991, vol. 266, No. 10, pp 6578-6585.
Hirose et al., "Renaturation of Ovotransferrin Under Two-step Conditions Allowing Primary Folding of the Fully Reduced Form and the Subsequent Regeneration of the Intramolecular Disulfides," The Journal of Biological Chemistry, Oct. 5, 1989, vol. 264, No. 28, pp 16867-16872.
Huang et al., "Biosynthesis of Human Fibrinogen, Subunit Interactions and Potential Intermediates in the Assembly," The Journal of Biological Chemistry, Apr. 25, 1993, vol. 268, No. 12, pp 8919-8926.
Kingsman et al., "Heterologous Gene Expression in Saccharomyces cerevisiae," Biotechnology and Genetic Engineering Reviews, Sep. 1985, 3:377-416.
Lord and Fowlkes, "Expression of a Fibrinogen Fusion Peptide in Escherichia coli: A Model Thrombin Substrate for Structure/Function Analysis," Blood, Jan. 1989, vol. 73, No. 1, pp 166-171.
Matras, "Fibrin Seal: The State of the Art," The Journal of Oral Maxillofacial Surgery, (1985), 13:605-611.
Mosesson, "The Assembly and Structure of the Fibrin Clot," Nouv. Rev. Fr. Hematol., (1992), 34:11-16.
Orsini et al., "Efficient renaturation and Fibrinolytic Properties of Prourokinase and a Deletion Mutant Expressed in Escherichia coli as Inclusion Bodies," Eur. J. Biochem., (1991) 195:691-697.
Rinas et al., "Denaturation-Renaturation of the Fibrin-Stabilizing Factor XIII a-Chain Isolated from Human Placenta, Properties of the Native and Reconstituted Protein," Biol. Chem. Hoppe-Seyler, Jan. 1990, 371:49-56.
Rixon et al., "Nucleotide Sequence of the Gene for the .gamma. Chain of Human Fibrinogen," Biochemistry, (1985), 24:2077-2086.
Rixon et al., "Characterization of a Complementary Deoxyribonucleic Acid Coding for the .alpha. Chain of Human Fibrinogen," Biochemistry, (1983), 22:3237-3244.
Roberts et al., "Heterologous Gene Expression in Aspergillus niger: a Glucoamylase-porcine Pancreatic Prophospholipase A.sub.2 Fusion Protein is Secreted and Processed to Yield Mature Enzyme," Gene, (1992), 122:155-161.
Roy et al., "Regulation of Fibrinogen Assembly: Transfection of Hep G2 Cells with B.beta. cDNA Specifically Enhances Synthesis of the Three Component Chains of Fibrinogen," The Journal of Biological Chemistry, Apr. 15, 1990, vol. 265, No. 11, pp 6389-6393.
Roy et al., "Assembly and Secretion of Recombinant Human Fibrinogen," The Journal of Biological Chemistry, Mar. 15, 1991, vol. 266, No. 8, pp 4758-4763.
Roy et al., "Assembly and Secretion of Fibrinogen: Degradation of Individual Chains," The Journal of Biological Chemistry, Nov. 15, 1992, vol. 267, No. 32, pp 23151-23158.
Rudolph, "Folding for Profit: Renaturation of Recombinant Proteins from Inclusion Bodies as a New Downstream Process," Boehringer Manneheim GmbH, pp 295-297.
Rudolph, "Renaturation of Recombinant, Disulfide-bonded Proteins from "Inclusion Bodies"," Boehringer Manneheim GmbH, pp 149-171.
Tsuchiya et al., "High Level Expression of the Synthetic Human Lysozyme Gene in Aspergillus oryzae," Appl. Microbiol. Biotechnol., (1992), 38:109-114.
Van den Berg et al., "Kluyveromyces as a Host for Heterologous Gene Expression: Expression and Secretion of Prochymosin," Bio/Technology, Feb. 1990, 8:135-139.
Wingfield and Dickinson, "Increased Activity of a Model Heterologous Protein in Saccharomyces cerevisiae Strains with Reduced Vacuolar Proteinases," Microbiology and Biotechnology, (1993) pp 211-215.
Zhang et al., "Symmetrical Disulfide Bonds are not Necessary for Assembly and Secretion of Human Fibrinogen," The Journal of Biological Chemistry, May 25, 1993, vol. 268, No. 15, pp 11278-11282.
Zhang and Redman, "Identification of B.beta. Chain D
Bristol--Myers Squibb Company
Furman Jr. Theodore R.
Kemmerer Elizabeth
Kilcoyne John M.
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