Hamostaseologie 1989; 09(03): 157-166
DOI: 10.1055/s-0038-1655264
Originalarbeiten
Schattauer GmbH

Das vaskuläre Antikoagulans (VAC), ein Annexin mit einem neuen Mechanismus der Antikoagulation

C. P. M Reutelingsperger
1   Department für Biochemie, Universität Limburg, Maastricht (Niederlande)
› Author Affiliations
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Publication History

Publication Date:
25 June 2018 (online)

 

 
  • LITERATUR

  • 1 Back R, Gentry R, Nemerson Y. Factor VII binding to tissue factor in reconstituted phospholipid vesicles: induction of cooperativity by phosphatidylserine. Biochemistry 1986; 25: 4007-20.
  • 2 Bangham A D. A correlation between surface charge and coagulant action of phospholipids. Nature 1961; 192: 1197-8.
  • 3 Barrowcliffe T W, Thomas D R. Antithrombin III and heparin. In: Bloom A L, Thomas D P. (Eds). Haemostasis and Thrombosis. 2nd. ed. Edinburgh: Churchill Livingstone; 1987: 849-69.
  • 4 Barton P G, Jackson C M, Hanahan D J. Relationship between factor v and activated factor X in the generation of prothrombinase. Nature 1967; 214: 923-4.
  • 5 Barton P G. Sequence theories of blood coagulation re-evaluated with reference to lipid protein interactions. Nature 1967; 215: 1508-9.
  • 6 Broze Jr G J, Miletich J P. Isolation of the tissue factor inhibitor produced by Hep G2 hepatoma cells. Proc Natl Acad Sci USA 1987; 84: 1886-90.
  • 7 Broze Jr G J, Miletich J P. Characterization of the inhibition of tissue factor in serum. Blood 1987; 69: 150-55.
  • 8 Burgoyne R D. Calpactin in exocytosis. Nature 1988; 331: 20.
  • 9 Chap H, Comfurius P, Bevers E M, Fauvel J, Vicendo P, Douste-Blazy L, Zwaal R F A. Potential anticoagulant activity of lipocortins and other calcium/phospholipid binding proteins. Biochem Biophys Res Commun 1988; 150: 97-8.
  • 10 Cole E R, Koppel J L, Olwin J H. Phospholipid-protein interactions in the formation of prothrombin activator. Thrombos Diathes Haemorrh 1965; 14: 431-44.
  • 11 Comp P C, Esmon C T. Activated protein C inhibits platelet prothrombin-converting activity. Blood 1979; 54: 1272-81.
  • 12 Cooper J A, Hunter T. Regulation of cell growth and transformation by tyrosine specific protein kinases: the search for important cellular substrate proteins. Curr Topics Microbiol Immunol 1983; 107: 125-61.
  • 13 Creutz C E, Zaks W J, Hamman H C, Crane S, Martin W H, Gould K L, Oddie K M, Parsons S J. Identification of chromaffin granule-binding proteins. J Biol Chem 1987; 262: 1860-8.
  • 14 Crompton M R, Moss S E, Crumpton M J. Diversity in the lipocortin/calpactin family. Cell 1988; 55: 1-3.
  • 15 Crompton M R, Owens R J, Totty N F, Moss S E, Waterfield M D, Crumpton M J. Primary structure of the human membrane associated Ca2+-binding protein p68: a novel member of a protein family. EMBO J 1988; 07: 21-27.
  • 16 Davidson F F, Dennis E A, Powell M, Glenney Jr J R. Inhibition of phospholipase A2 by »lipocortins« and calpactins. J Biol Chem 1987; 262: 1698-705.
  • 17 Davie E W, Ratnoff D D. Waterfall sequence for intrinsic blood clotting. Science 1964; 145: 1310-1.
  • 18 Di Rosa M, Flower R J, Hirata F, Parente L, Russa-Marie F. Nomenclature announcement. Antiphospholipase proteins. Prostaglandins 1984; 28: 441-2.
  • 19 Drust D S, Creutz C E. Aggregation of chromaffin granules by calpactin at micromolar levels of calcium. Nature 1988; 331: 88-91.
  • 20 Esmon C T, Suttie J W, Jackson C M. The functional significance of vitamin K-action. Difference in phospholipid binding between normal and abnormal prothrombin. J Biol Chem 1975; 205: 4095-9.
  • 21 Esnouf M P, Jobin F. Lipids in prothrombin conversion. Thrombos Diathes Haemorrh 1965; 17: 103-10.
  • 22 Evans H J, Franson R, Qureshi G D, MooPenn W F. Isolation of anticoagulant proteins from cobra venom (Maja nigricollis). Identity with phospholipases A2 . J Biol Chem 1980; 255: 3793-7.
  • 23 Fava R A, Cohen S. Isolation of a calciumdependent 35 kilodalton substrate for the epidermal growth factor receptor/kinase from A-431 cells. J Biol Chem 1984; 259: 2636-45.
  • 24 Flower R J. Lipocortin and the mechanism of action of the glucocorticoids. Br J Pharmacol 1988; 94: 987-1015.
  • 25 Flower R J, Wood J N, Parente L. Macrocortin and the mechanism of action of the glucocorticoids. Adv. Inflammation Res 1984; 07: 61-69.
  • 26 Freyssinet J M, Wiesel M L, Gauchy J, Boneu B, Cazenave J P. An IgM lupus anticoagulant that neutralizes the enhancing effects of phospholipid on purified endothelial thrombomodulin activity. A mechanism for thrombosis. Thromb Haemost 1986; 55: 309-13.
  • 27 Funakoshi T, Heimark R L, Hendrickson L E, McMullen B A, Fujikawa K. Human placental anticoagulant protein: isolation and characterization. Biochemistry 1987; 26: 5572-8.
  • 28 Funakoshi T, Hendrickson L E, McMullen B A, Fujikawa K. Primary structure of human placental anticoagulant protein. Biochemistry 1987; 26: 8087-92.
  • 29 Geisow M J, Walker J H. New proteins involved in cell regulation by Ca2+ and phospholipids. Trends in Bioch Sc 1986; 11: 420-23.
  • 30 Geisow M J. Common domain structure of Ca2+ and lipid-binding proteins. FEBS Lett 1986; 203: 99-103.
  • 31 Geisow M I, Fritsche U, Hexham I M, Dash B, Johnson T. A consensus-amino acid sequence repeat in Torpedo and mammalian Ca2+-dependent membranebinding proteins. Nature 1986; 320: 636-38.
  • 32 Gerke V, Weber K. Identity of p36K phosphorylated upon Rous sarcoma virus transformation with a protein purified from brush borders; calcium-dependent binding to non-erythroid spectrin and Factin. EMBO J 1984; 03: 227-33.
  • 33 Glenney J, Zokas L. Antibodies to the Nterminus of calpactin II (p 35) affect Ca2+binding and phosphorylation by the epidermal growth factor receptor in vitro. Biochemistry 1988; 27: 2069-76.
  • 34 Glenney J. Phospholipid-dependent Ca2+binding by the 36-kDa Tyrosine kinase substrate (calpactin) and its 33-kDa core. J Biol Chem 1986; 261: 7247-52.
  • 35 Glenney Jr J R, Tack B, Powell M A. Calpactins: Two distinct Ca2+-regulated phospholipidand actin binding proteins isolated from lung and placenta. J Cell Biol 1987; 104: 503-11.
  • 36 Glenney J R. Two related but distinct forms of the Mr 36,000 tyrosine kinase substrate (calpactin) that interact with phospholipid and actin in a Ca2+-dependent manner. Proc Natl Acad Sci USA 1986; 83: 4258-62.
  • 37 Glenney Jr J R, Tack B F. Amino-terminal sequence of p 36 and associated p 10: identification of the site of tyrosine phosphorylation and homology with S-100. Proc Natl Acad Sci USA 1985; 82: 7884-8.
  • 38 Gould K L, Woodgett J R, Isacke C M, Hunter T. The protein-tyrosine kinase substrate, p 36, is also substrate for protein kinase C in vitro and in vivo. Mol Cell Biol 1986; 06: 2738-44.
  • 39 Govers-Riemslag J W P, Speyer H, Zwaal R F A, Rosing J. The effects of bovine prothrombin fragment 1 and fragment 1.2 on prothrombin activation. Thrombos Res 1985; 38: 375-88.
  • 40 Grundmann U, Abel K-J, Bohn H, Löbermann H, Lottspeich F, Kueper H. Characterization of cDNA encoding human placental anticoagulant protein (PP 4) : homology with the lipocortin family. Proc Natl Acad Sei USA 1988; 85: 3708-12.
  • 41 Haigler H T, Schlaepfer D D, Wilson H B. Characterization of lipocortin I and an immunologically unrelated 33-kda protein as epidermal growth factor receptor/kinase substrate and phospholipase A2 inhibitors. J Biol Chem 1987; 262: 6921-30.
  • 42 Hemker H C, Kahn M J P. Reaction sequence of blood coagulation. Nature 1967; 215: 1201-2.
  • 43 Hemker H C, Esnouf P, Hemker P W, Swart A C W, MacFarlane R G. Formation of prothrombin converting activity. Nature 1967; 215: 248-51.
  • 44 Hemker H C, Kahn M J P, Devilee P P. The absorption of coagulation factors onto phospholipids. Thromb Diathes Haemorrh 1970; 24: 213-23.
  • 45 Hemker H C, Muller A D, Loeliger E A. Two types of prothrombin in vitamin K deficiency. Thrombos Diathes Haemorrh 1970; 23: 632-7.
  • 46 Hemker H C, Veltkamp J J, Loeliger E A. Kinetic aspects of the interaction of blood clotting enzymes. Thrombos Diathes Haemorrh 1968; 19: 345-63.
  • 47 Hemker H C, Veltkamp J J, Hensen A, Loeliger E A. Nature of prothrombin biosynthesis: preprothrombinaemia in vitamin K-deficiency. Nature 1963; 200: 589-90.
  • 48 Hirata F. Roles of lipomodulin: a phospholipase inhibitory protein in immunoregulation. Adv Inflammation Res 1984; 07: 71-8.
  • 49 Hornstra G, Hemker H C. Clot-promoting effect of platelet-vessel wall interaction: influence of dietary fats and relation to arterial thrombus formation in rats. Haemostasis 1979; 08: 211-26.
  • 50 Hougie C, Biggs R, Denson K W E. A study of the reaction product of factor VIII and factor IX by gel filtration. Thromb Diathes Haemorrh 1967; 18: 211-22.
  • 51 Huang K-S, McGray P, Mattaliano R J, Burne C, Chow E P, Sinclair L K, Pepinsky R B. Purification and characterization of proteolytic fragments of lipocortin I that inhibit phospholipase A2 . J Biol Chem 1987; 262: 7639-45.
  • 52 Huang K S, Wallner B P, Mattaliano R J, Tizard R, Burne C, Frey A, Hession C, McGray P, Sinclair L K, Chow E P, Browning J L, Ramachandran K L, Tang J, Smart J E, Pepinsky R B. Two human 35 kd inhibitors of phospholipase A2 are related to substrates of pp 60v-src and of the epidermal growth factor receptor kinase. Cell 1986; 46: 191-9.
  • 53 Iwasaki A, Suda M, Nakao H, Nagoya T, Saino Y, Arai K, Mizoguchi T, Sato F, Yoshizaki H, Hirata M, Miyata T, Shidara Y, Murata M, Maki M. Structure and expression of cDNA for an inhibitor of blood coagulation isolated from human placenta: a new lipocortin-like protein. J Biochem 1987; 102: 1261-73.
  • 54 Jackson C M, Nemerson Y. Blood coagulation. Ann Rev Biochem 1980; 49: 765-811.
  • 55 Kaplan R, Jaye M, Burgess W H, Schlaepfer D D, Haigler H T. Cloning and expression of cDNA for human endonexin II, a Ca2+ and phospholipid binding protein. J Biol Chem 1988; 263: 8037-43.
  • 56 Kondo S, Noguchi M, Funakoshi T, Fujikawa K, Kisiel W. Inhibition of human factor VIIa-tissue factor activity by placental anticoagulant protein. Thromb Res 1987; 48: 449-59.
  • 57 Kretsinger R H. Structure and evolution of calcium-modulated proteins. CRC Crit Rev Biochem 1980; 08: 119-74.
  • 58 Kristensen T, Saris C J M, Hunter T, Hicks L J, Noonan D J, Glenney Jr J R, Tack B F. Cloning of bovine calpactin I heavy chain (p36), a major substrate for the protein-tyrosine kinase pp 60src. Homology with the human phospholipase A2 inhibitor, lipocortin. Biochemistry 1986; 21: 4997-503.
  • 59 Lim T K, Bloomfield V A, Nelsestuen G L. Structure of the prothrombinand blood clotting factor X-membrane complex. Biochemistry 1977; 16: 4177-81.
  • 60 Lindhout T, Govers-Riemslag J W P, van de Waart P, Hemker H C, Rosing J. Factor Va-factor Xa interaction. Effects of phospholipid vesicles of varying composition. Biochemistry 1982; 21: 5494-502.
  • 61 MacFarlane R G. An enzyme cascade in the blood clotting mechanism and its function as biochemical amplifier. Nature 1964; 202: 498-9.
  • 62 Magnusson S, Sottrup-Jensen L, Peterson T E, Morris H R, Dell A. Primary struc, ture of the vitamin K-dependent part of prothrombin. FEBS Lett 1974; 44: 189-93.
  • 63 Mann K G. The assembly of blood clotting complexes on membranes. Trends in Biochem Sc 1987; 12: 229-33.
  • 64 Marcus A J. The role of lipids in blood coagulation. Adv Lipid Res 1966; 04: 1-37.
  • 65 Maurer-Fogy I, Reutelingsperger C P M, Pieters J, Bodo G, Stratowa C, Hauptmann R. Cloning and expression of cDNA for human vascular anticoagulant, a Ca2+ dependent phospholipid-binding protein. Eur J Biochem 1988; 174: 585-92.
  • 66 Miele L, Cordella-Miele E, Facchiano A, Mukherjee A B. Novel antiinflammatory peptides from the region of highest similarity between uteroglobin and lipocortin I. Nature 1988; 335: 726-30.
  • 67 Moore P B. 67 kDa calcimedin, a new Ca2+-binding protein. Biochem J 1986; 238: 49-54.
  • 68 Nawroth P P, Stern D M. Endothelial cells as active participants in procoagulant reactions. In: Gimbrone Jr M. (Ed). Vascular Endothelium in Hemostasis and Thrombosis. Edinburgh: Churchill Livingstone; 1986: 14-39.
  • 69 Nawroth P P, Kisiel W, Stern D M. Anticoagulant and antithrombotic properties of a ã-carboxyglutamic acid-rich peptide derived from the light chain of blood coagulation factor X. Thrombos Res 1986; 44: 625-37.
  • 70 Nelsestuen G L, Broderius M. Interaction of prothrombin and blood clotting factor X with membranes of varying composition. Biochemistry 1977; 16: 4172-7.
  • 71 Nelsestuen G L, Lim T K. Equilibria involved in prothrombinand blood-clotting factor X-membrane binding. Biochemistry 1977; 19: 4164-71.
  • 72 Nelsestuen G L, Suttie J W. The purification and properties of an abnormal prothrombin protein produced by dicoumaroltreated cows. J Biol Chem 1972; 247: 8176-82.
  • 73 Nelsestuen G L, Suttie J W. Mode of action of Vitamin K. Calcium binding properties of bovine prothrombin. Biochemistry 1972; 11: 4961-4.
  • 74 Nelsestuen G L, Broderius M, Martin G. Role of ã-carboxyglutamic acid. J Biol Chem 1976; 251: 6886-93.
  • 75 Nelsestuen G L, Zytkovicz T H, Howard J A. The mode of action of vitamin K. Identification of ã-carboxyglutamic acid as a component of prothrombin. J Biol Chem 1974; 249: 6347-50.
  • 76 Nemerson Y, Furie B. Zymogens and cofactors of blood coagulation. CRC Critical Rev Biochem 1980; 09: 45-85.
  • 77 Nemerson Y. Tissue factor and hemostasis. Blood 1988; 71: 1-8.
  • 78 Nesheim M E, Taswell J B, Mann K G. The contribution of bovine factor V and factor Va to the activity of prothrombinase. J Biol Chem 1979; 254: 10952-62.
  • 79 Op den Kamp J A F. Lipid asymmetry in membranes. Ann Rev Biochem 1979; 48: 47-71.
  • 80 Owens R J, Crumpton M J. Isolation and characterization of a novel 68000-Mr Ca2+binding protein of lymphocyte membrane. Biochem J 1984; 219: 309-16.
  • 81 Owren P A, Stormorken H. The mechanism of blood coagulation. Ergebnisse der gesamten Physiologie und experimentellen Pharmakologie 1973; 68: 2-53.
  • 82 Papahadjopoulos D, Hanahan D J. Observations on the interaction of phospholipids and certain clotting factors in prothrombin activator formation. Biochim Biophys Acta 1964; 90: 436-9.
  • 83 Papahadjopoulos D, Hougic C, Hanahan D J. Influence of surface charge of phospholipids on their clot-promoting activity. Proc Soc Exp Biol Med 1962; 111: 412-6.
  • 84 Pepinsky R B, Sinclair L K, Browning J L, Mattaliano R J, Smart J E, Chow E P, Falbel T, Ribolini A, Garwin J L, Wallner B P. Purification and partial sequence analysis of a 37-kda protein inhibits phospholipase A2 activity from rat peritoneal exudates. J Biol Chem 1986; 261: 4239-46.
  • 85 Pepinsky R B, Tizard R, Mattaliano R J, Sinclair L K, Miller G T, Browning J L, Chow E F, Burne C, Huang K-S, Pratt D, Wächter L, Hession C, Frey A Z, Wallner B P. Five distict calcium and phospholipid proteins share homology with lipocortin I. J Biol Chem 1988; 263: 10799-811.
  • 86 Pfaeffle M, Ruggiero F, Hofmann H, Fernandez M P, Selmin O, Yamada Y, Garrone R, von der Mark K. Biosynthesis, secretion and extracellular localization of anchorin CII, a collagen-binding protein of the calpactin family. EMBO J 1988; 07: 2335-42.
  • 87 Powell M A, Glenney J R. Regulation of calpactin I phospholipid binding by calpactin I light chain binding and phosphorylation by p60v-src . Biochem J 1987; 247: 321-8.
  • 88 Rao L V M, Rapaport S I. Studies of a mechanism inhibiting the initiation of the extrinsic pathway of coagulation. Blood 1987; 69: 645-51.
  • 89 Reekers P P M, Lindhout M J, Kop-Klaassen B H M, Hemker H C. Demonstration of three anomalous plasma proteins induced by a vitamin K antagonist. Biochim Biophys Acta 1973; 317: 559-62.
  • 90 Reutelingsperger C P M. Vascular anticoagulant a new physiological anticoagulant mechanism. Thesis. University of Limburg; Maastricht, the Netherlands: 1987
  • 91 Reutelingsperger C P M, Hornstra G, Hemker H C. Isolation and partial purification of a novel anticoagulant from arteries of human umbilical cord. Eur J Biochem 1985; 151: 625-9.
  • 92 Reutelingsperger C P M, Kop J M M, Hornstra G, Hemker H C. Purification and characterization of a novel protein from bovine aortic intima inhibits coagulation. Eur J Biochem 1988; 173: 171-8.
  • 93 Rosing J, Tans G, Govers-Riemslag J W P, Zwaal R F A, Hemker H C. The role of phospholipids and factor va in the prothrombinase complex. J Biol Chem 1980; 255: 274-83.
  • 94 Salem H H. The natural anticoagulants. Clin Haematol 1986; 15: 371-91.
  • 95 Sanders N L, Bajaj S P, Zivelin A, Rapaport S I. Inhibition of tissue factor/factor Vila activity in plasma requires factor X and an additional plasma component. Blood 1985; 66: 204-12.
  • 96 Saris C J M, Tack B F, Kristensen T, Glenney Jr J R, Hunter T. The cDNA sequence for the protein-tyrosine kinase substrate p36 (Calpactin I heavy chain) reveals a multidomain protein with internal repeats. Cell 1986; 46: 201-12.
  • 97 Suttie J W. Control of clotting factor biosynthesis by vitamin K. Fed Proc 1969; 28: 1696-701.
  • 98 Schlaepfer D D, Haigler H T. Characterization of Ca2+-dependent phospholipid binding and phosphorylation of lipocortin. I. J Biol Chem 1987; 262: 6931-7.
  • 99 Schlaepfer D D, Haigler H T. In vitro protein kinase C phosphorylation site of placental lipocortin. Biochemistry 1988; 27: 4253-8.
  • 100 Schlaepfer D D, Mehlman T, Burgess W H, Haigler H T. Structural and functional characterization of endonexin II, a calciumand phospholipid binding protein. Proc Natl Acad Sei USA 1987; 84: 6078-82.
  • 101 Shadle P J, Weber K. Calcium binding protein from porcine intestine binds to phosphatidylserine vesicles in the presence of calcium. Biochim Biophys Acta 1987; 897: 502-6.
  • 102 Shadle P J, Gerke V, Weber K. Three Ca2+-binding proteins from porcine liver and intestine differ immunologically and physiochemically and are distinct in Ca2+affinities. J Biol Chem 1985; 260: 16354-60.
  • 103 Sperling R, Furie B C, Blumenstein M, Keyt B, Furie B. Metal binding properties of ã-carboxyglutamic acid. J Biol Chem 1978; 253: 3898-906.
  • 104 Stenflo J, Ganrot P O. Binding of Ca2+ to normal and dicoumarol-induced prothrombin. Biochem Biophys Res Commun 1973; 50: 98-104.
  • 105 Stenflo J, Ganrot P O. Vitamin K and the biosynthesis of prothrombin. Identification and purification of dicoumarol-induced prothrombin from bovine plasma. J Biol Chem 1972; 247: 8160-6.
  • 106 Stenflo J, Suttie J W. Vitamin Independent formation of ã-carboxy glutamic acid. Ann Rev Biochem 1977; 46: 157-72.
  • 107 Stenflo J, Ferlund P, Egan W, Roepstorff P. Vitamin K dependent modifications of glutamic acid residues in prothrombin. Proc Natl Acad Sci USA 1974; 71: 2730-3.
  • 108 Südhof T C, Ebbecke M, Walker J H, Fritsche U, Boustead C. Isolation of mammalian calelectrins : a new class of ubiquitous Ca2+-regulated proteins. Biochemistry 1984; 23: 1103-9.
  • 109 Südhof T C, Slaughter C A, Leznicky I, Barjon P, Reijnolds G A. Human 67-kDa calectrin contains a duplication of four repeats found in 35-kDa lipocortins. Proc Natl Acad Sci USA 1988; 85: 664-8.
  • 110 Südhof T C, Walker J H, Obrocki J. Calelectrin self-aggregates and promotes membrane aggregation in the presence of calcium. EMBO J 1982; 01: 1167-70.
  • 111 Suzuki K, Dählbeck B, Stenflo J. Thrombin-catalyzed activation of human coagulation factor V. J Biol Chem 1982; 257: 6556-64.
  • 112 Tait J F, Sakata M, McMullen B A, Miao C H, Funakoshi T, Hendrickson L E, Fujikawa K. Placental anticoagulant proteins: isolation and comparative characterization of four members of the lipocortin family. Biochemistry 1988; 27: 6268-76.
  • 113 Thiagarajan P, Shapiro S S, De Marco L. Monoclonal immunoglobulin M lambda coagulation inhibitor with phospholipid specificity. Mechanism of a lupus anticoagulant. J Clin Invest 1980; 66: 397-405.
  • 114 Tracy P B, Eide L L, Mann K G. Human prothrombinase complex assembly and function on isolated peripheral blood cell populations. J Biol Chem 1985; 260: 2119-24.
  • 115 Travis J, Salvesen G S. Human plasma proteinase inhibitors. Ann Rev Biochem 1983; 52: 655-709.
  • 116 Tufty R M, Kretsinger R H. Troponin and parvalbumin calcium-binding regions predicted in myosin light chain and T4 lysozyme. Science 1975; 187: 167-9.
  • 117 van Dieijen G, Tans G, Rosing J, Hemker H C. The role of phospholipid and factor VIIIa in the activation of bovine factor X. J Biol Chem 1981; 256: 3433-42.
  • 118 van Dieijen G, van Rijn J L ML, Govers-Riemslag J W P, Hemker H C, Rosing J. Assembly of the intrinsic factor X activating complex-interactions between factor IXa, factor VIIIa and phospholipid. Thrombos Haemostas 1985; 53: 396-400.
  • 119 Vehar G A, Davie E W. Preparation and properties of bovine factor VIII (antihemophilic factor). Biochemistry 1980; 19: 401-10.
  • 120 Verhey H M, Boffa M C, Rothen C, Bryckaert M C, Verger R, de Haas G H. Correlation of enzymatic activity and anticoagulant properties of phospholipase A2 . Eur J Biochem 1980; 112: 25-32.
  • 121 Walker F J, Sexton P W, Esmon C T. The inhibition of blood coagulation by activated protein C through the selective inactivation of activated factor V. Biochim Biophys Acta 1979; 571: 333-42.
  • 122 Wallner B P, Mattaliano R J, Hession C, Cate R L, Tizard R, Sinclair L K, Foeller C, Chow E P, Browning J L, Ramachandran K L, Pepinsky R B. Cloning and expression of human lipocortin, a phospholipase A2 inhibitor with potential antiinflammatory activity. Nature 1986; 320: 77-81.
  • 123 Weber K, Johnsson N, Plessmann U, Van P H, Soeling H-D, Ampe C, van de Kerckhove J. The amino acid sequence of protein II and its phosphorylation site for protein kinase C, the domain structure Ca2+-modulated lipid proteins. EMBO J 1987; 06: 1599-604.
  • 124 Zokas L, Glenney Jr J R. The calpactin light chain is tightly linked to the cytoskeletal form of calpactin I: studies using monoclonal antibodies to calpactin subunits. J Cell Biol 1987; 105: 2111-21.
  • 125 Østerud B, Rapaport S I. Synthesis of instrinsic factor X activator. Biochemistry 1970; 09: 1854-61.
  • 126 Zwaal R F A. Membrane and lipid involvement in blood coagulation. Biochim Biophys Acta 1978; 515: 163-205.
  • 127 Zwaal R F A, Bevers E M, Comfurius R. Platelets and coagulation. In: Zwaal R F A, Hemker H C. (Eds). Blood Coagulation. Amsterdam: Elsevier; 1986: 141-69.