Mammalian recombinant coagulation proteins: Structure and function

Transfusion Science

Volumn 19, Issue 2, 1998, Pages 177-189

  White II, Gilbert C ^a,b   Pickens, Edward M ^c   Liles, Darla K ^c   Roberts, Harold R ^c  

^a UNIVERSITY OF NORTH CAROLINA   (United States)

^b UNIVERSITY OF NORTH CAROLINA SCHOOL OF MEDICINE   (United States)

^c NONE

Author keywords

[No Author keywords available]

Indexed keywords

ASPARTIC ACID; BLOOD CLOTTING FACTOR; BLOOD CLOTTING FACTOR 9; COAGULATING AGENT; DEOXYRIBONUCLEASE; GLUCOSYLCERAMIDASE; GLYCAN; HEPATITIS B VACCINE; INTERLEUKIN 2; RECOMBINANT ALPHA INTERFERON; RECOMBINANT BETA INTERFERON; RECOMBINANT BLOOD CLOTTING FACTOR 7A; RECOMBINANT BLOOD CLOTTING FACTOR 8; RECOMBINANT ERYTHROPOIETIN; RECOMBINANT GAMMA INTERFERON; RECOMBINANT GRANULOCYTE COLONY STIMULATING FACTOR; RECOMBINANT GRANULOCYTE MACROPHAGE COLONY STIMULATING FACTOR; RECOMBINANT GROWTH HORMONE; RECOMBINANT HUMAN INSULIN; RECOMBINANT PROTEIN; SERINE; TISSUE PLASMINOGEN ACTIVATOR; TYROSINE; VON WILLEBRAND FACTOR;

AMINO ACID SEQUENCE; ARTICLE; BLEEDING; BLOOD CLOTTING; BLOOD CLOTTING DISORDER; BLOOD PROTEIN DISORDER; CARBOXYLATION; CLINICAL TRIAL; DISULFIDE BOND; DRUG HYDROXYLATION; HEMOPHILIA A; HEMOPHILIA B; HUMAN; INTRAVENOUS DRUG ADMINISTRATION; NONHUMAN; PROTEIN DEGRADATION; PROTEIN MODIFICATION; PROTEIN PHOSPHORYLATION; PROTEIN PROCESSING; PROTEIN SECONDARY STRUCTURE; PROTEIN TERTIARY STRUCTURE; RECOMBINANT DNA TECHNOLOGY;

ANIMALS; BLOOD COAGULATION FACTORS; HUMANS; MAMMALS; RECOMBINANT PROTEINS; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 0031788456     PISSN: 09553886     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0955-3886(98)00027-7     Document Type: Article

References (57)

1. Goldstein JL, Brown MS: The clinical investigator: bewitched, bothered and bewildered - but still beloved. J Clin Invest 1997; 99:2803-2812.
2. Chasin L, Urlaub G: Isolation of Chinese hamster ovary cell mutants deficient in dihydrofolate reductase activity. Proc Natl Acad Sci 1980; 77:4216-4220.
3. Kaufman RJ: Selection and coamplification of heterologous genes in mammalian cells. Methods in Enzymology 1990; 185:537-566.
4. Nelsestuen GL, Zytkovicz TH, Howard JB: The mode of action of vitamin K. Identification of gamma-carboxyglutamic acid as a component of prothrombin. J Biol Chem 1974; 249:6347-6350.
5. Stenflo J, Fernlund P, Egan W, Roepstorff P: Vitamin K-dependent modifications of glutamic acid residues in prothrombin. Proc Natl Acad Sci 1974; 71:2730-2733.
6. Fernlund P, Stenflo J: Hydroxyaspartic acid in vitamin K-dependent proteins. J Biol Chem 1983; 258:12509-12512.
7. Huttner W: Sulphation of tyrosine residues - a widespread modification of proteins. Nature 1982; 299:273-276.
8. Hortin GL: Sulfation of tyrosine residues in coagulation factor V. Blood 1990; 76:946-952.
9. Takeuchi M, Inoue N, Strickland TW, et al.: Relationship between sugar chain structure and biological activity of recombinant human erythropoietin produced in Chinese hamster ovary cells. Proc Natl Acad Sci 1989; 86:7819-7822.
10. Takeuchi M, Takasaki S, Shimada M, Kobata A: Role of sugar chains in vitro biological activity of human erythropoietin produced in recombinant Chinese hamster ovary cells. J Biol Chem 1990; 265:12127-12130.
11. Bucher D, Nebelin E, Thomsen J, Stenflo J: Identification of gamma-carboxyglutamic acid residues in bovine factors IX and X, and in a new vitamin K-dependent protein. FEBS Letters 1976; 68:293-296.
12. Bajaj SP, Rapaport SI, Brown SF: Isolation and characterization of human factor VII. Activation of factor VII by factor Xa. J Biol Chem 1981; 256:253-259.
13. Federici AS, Bader R, Pagani S, Colibretti ML, De Marco L, Mannucci PM: Binding of von Willebrand factor to glycoprotein Ib and IIb/IIIa complex: affinity is related to multimeric size. Br J Haematol 1989; 73:93-99.
14. Kaufman FJ, Wasley LC, Dorner AJ: Synthesis, processing, and secretion of human factor VIII expressed in mammalian cells. J Biol Chem 1988; 263:6352-6362.
15. Wood WI, Capon DJ, Simonsen CC, et al.: Expression of active human factor VIII from recombinant cDNA clones. Nature 1984; 312:330-333.
16. Pittman DD, Alderman EM, Tomkinson KN, Wanf JH, Giles AR, Kaufman RJ: Biochemical, immunochemical, and in vivo functional characterization of B-domain-deleted factor VIII. Blood 1993; 81:2925-2935.
17. Kumar HP, Hague C, Haley T, et al.: Elucidation of N-linked oligosaccharide structures of recombinant factor VIII using fluorophore-assisted carbohydrate electrophoresis. Biotech Applied Biochem 1996; 204:207-216.
18. Hironaka T, Kato M, Sawada S, Minaga T: The carbohydrate structures of blood coagulation factor VIII. Protein Nucleic Acid Enzyme 1992; 37 (Suppl. 11):1723-1729.
19. Galili U: The natural anti-gal antibody: evolution and autoimmunity in man. Immunol Series 1991; 55:355-373.
20. Pittman DD, Wang JH, Kaufman RJ: Identification and functional importance of tyrosine sulfate residues within recombinant factor VIII. Biochemistry 1992; 31:3315-3325.
21. White II GC, McMillan CW, Kingdon HS, Shoemaker CB: Use of recombinant antihemophilic factor in the treatment of two patients with classic hemophilia. New Eng J Med 1989; 320:166-170.
22. Schwartz RS, Ablidgaard CF, Aledort LM, et al.: Human recombinant DNA-derived antihemophilic factor (factor VIII) in the treatment of hemophilia A. Recombinant factor VIII study group. New Eng J Med 1990; 323:1800-1805.
23. ™) in previously treated patients with hemophilia A. Thrombos Haemostas 1997; 77:660-667.
24. Fijnvandraat K, Berntorp E, ten Cate JW, et al.: Recombinant B-domain deleted FVIII (rVIII-SQ): pharmacokinetics and initial safety aspects in hemophilia A patients. Thrombos Haemostas 1997; 77:298-302.
25. Fournel M: personal communication.
26. Esmon PC, Kuo HS, Fournel MA: Characterization of recombinant factor VIII and a recombinant factor VIII deletion mutant using a rabbit immunogenicity model system. Blood 1990; 76:1593-1600.
27. Lusher JM, Arkin S, Abildgaard CF, Schwartz RS: Kogenate previously untreated patient study group: recombinant factor VIII for the treatment of previously untreated patients with haemophilia A. New Eng J Med 1993; 328:453-459.
28. Bray GL, Gomperts ED, Courter S, et al.: A multicenter study of recombinant factor VIII (Recombinate): safety, efficacy, and inhibitor risk in previously untreated patients with hemophilia A. Blood 1994; 83:2428-2435
29. Lusher JM, Spira J: International r-FVIII SQ Study Group. Safety, efficacy, and inhibitor development in previously untreated patients (PUPs) treated exclusively with recombinant B-domain deleted FVIII (rFVIII SQ): 2.5 study years. Blood, in press.
30. Rosendaal FR, Nieuwenhuis HK, van den Berg HM, et al.: A sudden increase in factor VIII inhibitor development in multitransfused hemophilia A patients in the Netherlands. Dutch Hemophilia Study Group. Blood 1993; 81:2180-2186.
31. Peerlinck K, Arnout J, Gilles JG, Saint-Remy JM, Vermylen J: A higher than expected incidence of factor VIII inhibitors in multitransfused haemophilia A patients treated with an intermediate purity Pasteurized factor VIII concentrate. Thrombos Haemostas 1993; 69:115-118.
32. Robinson S, Schwinn H, Josic D: Investigation of inhibitors after treatment with a double virus inactivated FVIII preparation. Thrombos Haemostas 1997; (Suppl.):65.
33. Mannucci PM: Outbreak of hepatitis A among italian patients with haemophilia. Lancet 1992; 339:819.
34. Gerritzen A, Schneweis KE, Brackman H-H, et al.: Acute hepatitis A in haemophiliacs. Lancet 340, 1231-1232.
35. Mariani G, di Paolantonio T, Baklaya R, Morfini M, Mannucci PM: Prospective study of the evaluation of hepatitis C virus infectivity in a high-purity, solvent/detergent treated factor VIII concentrate: parallel evaluation of other markers for lipid-enveloped and nonlipid-enveloped viruses. Transfusion 1993; 33:814-818.
36. Hepatitis A among persons with hemophilia who received clotting factor concentrate - United States, September-December 1995, MMWR (Atlanta, Ga: Centers for Disease Control. US Department of Health and Human Services publication) 1996; 45:29-32.
37. Flores G, Juárez JC, Montoro JB, Tussell JM, Altisent C, Juste C, Jardi R: Seroprevalence of parvovirus B19, cytomegalovirus, hepatitis A virus and hepatitis E virus antibodies in haemophiliacs treated exclusively with clotting-factor concentrates considered safe against human immunodeficiency and hepatitis C viruses. Haemophilia 1995; 1:115-117.
38. Yee TT, Cohen BJ, Pasi KJ, Lee CA: Transmission of symptomatic parvovirus B19 infection by clotting factor concentrate. Brit J Haemat 1996; 93:457-459.
39. Ragni MV, Koch WC, Jordan JA: Parvovirus B19 infection in patients with hemophilia. Transfusion 1996; 36:238-241.
40. Kaufman RJ, Wasley LC, Furie BC, Furie B, Shoemaker CB: Expression, purification, and characterization of recombinant γ-carboxylated factor IX synthesized in Chinese hamster ovary cells. J Biol Chem 1986; 261:9622-9628.
41. Wasley LC, Rehemtulla A, Bristol JA, Kaufman RJ: Pace/furin can process the vitamin K-dependent pro-factor IX precursor within the secretory pathway. J Biol Chem 1993; 268:8458-8465.
42. Bond MD, Patel H, Huberty MC, et al.: Structural and biological characterization of Gla-related isoforms of recombinant human factor IX shows that Gla36 and Gla40 are not essential for in vitro clotting activity. Thrombos Haemostas 1995, 73, 1167-1168.
43. Gillis S, Furie BC, Furie B, et al.: γ-carboxyglutamic acids 36 and 40 do not contribute to human factor IX function. Protein Sci 1997; 6:185-196.
44. White II GC, Beebe A, Nielsen B: Recombinant factor IX. Thrombos Haemostas 1997; 78:261-265.
45. Bond MD: personal communication.
46. White II GC, Pasi J, Lusher J, Brackmann HH, Magill M, Courter S: Recombinant factor IX in the treatment of previously-treated patients with hemophilia B. Thrombos Haemostas 1997; (Suppl.):52.
47. Ragni M, White II GC, Pasi J, Garzone P, Courter S, Goodfellow J: Dose-response relationship of rFIX in the surgical setting. Blood 1996; 88 (Suppl):329a.
48. Thim L, Bjoern S, Christensen M, et al.: Amino acid sequence and posttranslational modifications of human factor VIIa from plasma and transfected baby hamster kidney cells. Biochemistry 1988; 27:7785-7793.
49. Hedner U, Glazer S, Pingel K, et al.: Successful use of recombinant factor VIIa in patients with severe haemophilia A during synovectomy. Lancet 1988; 2:1193.
50. Macik BG, Lindley CM, Lusher J, et al.: Safety and initial clinical efficacy of three dose levels of recombinant activated factor VII (rFVIIa): Results of a phase I study. Blood Coag Fibrinol 1993; 4:521-527.
51. Lusher JM, Roberts HR, Hedner U: Recombinant factor VIIa (NovoSeven) summary of world wide clinical experience. Blood Coag Fibrinol, in press.
52. Lusher JM, Roberts HR, Davignon G, et al.: A randomized double-blind comparison of two dosage levels of recombinant factor VIIa in the treatment of joint, muscle and mucocutaneous haemorrhages in persons with haemophilia A and B, with and without inhibitors. Thrombos Haemostas, in press.
53. Lusher JM, Ingerslev J, Roberts HR, Hedner U: Clinical experience with recombinant factory VIIa. A review. Thrombos Haemostas, submitted.
54. Nicolaisen EM, Hansen LL, Poulsen F, Glazer S, Hedner U: Immunological aspects of recombinant factor VIIa (rFVIIa) in clinical use. Thrombos Haemostas 1996; 76:200-204.
55. Schwarz HP, Turecek PL, Pichler L, Mitterer A, Mundt W, Dorner F, Roussi J, Drouet L: Recombinant von Willebrand factor. Thrombos Haemostas 1977; 78:571-576.
56. Furlan M, Robles R, Lämmle B: Partial purification and characterization of a protease from human plasma cleaving von Willebrand factor to fragments produced by in vivo proteolysis. Blood 1996; 87:4223-4234.
57. Turecek PL, Gritsch H, Pichler L, et al.: In vivo characterization of recombinant von Willebrand factor in dogs with von Willebrand disease. Blood, in press.