The tale of protein S and C4b-binding protein, a story of affection

• References

• 1 Stenflo J, Fernlund P, Egan W. et al. Vitamin K dependent modifications of glutamic acid residues in prothrombin. Proc Natl Acad Sci USA 1974; 71: 2730-2733.
• 2 Stenflo J, Dahlbäck B. Vitamin K-dependent Proteins in Blood Coagulation. In: The Molecular Basis of Blood Disease. 3rd ed. W. B. Saunders Company; Philadelphia: 2000. pp. 579-613.
• 3 Stenflo J. From gamma-carboxy-glutamate to protein C. J Thromb Haemost 2006; 4: 2521-2526.
• 4 Stenflo J. A new vitamin K-dependent protein. Purification from bovine plasma and preliminary characterization. J Biol Chem 1976; 251: 355-363.
• 5 Di Scipio RG, Hermodson MA, Yates SG. et al. A comparison of human prothrombin, factor IX (Christmas factor), factor X(Stuart factor), and protein S. Biochemistry 1977; 16: 698-706.
• 6 Dahlback B, Stenflo J. High molecular weight complex in human plasma between vitamin K-dependent protein S and complement component C4b-binding protein. Proc Natl Acad Sci USA 1981; 78: 2512-2516.
• 7 Walker FJ. Regulation of activated protein C by a new protein. A possible function for bovine protein S. J Biol Chem 1980; 255: 5521-5524.
• 8 Dahlback B, Stenflo J. Binding of bovine coagulation factor Xa to platelets. Biochemistry 1978; 17: 4938-4945.
• 9 Dahlback B. Humancoagluationfactor Vpurificationand thrombin-catalyzed activation. J Clin Invest 1980; 66: 583-591.
• 10 Dahlback B, Stenflo J. Inhibitory effect of activated protein C on activation of prothrombin by platelet-bound factor Xa. Eur J Biochem 1980; 107: 331-335.
• 11 Dahlback B, Stenflo J. The activation of prothrombin by platelet-bound factor Xa. Eur J Biochem 1980; 104: 549-557.
• 12 Dahlback B, Smith CA, Muller-Eberhard HJ. Visualization of human C4b-binding protein and its complexes with vitamin K-dependent protein S and complement protein C 4b. Proc Natl Acad Sci USA 1983; 80: 3461-3465.
• 13 Dahlback B, Muller-Eberhard HJ. Ultrastructure of C4b-binding protein fragments formed by limited pro-teolysis using chymotrypsin. J Biol Chem 1984; 259: 11631-11634.
• 14 Dahlbäck B, Stenflo J. The Protein C Anticoagulant System. In: The Molecular Basis of Blood Disease. 3rd ed. W. B. Saunders Company; Philadelphia: 2000. pp. 614-656.
• 15 Rezende SM, Simmonds RE, Lane DA. Coagulation, inflammation, and apoptosis: different roles for protein S and the protein S-C4b binding protein complex. Blood 2004; 103: 1192-1201.
• 16 Rigby AC, Grant MA. Protein S: a conduit between anticoagulation and inflammation. Crit Care Med 2004; 32 (Suppl. 05) S336-341.
• 17 Hansson K, Stenflo J. Post-translational modifications in proteins involved in blood coagulation. J Thromb Haemost 2005; 3: 2633-2648.
• 18 Dahlback B. Protein S and C4b-binding protein: components involved in the regulation of the protein C anticoagulant system. Thromb Haemost 1991; 66: 49-61.
• 19 Nelsestuen GL, Shah AM, Harvey SB. Vitamin K-dependent proteins. Vitam Horm 2000; 58: 355-389.
• 20 Saller F, Villoutreix BO, Amelot A. et al. The gamma-carboxyglutamic acid domain of anticoagulant protein S is involved in activated protein C cofactor activity, independently of phospholipid binding. Blood 2005; 105: 122-130.
• 21 Drakenberg T, Ghasriani H, Thulin E. et al. Solution structure of the Ca2+-Binding EGF3-4 pair from vitamin K-dependent protein S: identification of an un-usual fold in EGF3. Biochemistry 2005; 44: 8782-8789.
• 22 Persson KE, Stenflo J, Linse S. et al. Binding of calcium to anticoagulant protein S: role of the fourth EGF module. Biochemistry 2006; 45: 10682-10689.
• 23 Dahlback B, Villoutreix BO. The anticoagulant protein C pathway. FEBS Lett 2005; 579: 3310-3316.
• 24 Dahlback B, Villoutreix BO. Regulation of blood coagulation by the protein C anticoagulant pathway: novel insights into structure-function relationships and molecular recognition. Arterioscler Thromb Vasc Biol 2005; 25: 1311-1320.
• 25 Yegneswaran S, Wood GM, Esmon CT. et al. 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 1997; 272: 25013-25021.
• 26 Stern DM, Nawroth PP, Harris K. et al. Cultured bovine aortic endothelial cells promote activated protein C-protein S-mediated inactivation of factor Va. J Biol Chem 1986; 261: 713-718.
• 27 Hackeng TM, Hessing M, van’t Veer C. et al. Protein S binding to human end othelialcells is required for expression of cofactor activity for activated protein C. J Biol Chem 1993; 268: 3993-4000.
• 28 Norstrom EA, Tran S, Steen M. et al. Effects of factor Xa and protein S on the individual activated protein C-mediated cleavages of coagulation factor Va. J Biol Chem 2006; 281: 31486-31494.
• 29 Autin L, Steen M, Dahlback B. et al. Proposed structural models of the prothrombinase (FXa-FVa) complex. Proteins 2006; 63: 440-450.
• 30 Nicolaes GA, Dahlback B. Factor V and thrombotic disease: description of a janus-faced protein. Arterioscler Thromb Vasc Biol 2002; 22: 530-538.
• 31 Hackeng TM, van’t Veer C, Meijers JC. et al. Human protein S inhibits prothrombinase complex activity on endothelial cells and platelets via direct interactions with factors Va and Xa. J Biol Chem 1994; 269: 21051-21058.
• 32 Heeb MJ, Mesters RM, Tans G. et al. Binding of protein Stofactor Va associated with inhibition of prothrombinase that is independent of activated protein C. J Biol Chem 1993; 268: 2872-2877.
• 33 Heeb MJ, Rosing J, Bakker HM. et al. Protein S binds to and inhibits factor Xa. Proc Natl Acad Sci USA 1994; 91: 2728-2732.
• 34 van’t Veer C, Hackeng TM, Biesbroeck D. et al. Increased prothromb in activation in protein S-deficient plasma under flow conditions on endothelial cell ma-trix: an independent function of protein S in plasma. Blood 1995; 85: 1815-1821.
• 35 van Wijnen M, Stam JG, van’t Veer C. et al. The interaction of protein S with the phospholipid surface is essential for the activated protein C -independent activity of protein S. Thromb Haemost 1996; 76: 397-403.
• 36 Sere KM, Willems GM, Rosing J. et al. Protein S multimers are generated in vitro and affect protein S structure-function analyses. Semin Hematol 2006; 43 1 Suppl 1 S111-120.
• 37 Heeb MJ, Radtke KP, Fernandez JA. et al. Plasma contains protein S monomers and multimers with similar direct anticoagulant activity. J Thromb Haemost 2006; 4: 2215-2222.
• 38 Heeb MJ, Schuck P, Xu X. Protein S multimers and monomers each have direct anticoagulant activity. J Thromb Haemost 2006; 4: 385-391.
• 39 Hackeng T, Sere KM, Tans G. et al. Protein S stimulates inhibition of the tissue factor pathway by tissue factor pathway inhibitor. Proc Natl Acad Sci USA 2006; 103: 3106-3111.
• 40 Blom AM, Villoutreix BO, Dahlback B. Complement inhibitor C4b-binding protein-friend or foe in the innate immune system?. Mol Immunol 2004; 40: 1333-1346.
• 41 Villoutreix BO, Blom AM, Webb J. et al. The complement regulator C4b-binding protein analyzed by molecular modeling, bioinformatics and computer-aided experimental design. Immunopharmacology 1999; 42: 121-134.
• 42 Dahlback B. Inhibition of protein Cacofactor function of human and bovine protein S by C4b-binding protein. J Biol Chem 1986; 261: 12022-12027.
• 43 Webb JH, Blom AM, Dahlback B. Vitamin K-dependent protein S localizing complement regulator C4b-binding proteintothe surface of apoptotic cells. J Immunol 2002; 169: 2580-2586.
• 44 Dahlback B, Wiedmer T, Sims PJ. Binding of anticoagulant vitamin K-dependent protein S to plateletderived microparticles. Biochemistry 1992; 31: 12769-12777.
• 45 Anderson HA, Maylock CA, Williams JA. et al. Serum-derived protein S binds to phosphatidylserine and stimulates the phagocytosis of apoptotic cells. Nat Immunol 2003; 4: 87-91.
• 46 Kask L, Trouw LA, Dahlback B. et al. The C4b-binding protein-protein S complex inhibits the phagocytosis of apoptotic cells. J Biol Chem 2004; 279: 23869-23873.
• 47 Manfioletti G, Brancolini C, Avanzi G. et al. 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 1993; 13: 4976-4985.
• 48 Melaragno MG, Fridell YW, Berk BC. The Gas6/Axl system: a novel regulator of vascular cell function. Trends Cardiovasc Med 1999; 9: 250-253.
• 49 Crosier KE, Crosier PS. New insightsin to the control of cell growth; the role of the AxI family. Pathology 1997; 29: 131-135.
• 50 Hafizi S, Dahlback B. Gas6 and protein S. Vitamin K-dependent ligands for the Axl receptor tyrosine kinase subfamily. Febs J 2006; 273: 5231-5244.
• 51 Hafizi S, Dahlback B. Signalling and functional diversity within the Axl subfamily of receptor tyrosine kinases. Cytokine Growth Factor Rev 2006; 17: 295-304.
• 52 Godowski PJ, Mark MR, Chen J. et al. Reevaluation of the roles of protein S and Gas6 as ligands for the receptor tyrosine kinase Rse/Tyro 3. Cell 1995; 82: 355-358.
• 53 Evenas P, Dahlback B, Garciade Frutos P. The first laminin G-type domain in the SHBG-like region of protein S contains residues essential for activation of the receptor tyrosine kinase sky. Biol Chem 2000; 381: 199-209.
• 54 Sasaki T, Knyazev PG, Cheburkin Y. et al. Crystal structure of a C-terminal fragment of growth arrest-specific protein Gas6. Receptor tyrosine kinase activation by laminin G-like domains. J Biol Chem 2002; 277: 44164-44170.
• 55 Sasaki T, Knyazev PG, Clout NJ. et al. Structural basis for Gas6-Axl signalling. Embo J 2006; 25: 80-87.
• 56 Dahlback B. Blood coagulation and its regulation by anticoagulant pathways: genetic pathogenesis of bleeding and thrombotic diseases. J Intern Med 2005; 257: 209-223.
• 57 Zoller B, Garcia de Frutos P, Hillarp A. et al. Thrombophilia as a multigenic disease. Haematologica 1999; 84: 59-70.
• 58 Zoller B, Garcia de Frutos P, Dahlback B. Evaluation of the relationship between protein S and C4b- binding protein isoforms in hereditary protein S deficiency demonstrating type I and type III deficiencies to be phenotypic variants of the same genetic disease. Blood 1995; 85: 3524-3531.
• 59 Persson KE, Dahlback B, Hillarp A. Diagnosing protein S deficiency: analytical considerations. Clin Lab 2003; 49: 103-110.
• 60 Lanke E, Johansson AM, Hillarp A. et al. Co-segregation of the PROS1 locus and protein S deficiency in families having no detectable mutations in PROS1. J Thromb Haemost 2004; 2: 1918-1923.
• 61 Johansson AM, Hillarp A, Sall T. et al. Large deletions of the PROS1 gene in a large fraction of mutation-negative patients with protein S deficiency. Thromb Haemost 2005; 94: 951-957.
• 62 Giri TK, Garciade Frutos P, Dahlback B. Protein S Thr103Asn mutation associated with type II deficiency reproduced in vitroand functionally characterised. Thromb Haemost 2000; 84: 413-419.
• 63 Hayashi T, Nishioka J, Suzuki K. Molecular mechanism of the dysfunction of protein S (Tokushima) (Lys155-->Glu)for the regulation of the blood coagulation system. Biochim Biophys Acta 1995; 1272: 159-167.