Contributions of Gla and EGF-like domains to the function of vitamin K- dependent coagulation factors

Critical Reviews in Eukaryotic Gene Expression

Volumn 9, Issue 1, 1999, Pages 59-88

  Stenflo, Johan ^a  

^a LUND UNIVERSITY   (Sweden)

Author keywords

Blood coagulation; Calcium binding; EGF like domains; Vitamin K; carboxyglutamic acid

Indexed keywords

4 CARBOXYGLUTAMIC ACID; BLOOD CLOTTING FACTOR; BLOOD CLOTTING FACTOR 10; BLOOD CLOTTING FACTOR 7; BLOOD CLOTTING FACTOR 9; EPIDERMAL GROWTH FACTOR; PHOSPHOLIPID; PROTEIN C; PROTEIN S; PROTHROMBIN; SERINE PROTEINASE; VITAMIN K GROUP;

AMINO TERMINAL SEQUENCE; ANTICOAGULATION; BINDING AFFINITY; BLOOD CLOTTING; CALCIUM BINDING; HUMAN; MEMBRANE BINDING; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; REVIEW;

EID: 0033382739     PISSN: 10454403     EISSN: None     Source Type: Journal    
DOI: 10.1615/critreveukaryotgeneexpr.v9.i1.50     Document Type: Review

References (231)

1. Ahmad SS, Wong MY, Rawala R, Jameson BA, Walsh PN (1998): Coagulation factor IX residues G4-Q11 mediate its interaction with a shared factor IX/IXa binding site on activated platelets but not the assembly of the functional factor X activating complex. Biochemistry 37:1671-1679.
2. Appella E, Robinson EA, Ullrich SJ, Stoppelli MP, Corti A, Cassani G, Blasi F (1987): The receptor-binding sequence of urokinase. A biological function for the growth-factor module of proteases. J Biol Chem 262(10):4437-4440.
3. Arni RK, Padmanabhan K, Padmanabhan KP, Wu T-P, Tulinsky A (1994): Structure of non-covalent complex of prothrombin kringle 2 with PPACK-thrombin. Chem Phys Lipids 67/68:59-66.
4. 2+-binding to the gamma-carboxyglutamic acid and epidermal growth factor-like regions of factor IX. Studies using intact domains isolated from controlled proteolytic digests of bovine factor X. J Biol Chem 266:2430.
5. 2-terminal epidermal growth factor-like module of factor IXaβ and factor X. J Biol Chem 269: 3690-3697.
6. 2-terminal epidermal growth factor-like module of factor IXa beta and factor X. J Biol Chem 269: 3690-3697.
7. Baglia FA, Walsh PN (1998): Prothrombin is a cofactor for the binding of factor XI to the platelet surface and for platelet-mediated factor XI activation by thrombin. Biochemistry 37:2271-2281.
8. Baker ME, French FS, Joseph DR (1987): Vitamin K-dependent protein S is similar to rat androgen-binding protein. Biochem J 243:293-296.
9. Banner DW (1997): The factor VIIa/tissue factor complex. Thromb Haemost 78:512-515.
10. Banner DW, D'Arcy A, Chene C, Winkler FK, Guha A, Konigsberg WH, Nemerson Y, Kirchhofer D (1996): The crystal structure of the complex of blood coagulation factor VIIa with soluble tissue factor. Nature 380:41-46.
11. Baron M, Norman DG, Harvey TS, Handford PA, Mayhew M, Tse AGD, Brownlee GG, Campbell ID (1992): The three-dimensional structure of the first EGF-like module of human factor IX: comparison with EGF and TGF-α. Protein Sci 1:81-90.
12. Bathurst IC, Brennan SO, Carrell RW, Cousens LS, Brake AJ, Barr PJ (1987): Yeast KEX3 protease has the properties of a human proalbumin converting enzyme. Science 235:348-350.
13. Bentley AK, Rees DJG, Rizza C, Brownlee GG (1986): Defective propeptide processing of blood clotting factor IX caused by mutation of arginine to glutamine in position -4. Cell 45:343-348.
14. Bersch B, Hernandez J-F, Marion D, Arlaud GJ (1998): Solution structure of the epidermal growth factor (EGF)-like module of human complement protease Clr, an atypical member of the EGF family. Biochemistry 37:1204-1214.
15. Blasi F, Vassalli JD, Danö J (1987): Urokinase-type plasminogen activator: proenzyme, receptor, and inhibitors. J Cell Biol 104:801-804.
16. Bork P, Downing AK, Kieffer B, Campbell ID (1996): Structure and distribution of modules in extracellular proteins. Quart Rev Biophys 29:119-167.
17. Borowski M, Furie BC, Bauminger S, Furie B (1986): Prothrombin requires two sequential metal-dependent conformational transitions to bind phospholipid. Conformation-specific antibodies directed against the phospholipid-binding site on prothrombin. J Biol Chem 261:14969-14975.
18. Bourin MC, Lindahl U (1993): Glycosaminoglycans and the regulation of blood coagulation. Biochem J 289: 313-330.
19. Brandstetter H, Bauer M, Huber R, Lollar P, Bode W (1995): X-ray structure of clotting factor IXa: active site and module structure related to Xase activity and hemophilia B. Proc Natl Acad Sci USA 92:9796-9800.
20. Breyer JA, Cohen S (1990): The epidermal growth factor precursor isolated from murine kidney membranes. Chemical characterization and biological properties. J Biol Chem 265:16564-16570.
21. Bristol JA, Freedman SJ, Furie BC, Furie B (1994): Profactor IX: the propeptide inhibits binding to membrane surfaces and activation by factor XIa. Biochemistry 33:14136-14143.
22. Broze GJ (1995): Tissue factor pathway inhibitor and the revised theory of coagulation. Annu Rev Med 46: 103-112.
23. Campbell ID, Bork P (1993): Epidermal growth factor-like modules. Curr Op Struct Biol 3:385-392.
24. Campbell ID, Downing AK (1994): Building protein structure and function from modular units. Trends Biotechnol 12:168-172.
25. Chang J-Y, Stafford DW, Straight DL (1995): The roles of factor VII's structural domains in tissue factor binding. Biochemistry 34:12227-12232.
26. Chang JY, Monroe DM, Stafford DW, Brinkhous KM, Roberts HR (1997): Replacing the first epidermal growth factor-like domain of factor IX with that of factor VII enhances activity in vitro and in canine hemophilia B. J Clin Invest 100:886-892.
27. Cheung W-F, Hamaguchi N, Smith KJ, Stafford DW (1992): The binding of human factor IX to endothelial cells is mediated by residues 3-11. J Biol Chem 267: 20529-20531.
28. Cheung WF, van den Born J, Kuhn K, Kjellen L, Hudson BG, Stafford DW (1996): Identification of the endothelial cell binding site for factor IX. Proc Natl Acad Sci USA 93:11068-11073.
29. Christiansen WT, Jalbert LR, Robertson RM, Jhingan A, Prorok M, Castellino FJ (1995): Hydrophobic amino acid residues of human anticoagulation protein C that contribute to its functional binding to phospholipid vesicles. Biochemistry 34:10376-10382.
30. Christophe OD, Lenting PJ, Kolkman JA, Brownlee GL, Mertens K (1998): Blood coagulation factor IX residues Glu78 and Arg94 provide a link between both epidermal growth factor-like domains that is crucial in the interaction with factor VIII light chain. J Biol Chem 273:202-227
31. Colpitts TL, Castellino FJ (1994): Calcium and phospholipid binding properties of synthetic gamma-carboxyglutamic acid-containing peptides with sequence counterparts in human protein C. Biochemistry 33:3501-3508.
32. Cooke RM, Wilkinson AJ, Baron M, Pastore A, Tappin MJ, Campbell ID, Gregory H, Sheard B (1987): The solution structure of human epidermal growth factor. Nature 327:339-341.
33. Dahlbäck B (1994): Inherited resistance to activated protein C, a major cause of venous thrombosis, is due to a mutation in the factor V gene. Haemostasis 24: 139-151.
34. Dahlbäck B (1995): The protein C anticoagulant system: inherited defects as basis for venous thrombosis. Thromb Res 77:1-43.
35. Dahlbäck B (1997a): Factor V and protein S as cofactors to activated protein C. Haematologica 82:91-95.
36. Dahlbäck B (1997b): Resistance to activated protein C as risk factor for thrombosis: molecular mechanisms, laboratory investigation, and clinical management. Semin Hematol 34:217-234.
37. Dahlbäck B, Hildebrand B, Linse S (1990): Novel type of very high affinity calcium-binding sites in beta-hydroxyasparagine-containing epidermal growth factor-like domains in vitamin K-dependent protein S. J Biol Chem 265:18481-91848.
38. Dahlbäck B (1991): Protein S and C4b-binding protein: components involved in the regulation of the protein C anticoagulant system. Thromb Haemost 66:49-61.
39. Dahlbäck B, Hildebrand B, Malm J (1990): Characterization of functionally important domains in human vitamin K-dependent protein S using monoclonal antibodies. J Biol Chem 265:8127-8135.
40. Dahlbäck B, Lundwall Å, Stenflo J (1986): Primary structure of bovine vitamin K-dependent protein S. Proc Natl Acad Sci USA 83:4199-4203.
41. Dahlbäck B, Stenflo J (1994): The protein C anticoagulant system. Stamatoyannopoulos G, Nienhuis AW, Majerus PW, Varmus H (eds): "The Molecular Basis of Blood Diseases." Philadelphia: W.B. Saunders, pp. 599-628.
42. Davie EW (1995): Biochemical and molecular aspects of the coagulation cascade. Thromb Haemost 74:1-6.
43. Davie EW, Fujikawa K, Kisiel W (1991): The coagulation cascade: initiation, maintainance, and regulation. Biochemistry 30:10363-10370.
44. Davie EW, Ratnoff OD (1964): Waterfall sequence for intrinsic blood clotting. Science 145:1310-1312.
45. Davis LM, McGraw RA, Ware JL, Roberts H, Stafford DW (1987): Factor IX Alabama: a point mutation in a clotting protein results in hemophilia B. Blood 69:140-143.
46. Dickinson CD, Ruf W (1997): Active siter modification of factor VIIa affects interactions of the protease domain with tissue factor. J Biol Chem 272:19875-19879.
47. Doolittle RF (1994): "The Molecular Biology of Fibrinogen." Philadelphia: W.B. Saunders.
48. Doolittle RF, Feng DF (1987): Reconstructing the evolution of vertebrate blood coagulation from a consideration of the amino acid sequences of clotting proteins. Stamatoyannopoulos G, Nienhuis AW, Majerus PW, Varmus H (eds): "The Molecular Basis of Blood Diseases." Philadelphia: W.B. Saunders, pp. 721-723.
49. Downing AK, Knott V, Werner JM, Cardy CM, Campbell ID, Handford PA (1996): Solution structure of a pair of calcium-binding epidermal growth factor-like domains: implications for the Marfan syndrome and other genetic disorders. Cell 85:597-605.
50. Edenbrandt CM, Lundwall Å, Wydro RM, Stenflo J (1990): Molecular analysis of the gene for vitamin K-dependent protein S and its pseudogene. Cloning and partial gene organization. Biochemistry 29:7861-7868.
51. Edgington TS, Dickinson CD, Ruf W (1997): The structural basis of function of the TF. VIIa complex in the cellular initiation of coagulation. Thromb Haemost 78:401-405.
52. Edgington TS, Mackman N, Brand K, Ruf W (1991): The structural biology of expression and function of tissue factor. Thromb Haemost 66:67-79.
53. Esmon CT (1989): The roles of protein C and thrombomodulin in the regulation of blood coagulation. J Biol Chem 264:4743-4746.
54. Esmon CT (1993): Molecular events that control the protein C anticoagulant pathway. Thromb Haemost 70:29-35.
55. Esmon CT (1995): Thrombomodulin as a model of molecular mechanisms that modulate protease specificity and function at the vessel surface. FASEB J 9:946-955.
56. Esmon CT, Ding W, Yasuhiro K, Gu JM, Ferrell G, Regan LM, Stearns ???, Kurosawa DJ, Kurosawa S, Mather T, Laszik Z, Esmon NL (1997): The protein C pathway: new insights. Thromb Haemost 78:70-74.
57. Fernlund P, Stenflo J (1983): β-Hydroxyaspartic acid in vitamin K-dependent proteins. J Biol Chem 258: 12509-12512.
58. Foster DC, Rudinski MS, Schach BG, Berkner KL, Kumar AA, Hagen FS, Sprecher CA, Insley MY, Davie EW (1987): Propeptide of human protein C is necessary for gamma-carboxylation. Biochemistry 26:7003-7011.
59. Freedman SJ, Blostein MD, Baleja JD, Jacobs M, Furie BC, Furie B (1996): Identification of the phospholipid binding site in the vitamin K-dependent blood coagulation protein factor IX. J Biol Chem 271:16227-16236.
60. Freedman SJ, Furie BC, Furie B, Baleja JD (1995a): Structure of the calcium ion-bound gamma-carboxyglutamic acid-rich domain of factor IX. Biochemistry 34:12126-12137.
61. Freedman SJ, Furie BC, Furie B, Baleja JD (1995b): Structure of the metal-free γ-carboxyglutamic acid-rich membrane binding region of factor IX by two-dimensional NMR spectroscopy. J Biol Chem 270:7980-7987.
62. Fujimaki K, Yamazaki T, Taniwaki M, Ichinose A (1998): The gene for protein Z is localized to chromosome 13 at band q34 and is coded by eight regular exons and one alternative exon. Biochemistry 37:6838-6846.
63. Furie B, Furie BC (1988): The molecular basis of blood coagulation. Cell 53:505-518.
64. Furie B, Furie BC (1990): Molecular basis of vitamin K-dependent gamma-carboxylation. Blood 75:1753-1762.
65. Furie BC, Furie B (1997): Structure and mechanism of action of the vitamin K-dependent gamma-glutamyl carboxylase: recent advances from mutagenesis studies. Thromb Haemost 78:595-598.
66. Gailani D, Broze GJJ (1991): Factor XI activation in a revised model of blood coagulation. Science 253:909-912.
67. Gerads I, Govers-Riemslag JWP, Tans G, Zwaal RFA, Rosing J (1990): Prothrombin activation on membranes with anionic lipids containing phosphate, sulfate, and/or carboxyl groups. Biochemistry 29:7967-7974.
68. Gerlitz B, Grinnell BW (1996): Mutation of protease domain residues Lys37-39 in human protein C inhibits activation by the thrombomodulin-thrombin complex without affecting activation by free thrombin. J Biol Chem 271: 22285-22288.
69. Gershagen S, Fernlund P, Lundwall Å (1987): A cDNA coding for human sex hormone binding globulin. Homology to vitamin K-dependent protein S. FEBS Lett 220:129-135.
70. Giannelli F, Green PM, Sommer SS, Poon MC, Ludwig M, Schwaab R, Reitsma PH, Goossens M, Yoshioka A, Figueiredo MS, Brownlee GG (1997): Haemophilia B: database of point mutations and short additions and deletions, 7th edition. Nucl Acids Res 25:133-135.
71. Grinell BW, Gerlitz B, Berg DT (1994): Identification of a region in protein C involved in thrombomodulin-stimulated activation by thrombin: potential repulsion at anion-binding site I in thrombin. Biochem J 303:929-933.
72. Hackeng TM, van't Veer C, Meijers JC, Bouma BN (1994): Human protein S inhibits prothrombinase complex activity on endothelial cells and platelets via direct interactions with factors Va and Xa. J Biol Chem 269: 21051-21058.
73. Han X, Fiehler R, Broze G (1998): Isolation of a protein Z-dependent plasma protease inhibitor. Proc Natl Acad Sci USA 95:9250-9255.
74. Handford P, Downing AK, Rao Z, Hewett DR, Sykes BC, Kielty CM (1995): The calcium binding properties and molecular organization of epidermal growth factor-like domains in human fibrillin-1. J Biol Chem 270:6751-6756.
75. Handford PA, Baron M, Mayhew M, Wills A, Beesley T, Brownlee GG, Campbell ID (1990): The first EGF-like domain from human factor IX contains a high-affinity calcium binding site. EMBO J 9:475-480.
76. Handford PA, Mayhew M, Baron M, Winship PR, Campbell ID, Brownlee GG (1991): Key residues involved in calcium-binding motifs in EGF-like domains. Nature 351:164-167.
77. Hase S, Nishimura H, Kawabata S-I, Iwanaga S, Ikenaka T (1990): The structure of (Xylose)2 glucose-O-serine 53 found in the first epidermal growth factor-like domain of bovine blood clotting factor IX. J Biol Chem 265:1858-1861.
78. Hauschka PA, Lian JB, Cole DEC, Gendberg CM (1989): Osteocalcin and matrix Gla protein: vitamin K-dependent proteins in bone. Physiol Rev 69:990-1047.
79. Hayashi T, Nishioka J, Shigekiyo T, Saito S, Suzuki K (1994): Protein S Tokushima: abnormal molecule with a substitution of Glu for Lys-155 in the second epidermal growth factor-like domain of protein S. Blood 83: 683-690.
80. Hayashi T, Nishisoka J, Suzuki K (1995): Molecular mechanism of the dysfunction of protein S Tokushima (Lys 155-Glu) for the regulation of the blood coagulation system. Biochim Biophys Acta 1272:159-167.
81. He X, Shen L, Dahlbäck B (1995): Expression and functional characterization of chimeras between human and bovine vitamin K-dependent protein S defining modules important for the species-specificity of the activated protein C cofactor activity. Eur J Biochem 227:433-440.
82. He X, Shen L, Villoutreix BO, Dahlbäck B (1998): Amino acid residues in thrombin-sensitive region and first epidermal growth factor domain of vitamin K-dependent protein S determining specificity of the activated protein C cofactor function. J Biol Chem 273: 27449-27458.
83. Heeb MJ, Mesters RM, Tans G, Rosing J, Griffin JH (1993): Binding of protein S to factor Va associated with inhibition of prothrombinase that is independent of activated protein C. J Biol Chem 268(4):2872-2877.
84. Heeb MJ, Rosing J, Bakker HM, Fernandez JA, Tans G, Griffin JH (1994): Protein S binds to and inhibits factor Xa. Proc Natl Acad Sci USA 91:2728-2732.
85. Henriksen RA, Jackson CM (1975): Cooperative calcium binding by the phospholipid binding region of bovine prothrombin: a requirement for intact disulfide bridges. Arch Biochem Biophys 170:149-159.
86. Hertzberg MS, Ben-Tal O, Furie B, Furie BC (1992): Construction, expression, and characterization of a chimera of factor IX and factor X. The role of the second epidermal growth factor domain and serine protease domain in factor Va binding. J Biol Chem 267:14759-14766.
87. Higashi S, Matsumoto N, Iwanaga S (1996): Molecular mechanism of tissue factor-mediated acceleration of factor VIIa activity. J Biol Chem 271:26569-26574.
88. Hoffman M, Monroe DM, Oliver JA, Roberts HR (1995): Factors IXa and Xa play distinct roles in tissue factor-dependent initiation of coagulation. Blood 86: 1794-1801.
89. Hogg PJ, Öhlin AK, Stenflo J (1992): Identification of structural domains in protein C involved in its interaction with thrombin-thrombomodulin on the surface of endothelial cells. J Biol Chem 267:703-706.
90. Hu CJ, Baglia FA, Mills DC, Konkle BA, Walsh PN (1998): Tissue-specific expression of functional platelet factor XI is independent of plasma factor XI expression. Blood 91:3800-3807.
91. Huang LH, Ke X-H, Sweeny W, Tam JP (1989): Calcium binding and putative activity of the epidermal growth factor domain of blood coagulation factor IX. Biochem Biophys Res Commun 60:133-139.
92. Hubbard BR, Jacobs M, Ulrich MMW, Furie B, Furie BC (1989): Vitamin K-dependent carboxylation: In vitro modification of synthetic peptides containing the gamma-carboxylation recognition site. J Biol Chem 264:14145-14150.
93. Hunter MJ, Komives EA (1995): Thrombin-binding affinities of different disulfide-bonded isomers of the fifth EGF-like domain of thrombomodulin. Protein Sci 4:2129-2137.
94. Husten EJ, Esmon CT, Johnson AE (1987): The active site of blood coagulation factor Xa. Its distance from the phospholipid surface and its conformational sensitivity to components of the prothrombinase complex. J Biol Chem 262:12953-12961.
95. Jackson CM (1988): Calcium ion binding to gamma-carboxyglutamic acid-containing proteins from the blood clotting system: What we still don't understand. Suttie JW (ed): "Current Advances in Vitamin K Research." New York: Elsevier, pp. 305-324.
96. Jacobs M, Freedman SJ, Furie BC, Furie B (1994): Membrane binding properties of the factor IX gamma-carboxyglutamic acid-rich domain prepared by chemical synthesis. J Biol Chem 269:25494-25501.
97. Jalbert LR, Chan JC, Christiansen WT, Castellino FJ (1996): The hydrophobic nature of residue-5 of human protein C is a major determinant of its functional interactions with acidic phospholipid vesicles. Biochemistry 35:7093-7099.
98. Jia S, McGinnis K, VanDusen WJ, Burke CJ, Kuo A, Griffin PR, Sardana MK, Elliston KO, Stern AM, Friedman PA (1994): A fully active catalytic domain of bovine aspartyl (asparaginyl) beta-hydroxylase expressed in Escherichia coli: characterization and evidence for the identification of an active-site region in vertebrate alpha-ketoglutarate-dependent dioxygenases. Proc Natl Acad Sci USA 91:7227-7231.
99. Jia S, VanDusen WJ, Dichl RE, Kohl NE, Dixon RA, Elliston KO, Stern AM, Friedman PA (1992): cDNA cloning and expression of bovine aspartyl (asparaginyl) beta-hydroxylase. J Biol Chem 267:14322-14327.
100. Julius D, Brake A, Blair L, Kunisawa R, Thorner J (1984): Isolation of the putative structural gene for the lysine-arginine-cleaving endopeptidase required for processing of yeast prepro-alpha-factor. Cell 37:1075-1089.
101. Kalafatis M, Egan JO, van't Veer C, Cawthern KM, Mann KG (1997): The regulation of clotting factors. Crit Rev Eukaryotic Gene Expression 7:241-280.
102. Kalafatis M, Bertina RM, Rand MD, Mann KG (1995): Characterization of the molecular defect in factor V R506Q. J Biol Chem 270:4053-4057.
103. Kane WH, Davie EW (1988): Blood coagulation factors V and VIII: structural and functional similarities and their relationship to hemorrhagic and thrombotic disorders. Blood 71:539-555.
104. Kawabata S, Nakagawa K, Muta T, Iwanaga S, Davie EW (1993): Rabbit liver microsomal endopeptidase with substrate specificity for processing proproteins is structurally related to rat testes metalloendopeptidase 24.15. J Biol Chem 268:12498-12503.
105. Kazama Y, Pastuszyn A, Wildgoose P, Hamamoto T, Kisiel W (1993): Isolation and characterization of proteolytic fragments of human factor VIIa which inhibit the tissue factor-enhanced amidolytic activity of factor VIIa. J Biol Chem 268:16231-16240.
106. Kelly CR, Dickinson CD, Ruf W (1997): Calcium binding to the first epidermal growth factor module of coagulation factor VIIa is important for cofactor interaction and proteolytic function. J Biol Chem 272:17467-17472.
107. Kielty CM, Shuttleworth A (1993): The role of calcium in organization of fibrillar microfibrils. FEBS Lett 336: 323-326.
108. Kivirikko KI, Myllylä R (1987): Recent developments in posttranslational modification: intracellular processing. Methods Enzymol 144:96-114.
109. Kjalke M, Monroe DM, Hoffman M, Oliver JA, Ezban M, Roberts HR (1998): Active-site-inactivated factors VIIa, Xa, and IXa inhibit individual steps in a cell-based model of tissue factor-initiated coagulation. Thromb Haemost 80:578-584.
110. Knott V, Downing K, Cardy CM, Handford P (1996): Calcium binding properties of an epidermal growth factor-like domain pair from human fibrillin-1. J Mol Biol 255:22-27.
111. Kulman JD, Harris JE, Haldeman BA, Davie EW (1997): Primary structure and tissue distribution of two novel proline-rich gamma-carboxyglutamic acid proteins. Proc Natl Acad Sci USA 94:9058-9062.
112. Lee B, Godfrey M, Vitale E, Hori H, Mattei MG, Sarfarazi M, Tsipouras P, Ramirez F, Hollister DW (1991): Linkage of Marfan syndrome and a phenotypically related disorder to two different fibrillin genes. Nature 352:330-334.
113. Lenting PJ, Donath M-JSH, van Mourik JA, Mertens K (1994): Identification of a binding site for blood coagulation factor IXa on the light chain of human factor VIII. J Biol Chem 269:7150-7155.
114. Lenting PJ, ter Maat H, Christophe OD, Rees DJG, Mertens K (1996): Calcium binding to the first epidermal growth factor-like domain of human blood coagulation factor IX promotes enzyme activity and factor VIII light chain binding. J Biol Chem 271:25332-25337.
115. 1818 of human blood coagulation factor VIII comprises a binding site for activated factor IX. J Biol Chem 271:1935-1940.
116. Lin SW, Smith KJ, Welsch D, Stafford DW (1990): Expression and characterization of human factor IX and factor IX-factor X chimeras in mouse C127 cells. J Biol Chem 265:144-150.
117. Lind B, Johnsen AH, Thorsen S (1997): Naturally occurring Arg(-1) to His mutation in human protein C leads to aberrant propeptide processing and secretion of dysfunctional protein C. Blood 89:2807-2816.
118. Lindahl U, Lindholt K, Spillmann D, Kjellen L (1994): More to "heparin" than anticoagulation. Thromb Res 75:1-32.
119. Lorand L, Jeong J-M, Radek JT, Wilson J (1993): Human plasma factor XIII: subunit interactions and activation of zymogen. Methods Enzymol 222:22-35.
120. Lu D, Kalafatis M, Mann KG, Long GL (1996): Comparison of activated protein C/protein S-mediated inactivation of human factor VIII and factor V. Blood 87:4708-4717.
121. Lundblad A, Svensson S (1973): Isolation and characterization of 3-O-†-D-Xylopyranosyl-D-Glucose and 2-O-†-L-Fucopyranosyl-D-Glucose from normal human urine. Biochemistry 12:306-309.
122. Lundwall Å, Dackowski W, Cohen EH, Shaffer M, Mahr A, Dahlbäck B, Stenflo J, Wydro RM (1986): Isolation and sequence of the cDNA for human protein S, a regulator of blood coagulation. Proc Natl Acad Sci USA 83:6716-6720.
123. Macfarlane RG (1964): An enzyme cascade in the blood clotting mechanism, and its function as a biochemical amplifier. Nature 202:498-499.
124. Majerus PW (1993): Platelets. Stamatoyannopoulos G, Nienhuis AW, Majerus PW, Varmus H (eds): "The Molecular Basis of Blood Diseases." Philadelphia: W.B. Saunders, pp. 753-785.
125. Malhotra OP (1981): Dicoumarol-induced prothrombins. Ann NY Acad Sci 370:426-437.
126. Malhotra OP, Nesheim ME, Mann KG (1985): The kinetics of activation of normal and γ-carboxyglutamic acid-deficient prothrombins. J Biol Chem 260:279-287.
127. Manfioletti G, Brancolini C, Avanzi G, Schneider C (1993): The protein encoded by a growth arrest-specific gene (gas6) is a new member of the vitamin K-dependent proteins related to protein S, a negative coregulator in the blood coagulation cascade. Mol Cell Biol 13:4976-4985.
128. Mann KG, Lorand L (1993): Introduction: blood coagulation. Methods Enzymol 222:1-10.
129. Mann KG, Nesheim ME, Church WR, Haley P, Krishnaswamy S (1990): Surface-dependent reactions of the vitamin K-dependent enzyme complexes. Blood 76: 1-16.
130. Maslen CL, Corson GM, Maddox BK, Glanville RW, Sakai LY (1991): Partial sequence of a candidate gene for the Marfan syndrome. Nature 352:334-337.
131. Mather T, Oganessyan V, Hof P, Huber R, Foundling S, Esmon C, Bode W (1996): The 2.8 A crystal structure of Gla-domainless activated protein C. EMBO J 15: 6822-6831.
132. McCord DM, Monroe DM, Smith KJ, Roberts HR (1990): Characterization of the functional defect in factor IX Alabama. Evidence for a conformational change due to high affinity calcium binding in the first epidermal growth factor domain. J Biol Chem 265:10250-10254.
133. McDonald JF, Evans TC Jr, Emeagwali DB, Hariharan M, Allewell NM, Pusey ML, Shah AM, Nelsestuen GL (1997a): Ionic properties of membrane association by vitamin K-dependent proteins: the case for univalency. Biochemistry 36:15589-15598.
134. McDonald JF, Shah AM, Schwalbe RA, Kisiel W, Dahlbäck B, Nelsestuen GL (1997b): Comparison of naturally occurring vitamin K-dependent proteins: correlation of amino acid sequences and membrane binding properties suggests a membrane contact site. Biochemistry 36:5120-5127.
135. Morrissey JH (1995): Tissue factor modulation of factor VIIa activity: use in measuring trace levels of factor VIIa in plasma. Thromb Haemost 74:185-188.
136. Morrissey JH, Macik BG, Neuenschwander PF, Comp PC (1993): Quantitation of activated factor VII levels in plasma using a tissue factor mutant selectively deficient in promoting factor VII activation. Blood 81:734-744.
137. Mroczkowski B, Reich M (1993): Identilication of biologically active epidermal growth factor precursor in human fluids and secretions. Endocrinology 132:417-425.
138. Muranyi A, Finn BE, Gippert GP, Forsén S, Stenflo, J Drakenberg T (1998): Solution structure of the N-terminal EGF-like domain from human factor VII. Biochemistry 37:10605-10615.
139. Naito K, Fujikawa K (1991): Activation of human blood coagulation factor XI independent of factor XII. Factor XI is activated by thrombin and factor XIa in the presence of negatively charged surfaces. J Biol Chem 266:7353-7358.
140. Nelsestuen GL, Kisiel W, Discipio RG (1978): Interaction of vitamin K dependent proteins with membranes. Biochemistry 17:2134-2138.
141. Nelsestuen GL, Suttie JW (1972): Mode of action of vitamin K. Calcium binding properties of bovine prothrombin. Biochemistry 11:4961-4964.
142. Nesheim ME, Canfield WM, Kisiel W, Mann KG (1982): Studies of the capacity of factor Xa to protect factor Va from proteolysis by activated protein C. J Biol Chem 257:1443-1447.
143. Nishimura H, Kawabata S-I, Kisiel W, Hase S, Ikenaka T, Takao T, Shimonishi Y, Iwanaga S (1989): Identification of a disaccharide (Xyl-Glc) and a trisaccharide (Xyl2-Glc) O-glycosidically linked to a serine residue in the first epidermal growth factor-like domain of human factors VII and IX and protein Z and bovine protein Z. J Biol Chem 264:20320-20325.
144. Ny T, Elgh F, Lund B (1984): The structure of the human tissue-type plasminogen activator gene: correlation of intron and exon structures to functional and structural domains. Proc Natl Acad Sci USA 81:5355-5359.
145. Nyberg P, Dahlbäck B, Garcia de Frutos P (1998): The SHBG-like region of protein S is crucial for factor V-dependent APC-cofactor function. FEBS Lett 433: 28-32.
146. Öhlin AK, Björk I, Stenflo J (1990): Proteolytic formation and properties of a fragment of protein C containing the γ-carboxyglutamic acid rich region and the EGF-like region. Biochemistry 29:644-651.
147. Ohlson S, Hansson L, Glad M, Mosbach K, Larsson P-O (1997): High performance liquid affinity chromatography: a new tool in biotechnology. Trends Biotechnol 7: 179-186.
148. Olivera BM (1997): E.E. Just Lecture, 1996. Conus venom peptides, receptor and ion channel targets, and drug design: 50 million years of neuropharmacology. Mol Biol Cell 8:2101-2109.
149. Olivera BM, Rivier J, Clark C, Ramillo CA, Corpuz GP, Abogadie FC, Mena EE, Woodward SR, Hillyard DR, Cruz LJ (1990): Diversity of Conus neuropeptides. Science 249:257-263.
150. Olivera BM, Rivier J, Scott JK, Hillyard DR, Cruz LJ (1991): Conotoxins. J Biol Chem 266:22067-22070.
151. Padmanabhan K, Padmanabhan KP, Tulinsky A, Park CH, Bode W, Huber R, Blankenship DT, Cardin AD, Kisiel W (1993): Structure of human Des(1-45) factor Xa at 2.2 Å resolution. J Mol Biol 232:947-966.
152. Patthy L (1985): Evolution of the proteases of blood coagulation and fibrinolysis by assembly from modules. Cell 41:657-663.
153. Patthy L (1994): Introns and exons. Curr Op Struct Biol 4:383-392.
154. Pei G, Powers DD, Lentz BR (1993): Specific contribution of different phospholipid surfaces to the activation of prothrombin by the fully assembled prothrombinase. J Biol Chem 268:3226-3233.
155. Pennica D, Holmes WE, Kohr WJ, Harkins RN, Vehar GA, Ward CA, Bennett WF, Yelverton E, Seeburg PH, Heyneker HL, Goeddel DV, Collen D (1983): Cloning and expression of human tissue-type plasminogen activator cDNA in E. coli. Nature 301:214-221.
156. 2+-binding to the light chain of factor X. Studies using isolated intact fragments containing the gamma-carboxyglutamic acid region and/or the epidermal growth factor-like domains. J Biol Chem 266:2444.
157. Persson E, Olsen OH, Östergaard A, Nielsen LS (1997): Calcium-binding to the first epidermal growth factor-like domain of factor VIIa increases amidolytic activity and tissue factor affinity. J Biol Chem 272: 19919-19924.
158. Persson E, Selander M, Drakenberg T, Öhlin AK, Stenflo J (1989): Calcium binding to the isolated β-hydroxyaspartic acid-containing epidermal growth factor containing domain of bovine factor X. J Biol Chem 264: 16897-16904.
159. Persson E, Valcarce C, Stenflo J (1991b): The gamma-carboxyglutamic acid and epidermal growth factor-like domains of factor X. Effects of isolated domains on prothrombin activation and endothelial cell binding of factor X. J Biol Chem 266:2453-2458.
160. Ploos van Amstel HK, Reitsma PH, van der Logt PE, Bertina RM (1990): Intro-exon organization of the active human protein S gene PSa and its pseudogene PSb: duplication and silencing during primate evolution. Biochemistry 29:7853-7861.
161. Prendergast FG, Mann KG (1977): Differentiaton of metal ion-induced transitions of prothrombin fragment 1. J Biol Chem 252:840-850.
162. Rand MD, Lindblom A, Carlsaon J, Villoutreix BO, Stenflo J (1997): Calcium-binding to tandem repeats of EGF-like modules. Expression and characterization of the EGF-like modules of human Notch-1 implicated in receptor-ligand interactions. Protein Sci 6:2059-2071.
163. Rao LVM, Rapaport SI, Hoang AD (1993): Binding of factor VIIa to tissue factor permits rapid antithrombin III/ Heparin inhibition of factor VIIa. Blood 81:2600-2607.
164. Rao VM, Nordfang O, Hoang D, Pendurthi UR (1995): Mechanism of antithrombin III inhibition of factor VIIa/ tissue factor activity on cell surfaces. Comparison with tissue factor pathway inhibitor/factor Xa-induced inhibition of factor VIIa/tissue factor activity. Blood 85: 121-129.
165. 2+-binding epidermal growth factor-like domain: its role in protein-protein interactions. Cell 82:131-141.
166. Rapaport SI, Rao VM (1995): The tissue factor pathway: how it has become a "prima ballerina". Thromb Haemost 74:7-17.
167. Ratcliff JV, Furie B, Furie BC (1993): The importance of specific γ-carboxyglutamic acid residues in prothrombin. J Biol Chem 268:24339-24345.
168. Rebay I, Fleming RJ, Fehon RG, Cherbas L, Cherbas P, Artavanis-Tsakonas S (1991): Specific EGF repeats of Notch mediate interactions with Delta and Serrate: implications for Notch as a multifunctional receptor. Cell 67:687-699.
169. Rezaie AR, Neuenschwander PF, Morrissey JH, Esmon CT (1993): Analysis of the functions of the first epidermal growth factor-like domain of factor X. J Biol Chem 268:8176-8180.
170. Roberts HR (1993): Molecular biology of hemophilia B. Thromb Haemost 70:1-9.
171. R506Q by activated protein C. J Biol Chem 270:27852-27858.
172. Rosing J, Tans G (1997): Coagulation factor V: an old star shines again. Thromb Haemost 78:427-433.
173. Ruf W, Kalnik MW, Lund-Hansen T, Edgington TS (1991): Characterization of factor VII association with tissue factor in solution. High and low affinity binding sites in factor VII contribute to functionally distinct interactions. J Biol Chem 266:15719-15725.
174. Sadler JE, Davie EW (1994): Hemophilia A, hemophilia B, and von Willebrand disease. Stamatoyannopoulos G, Nienhuis AW, Majerus PW, Varmus H (eds): "The Molecular Basis of Blood Disease." Philadelphia: W.B. Saunders, pp. 657-700.
175. Schmidel DK, Tatro AV, Phelps LG, Tomczak JA, Long GL (1990): Organization of the human protein S gene. Biochemistry 29:7845-7852.
176. Schwalbe RA, Ryan J, Stern DM, Kisiel W, Dahlbäck B, Nelsestuen GL (1989): Protein structural requirements and properties of membrane binding by γ-carboxyglutamic acid-containing plasma proteins and peptides. J Biol Chem 264:20288-20296.
177. Scott DL, White SP, Otwinowski Z, Yuan W, Gelb MH, Sigler PB (1990): Interfacial catalysis: the mechanism of phospholipase A2. Science 250:1541-1546.
178. Sekiya F, Yamashita T, Atoda H, Komiyama Y, Morita T (1995): Regulation of the tertiary structure and function of coagulation factor IX by magnesium (II) ions. J Biol Chem 270:14325-14331.
179. Sekiya F, Yoshida M, Yamashita T, Morita T (1996a): Localization of the specific binding site for magnesium(II) ions in factor IX. FEBS Lett 392:205-208.
180. Sekiya F, Yoshida M, Yamashita T, Morita T (1996b): Magnesium (II) is a crucial constituent of the blood coagulation cascade. J Biol Chem 271:8541-8544.
181. 2+-free form of the amino-terminal epidermal growth factor like domain in coagulation factor X. Biochemistry 29: 8111-8118.
182. 2-terminal EGF-like domain in coagulation factor X. J Biol Chem 267:19642-19649.
183. Seshadri TP, Skrzypczak Jankun E, Yin M, Tulinsky A (1994): Differences in the metal ion structure between Sr-and Ca-prothrombin fragment 1. Biochemistry 33:1087-1092.
184. Shah AM, Kisiel W, Foster DC, Nelsestuen GL (1998): Manipulation of the membrane binding site of vitamin K-dependent proteins: enhanced biological function of human factor VII. Proc Natl Acad Sci USA 95: 4229-4234.
185. Shen L, Dahlbäck B (1994): Factor V and protein S as synergistic cofactors to activated protein C in degradation of factor VIIIa. J Biol Chem 269:18735-18738.
186. Shigekiyo T, Uno Y, Kawauchi S, Saito S, Hondo H, Nishioka J, Hayashi T, Suzuki K (1993): Protein S Tokushima: an abnormal protein S found in a Japanese family with thrombosis. Thromb Haemost 70:244-246.
187. Solymoss S, Tucker MM, Tracy PB (1988): Kinetics of inactivation of membrane-bound factor V by activated protein C. J Biol Chem 263:14884-14890.
188. 2+-prothrombin fragment 1. Biochemistry 31:2554-2566.
189. Stenberg Y, Drakenberg T, Dahlbäck B, Stenflo J (1998): Characterization of recombinant epidermal growth factor (EGF)-like modules fom vitamin K-dependent protein S expressed in Spodoptera cells. The cofactor activity depends on the N-terminal EGF module in human protein S. Eur J Biochem 251:558-564.
190. Stenberg Y, Julenius K, Dahlqvist I, Drakenberg T, Stenflo J (1997a): Calcium-binding properties of the third and fourth epidermal-growth-factor-like modules in vitamin-K-dependent protein S. Eur J Biochem 248:163-170.
191. Stenberg Y, Linse S, Drakenberg T, Stenflo J (1997b): The high affinity calcium-binding sites in the epidermal growth factor module region of vitamin K-dependent protein S. J Biol Chem 272:23255-23260.
192. Stenberg Y, Muranyi A, Thulin E, Drakenberg T, Stenflo J (1999): Calcium binding properties of an epidermal growth factor-like module pair from human protein S. The epidermal growth factor-like module region in protein S appears to be involved in factor Xa binding. Manuscript.
193. Stenflo J (1991): Structure-function relationships of epidermal growth factor modules in vitamin K-dependent clotting factors. Blood 78:1637-1651.
194. Stenflo J, Dahlbäck B (1994): Vitamin K-dependent proteins. Stamatoyannopoulos G, Nienhuis AW, Majerus PW, Varmus H (eds): "The Molecular Basis of Blood Diseases." Philadelphia: W.B. Saunders, pp. 565-598.
195. 2+ to normal and Dicoumarol-induced prothrombin. Biochem Biophys Res Commun 50:98-104.
196. Stenflo J, Holme E, Lindstedt S, Chandramouli N, Tsai Huang LH, Tam J, Merrifield RB (1989): Hydroxylation of aspartic acid in domains homologous to the epidermal growth factor precursor is catalyzed by a 2-oxoglutarate-dependent dioxygenase. Proc Natl Acad Sci USA 86:444-447.
197. Stenflo J, Lundwall Å, Dahlbäck B (1987): Beta-hydroxyasparagine in domains homologous to the epidermal growth factor precursor in vitamin K-dependent protein S. Proc Natl Acad Sci USA 84:368-372.
198. Stenflo J, Suttie JW (1977): Vitamin K-dependent formation of gamma-carboxyglutamic acid. Annu Rev Biochem 46:157-172.
199. Stenllo J, Öhlin AK, Owen WG, Schneider WJ (1988): Beta-hydroxyaspartic acid or beta-hydroxyasparagine in bovine low density lipoprotein receptor and in bovine thrombomodulin. J Biol Chem 263:21-24.
200. Strynadka NCJ, James MNG (1991): Towards an understanding of the effects of calcium on protein structure and function. Curr Opin Struct Biol 1:905-914.
201. Sunnerhagen M, Forsen S, Hoffren AM, Drakenberg T, Teleman O, Stenflo J (1995): Structure of the Ca(2+)-free Gla domain sheds light on membrane binding of blood coagulation proteins. Nat Struct Biol 2:504-509.
202. 2+ binding to the first EGF domain. A combined NMR-small angle X-ray scattering study. Biochemistry 35:11547-11559.
203. Suttie J (1985): Vitamin K-dependent carboxylase. Annu Rev Biochem 54:459-477.
204. Suttie J (1993): Synthesis of vitamin K-dependent proteins. FASEB J 7:445-452.
205. Suzuki K, Hayashi T, Nishioka J, Kosaka Y, Zushi M, Honda G, Yamamoto S (1989): A domain composed of epidermal growth factor-like structures of human thrombomodulin is essential for thrombin binding and for protein C activation. J Biol Chem 264:4872-4876.
206. Suzuki K, Stenflo J, Dahlbäck B, Teodorson B (1983): Inactivation of human coagulation factor V by activated protein C. J Biol Chem 258:1914-1920.
207. Südhof TC, Goldstein JL, Brown MS, Russel DW (1985): The LDL receptor gene: a mosaic of exons shared with different proteins. Science 228:815-824.
208. Thim L, Bjoern S, Christensen M, Nicolaisen EM, Lund Hansen T, Pedersen T, Hedner U (1988): Amino acid sequence and posttranslational modifications of human factor VIIa from plasma and transfected baby hamster kidney cells. Biochemistry 27:7785-7793.
209. Toomey JR, Smith KJ, Roberts HR, Stafford DW (1992): The endothelial cell binding determinant of human factor IX resides in the gamma-carboxyglutamic acid domain. Biochemistry 31:1806-1808.
210. Toomey JR, Smith KJ, Stafford DW (1991): Localization of the human tissue factor recognition determinant of human factor VIIa. J Biol Chem 266:19198-19202.
211. Tsiang M, Lentz SR, Sadler JE (1992): Functional domains of membrane-bound human thrombomodulin. EGF-like domains four to six and the serine/threonine-rich domain are required for cofactor activity. J Biol Chem 267:6164-6170.
212. Tulinsky A, Park CH, Skrzypczak-Jankun E (1988): Structure of prothrombin fragment 1 refined at 2.8 Å resolution. J Mol Biol 202:885-901.
213. Ullner M, Selander M, Persson E, Stenflo J, Drakenberg T, Teleman O (1992): Three-dimensional structure of the apo form of the N-terminal EGF-like module of blood coagulation factor X as determined by NMR spectroscopy and simulated folding. Biochemistry 31: 5974-5983.
214. Ulrich MMM, Furie B, Vermeer C, Furie BB (1988): Vitamin K-dependent carboxylation: A synthetic peptide based upon the gamma-carboxylation recognition site sequence of the prothrombin propeptide is an active substrate for the carboxylase in vitro. J Biol Chem 263:9697-9702.
215. Valcarce C, Holmgren A, Stenflo J (1994): Calcium-dependent interaction between gamma-carboxyglutamic acid-containing and N-terminal epidermal growth factor-like modules in factor X. J Biol Chem 269:26011-26016.
216. van Wijnen, Stam JG, Chang GTG, Meijers JCM, Reitsma PH, Bertina RM, Bouma BN (1998): Characterization of mini-protein S, a recombinant variant of protein S that lacks the sex hormone binding globulin-like domain. Biochem J 330:389-396.
217. Varadi K, Rosing J, Tans G, Pabinger I, Keil B, Schwarz HP (1996): Factor V enhances the cofactor function of protein S in the APC-mediated inactivation of factor VIII: influence of the factor VR506Q mutation. Thromb Haemost 76:208-214.
218. Varnum BC, Young C, Elliott G, Garcia A, Bartley TD, Fridell Y-W, Hunt RW, Trall G, Clogston C, Toso RJ, Yanagihara C, Bennett L, Sylber M, Merewether LA, Tseng A, Escobar E, Liu ET, Yamane HK (1995): Axl receptor tyrosine kinase stimulated by the vitamin K-dependent protein encoded by growth-arrest-specific gene 6. Nature 373:623-626.
219. Verde P, Stoppelli MP, Galeffi P, Di Nocera P, Blasi F (1984): Identification and primary sequence of an unspliced human urokinase poly(A)+ RNA. Proc Natl Acad Sci USA 81:4727-4731.
220. Walker FJ, Sexton PW, Esmon CT (1979): The inhibition of blood coagulation by activated protein C through the selective inactivation of activated factor V. Biochem Biophys Acta 571:333-342.
221. Walker, FJ (1981): Interactions of protein S with membranes. Semin Thromb Haemost 14:216-221.
222. Wang Q, VanDusen WJ, Petroski CJ, Garsky VM, Stern AM, Friedman PA (1991): Bovine liver aspartyl beta-hydroxylase. Purification and characterization. J Biol Chem 266:14004-14010.
223. Ware J, Diaguid DL, Liebman HL, Rabiet M-J, Kasper CK, Furie BC, Furie B, Stafford DW (1989): Factor IX San Dimas: Substitution of glutamine for Arginine-4 in the propeptide leads to incomplete gamma-carboxylation and altered phospholipid binding properties. J Biol Chem 264:11401-11406.
224. Wasley LC, Rehemtulla A, Bristol JA, Kaufman RJ (1993): PACE/Furin processes the vitamin K-dependent profactor IX precursor within the secretory pathway. J Biol Chem 1993:8458-8465.
225. Watzke HH, Wallmark A, Hamaguchi N, Giardina P, Stafford DW, High KA (1991): Factor X Santo Domingo. Evidence that the severe clinical phenotype arises from a mutation blocking secretion. J Clin Invest 88:1685-1689.
226. Welsch DJ, Nelsestuen GL (1988): Amino-terminal alanine functions in a calcium-specific process essential for membrane binding by prothrombin fragment 1. Biochemistry 27:4939-4945.
227. Wharton KA, Johansen KM, Xu T, Artavanis Tsakonas S (1985): Nucleotide sequence for the neurogenic locus notch implies a gene product that shares homology with proteins containing EGF-like repeats. Cell 43:567-581.
228. Wu SM, Stanley TB, Mutucumarana VP, Stafford DW (1997): Characterization of the gamma-glutamyl carboxylase. Thromb Haemost 78:599-604.
229. Yegneswaran S, Wood GM, Esmon CT, Johnson AE (1997): Protein S alters the active site location of activated protein C above the membrane surface. A fluorescence resonance energy transfer study of topography. J Biol Chem 272:25013-25021.
230. Zhang L, Castellino FJ (1994): The binding energy of human coagulation protein C to acidic phospholipid vesicles contains a major contribution from leucine 5 in the gamma-carboxyglutamic acid domain. J Biol Chem 269:3590-3595.
231. Zushi M, Gomi K, Yamamoto S, Maruyama I, Hayashi T, Suzuki K (1989): The last three consecutive epidermal growth factor-like structures of human thrombomodulin comprise the minimum functional domain for protein C-activating cofactor activity and anticoagulant activity. J Biol Chem 264:10351-10353.