Thrombosis and Haemostasis, Inhaltsverzeichnis Thromb Haemost 1995; 74(01): 129-133DOI: 10.1055/s-0038-1642665 Symposium Thrombin - Bilogical Activities Schattauer GmbH Stuttgart Thrombin Specificity Autor*innen Institutsangaben Marie-Claude Guillin Laboratoire de Recherche sur l’Hémostase et la Thrombose, Faculté de Médecine Xavier Bichat, Paris, France Annie Bezeaud Laboratoire de Recherche sur l’Hémostase et la Thrombose, Faculté de Médecine Xavier Bichat, Paris, France Marie-Christine Bouton Laboratoire de Recherche sur l’Hémostase et la Thrombose, Faculté de Médecine Xavier Bichat, Paris, France Martine Jandrot-Perrus Laboratoire de Recherche sur l’Hémostase et la Thrombose, Faculté de Médecine Xavier Bichat, Paris, France Artikel empfehlen Abstract als PDF herunterladen(opens in new window) Artikel einzeln kaufen(opens in new window) PDF (386 kb) Referenzen References 1 Fenton JW, Fasco MJ, Stackrow AB, Aronson DL, Young AM, Finlayson JS. Human thrombins: production, evaluation and properties of α-thrombin. J Biol Chem 1977; 252: 3587-3598 2 Blomback B, Blomback B, Hessel B, Iwanaga S. Structure of N-teiminal fragments of fibrinogen and specificity of thrombin. Nature 1967; 215: 1445-1448 3 Bode W, Mayr I, Baumann U, Huber R, Stone SR, Hofsteenge J. The refined 1.9 A crystal structure of human α-thrombin: interaction with D-Phe-Pro-Arg-chloromethylketone and significance of the Tyr-Pro-Pro-Trp insertion segment. Embo J 1989; 8: 3467-3475 4 Grutter MG, Priestle JP, Rahuel J, Grossenbacher H, Bode W, Hofsteenge J, Stone SR. Crystal structure of the thrombin-hirudin complex: a novel mode of serine protease inhibitor. Embo J 1990; 9: 2361-2365 5 Rydel TJ, Tulinsky A, Bode W, Huber R. Refined structure of the hirudin-thrombin complex. J Mol Biol 1991; 221: 583-601 6 Church FC, Pratt CW, Noyes CM, Kalayanamit T, Sherrit GB, Tobin RB, Meade B. Structural and functional properties of human α-thrombin, phosphopyridoxylated α-thrombin and βt-thrombin. Identification of lysyl residues in α-thrombin that are critical for heparin and fibrin(ogen) interactions. J Biol Chem 1989; 264: 18419-18425 7 Bode W, Turk D, Karshikov A. The refined 1.9 A X-ray crystal structure of D-Phe-Pro-Arg-chloromethylketone-inhibitedhuman α-thrombin: structure analysis, overall structure, electrostatic properties detailed active-site geometry, and structure-function relationships. Protein Sci 1992; 1: 426-471 8 Naski MC, Fenton JW, Maraganore JM, Olson ST, Shafer JA. The COOH-terminal domain ofhirudin. An exosite-directed competitive inhibitor of the action of α-thrombin on fibrinogen J Biol Chem 1990; 265: 13484-89 9 Bouton MC, Jandrot-Perrus M, Bezeaud A, Guillin MC. Late fibrin(ogen) fragment E modulates human α-thrombin specificity. Eur J Biochem 1993; 215: 143-149 10 Rogers SR, Pratt CW, Whinna HC, Church FC. Role of thrombin exosites in inhibition by heparin cofactor II. J Biol Chem 1992; 267: 3613-3617 11 Liu LW, Vu TK H, Esmon CT, Coughlin SR. The region of the thrombin receptor resembling hirudin binds to thrombin and alters enzyme specificity. J Biol Chem 1991; 266: 16977-16980 12 Tsiang M, Lentz SR, Dittman WA, Wen D, Scarpati EM, Sadler JE. Equilibrium binding of thrombin to recombinant human thrombomodulin: effect of hirudin, fibrinogen, factor Va and peptide analogues. Biochemistry 1990; 29: 10602-10612 13 Jandrot-Pemis M, Huisse MG, Krstenansky JL, Bezeaud A, Guillin MC. Effect of the hirudin carboxy-terminal peptide 54-65 on the interaction of thrombin with platelets. Thromb Haemost 1991; 66: 300-305 14 Mathews I, Padmanabhan KP, Ganesh V, Tulinsky A, Ishii M, Chen J, Turck CW, Coughlin SR, Fenton JW. Cry stallographic structures of thrombin complexed with thrombin receptor peptides : existence of expected and novel binding modes. Biochemistry 1994; 33: 3266-3279 15 Mathews I, Padmanabhan KP, Tulinsky A, Sadler JE. Structure of a nonadecapeptide of the fifth EGF domain of thrombomodulin complexed with thrombin. Biochemistry 1994; 33: 13547-13552 16 De Marco L, Mazzucato M, Masotti A, Ruggeri ZM. Localization and characterization of an α-thrombin binding site on platelet glycoprotein Iboc. J Biol Chem 1994; 269: 6478-6484 17 Gralnick HR, Williams S, McKeown LP, Hansmann K, Fenton JW, Krutzsch H. High-affinity α-thrombin to platelet glycoprotein Iba: identification of two binding domains. Proc Natl Acad Sci USA 1994; 91: 6334-6338 18 Binnie CG, Lord ST. A synthetic analog of fibrinogen α27-50 is an inhibitor of thrombin. Thromb Haemost 1991; 65: 165-168 19 Bouton MC, Jandrot-Perras M, Moog S, Cazenave JP, Guillin MC, Lanza F. Thrombin interaction with a recombinant N-terminal extracellular domain of the thrombin receptor in an acellular system. Biochem J 1995; 305: 635-641 20 Guillin MC, Bezeaud A. Thrombin derivatives obtained by autolytic or limited tryptic cleavage. Sem Thromb Haemost 1992; 18: 224-229 21 Bezeud A, De Raucourt E, Miyata T, Bouton MC, Angles-Cano E, Guillin MC. Limited proteolysis of human α-thrombin by urokinase yields a non-clotting enzyme. Thromb Haemost. 1995 In Press 22 Braun PJ, Hofsteenge J, Chang JY, Stone SR. Preparation and characterization of proteolyzed forms of human α-thrombin. Thromb Res 1988; 50: 273-283 23 Chang JY. The structures and proteolytic specificities of autolyzed human thrombin. Biochem J 1986; 240: 797-802 24 Rydel TJ, Yin M, Padmanabhan KP, Blankenship DT, Cardin AD, Correa PE, Fenton JW, Tulinsky A. Crystallographic structure fo human α-thrombin. J Biol Chem 1994; 269: 22000-22006 25 Boissel JP, LeBonniec B, Rabiet MJ, Labie D, Elion J. Covalent structures of γ and β autolytic derivatives of human α-thrombin. J Biol Chem 1984; 259: 5691-5697 26 Brower MS, Walz DA, Garry EE, Fenton JW. II. Thrombin-induced elastase alters human α-thrombin function : limited proteolysis near the β-cleavage site results in decreased fibrinogen clotting and platelet stimulatory activity. Blood 1987; 69: 813-819 27 Brezniak DV, Brower MS, Witting JI, Walz DA, Fenton JW. II. Human α-to ζ-thrombin cleavage occurs with neutrophil cathepsin G orchymotrypsin while fibrinogen clotting activity is retained. Biochemistry 1990; 29: 3526-3542 28 Bezeaud A, Guillin MC. Enzymic and nonenzymic properties of human β-thrombin. J Biol Chem 1988; 263: 3576-3581 29 Hofsteenge J, Braun PJ, Stone SR. Enzymatic properties of proteolytic derivatives of human α-thrombin. Biochemistry 1988; 27: 2144-2151 30 Jandrot-Perras M, Huisse MG, Temisien C, Bezeaud A, Guillin MC. Thrombin binding to platelet membrane glycoprotein lb. Sem Thromb Haemost 1992; 18: 261-266 31 Stone SR, Hofsteenge J. Kinetics of the inhibition of thrombin by hirudin. Biochemistry 1986; 25: 4622-4628 32 Miyata T, Morita T, Inomoto T, Kawauchi S, Shirakami A, Iwanaga S. Prothrombin Tokushima, a replacement of arginine-418 by tryptophan that impairs the fibrinogen clotting activity of derived thrombin Tokushima. Biochemistry 1987; 27: 1117-1122 33 Henriksen RA, Mann KG. Substitution of valine for glycine-558 in the congenital dysthrombin thrombin Quick II alters primary substrate specificity. Biochemistry 1989; 28: 2078-2082 34 Miyata T, Araga R, Umeyama H, Bezeaud A, Guillin MC, Iwanaga S. Prothrombin Salakta: substitution of glutamic acid-466 by alanine reduces the fibrinogen clotting activity and the esterase activity. Biochemistry 1992; 31: 7457-7462 35 Bezeaud A, Elion J, Guillin MC. Functional characterization of thrombin Salakta: an abnormal thrombin derived from a human prothrombin variant. Blood 1988; 71: 556-561 36 LeBonniec B, Guinto ER, Esmon CT. Interaction of thrombin des-ETW with antithrombin III, the Kunitz inhibitors, thrombomodulin and protein C. J Biol Chem 1992; 267: 19341-19348 37 LeBonniec B, Guinto ER, MacGillivray RT A, Stone SR, Esmon CT. The role of thrombin’s Tyr-Pro-Pro-Trp motif in the interaction with fibrinogen, thrombomodulin, protein C, antithrombin III and the Kunitz inhibitors. J Biol Chem 1993; 268: 19055-19061 38 LeBonniec B, Betz A, Guinto ER, Esmon CT, Stone SR. Mapping of the thrombin des-ETW conformation by using site-directed mutants ofhiradin. Evidence for the induction of nonlocal modifications by mutagenesis Biochemistry 1994; 33: 3959-3966 39 Wu Q, Sheehan JP, Tsiang M, Lentz SR, Birktoft JJ, Sadler JE. Single aminoacid substitutions dissociate fibrinogen-clotting and thrombomodulin-binding activities of human thrombin. Proc Natl Acad Sci USA 1991; 88: 6775-6779 40 Sheehan JP, Sadler JE. Molecular mapping of the heparin -binding exosite of thrombin. Proc Natl Acad Sci USA 1994; 91: 5518-5522 41 LeBonniec B, Esmon CT. Glu 192→ Gin substitution in thrombin mimics the catalytic switch induced by thrombomodulin. Proc Natl Acad Sci USA 1991; 88: 7371-7375 42 LeBonniec B, MacGillivray RT A, Esmon CT. Thrombin Glu-39 restricts the P’3 specificity tononacidic residues. J Biol Chem 1991; 266: 13796-13803 43 Jandrot-Perras M, Clemetson KJ, Huisse MG, Guillin MC. Thrombin interaction with platelet glycoprotein lb: effect of glycocalicin on thrombin specificity. Blood 1992; 80: 2781-2796 44 Henriksen RA, Mann KG. Identification of the primary structural defect in the dysthrombin Thrombin Quick I: substitution of cysteine for arginine-382. Biochemistry 1988; 27: 9160-9165 45 Gan ZR, Li Y, Chen Z, Lewis SD, Shafer JA. Identification of basic amino acid residues in thrombin essential for heparin-catalyzed inactivation by antithrombin III. J Biol Chem 1994; 269: 1301-1305 46 Ye J, Rezaie AR, Esmon CT. Glycosaminoglycan contributions to both protein C activation and thrombin inhibition involve a common arginine-rich site in thrombin that includes residues arginine 93,97 and 101. J Biol Chem 1994; 269: 17965-17970 47 Ami RK, Padmanabhan K, Padmanabhan KP, Wu TP, Tulinsky A. Structure of the noncovalent complexes of human and bovine fragment 2 with human PPACK-thrombin. Biochemistry 1993; 32: 4727-4737 48 Liu LW, Rezaie AR, Carson CW, Esmon NL, Esmon CT. Occupancy of anion binding exosite 2 on thrombin determines Ca2+dependence of protein C activation. J Biol Chem 1994; 269: 11807-11812 49 Bock OE. Acive-site-selective labeling of blood coagulation proteinases with fluorescence probes by the use of thioester peptide chloromethyl ketones. 2. Properties of thrombin derivatives as reporters of prothrombin fragment-2 binding and specificity of the labeling approach for other proteinases J Biol Chem 1992; 267: 14974-14981 50 Fenton JW II, Olson TA, Zabinski MP, Wilner GD. Anion binding exosite of human -thrombin and fibrin(ogen) recognition. Biochemistry 1988; 27: 7106-7112 51 White GC, Lundblad RL, Griffith MJ. Structure-function relations in platelet-thrombin reactions. J Biol Chem 1981; 256: 1763-1766 52 Noe G, Hofsteenge J, Rovelli G, Stone SR. The use of sequence-specific antibodies to identify a secondary binding site in thrombin. J Biol Chem 1988; 263: 11729-11735 53 Wu Q, Picard V, Aiach M, Sadler JE. Activation induced exposure of the thrombin anion-binding exosite: studies with recombinant mutant prothrombins and an antithrombin antibody. J Bid Chem 1994; 269: 3725-3730 54 Costa JM, Fiessinger JN, Capron L, Aiach M. Partial characterization of an autoantibody recognizing the secondary binding site(s) of thrombin in a patient with recurrent spontaneous arterial thrombosis. Thromb Haemost 1992; 67: 193-199 55 Amaud E, Lafay M, Gaussem P, Picard V, Jandrot-Perras M, Aiach M, Rendu F. An autoantibody directed against human thrombin anion-binding exosite in a patient with arterial thrombosis: effects cm platelets, endothelial cells and protein C activation. Blood 1994; 84: 1843-1850 56 Guillin MC, Belghiti J, Bezeaud A. An antibody directed against a thrombin secondary recognition site for fibrin(ogen) and thrombomodulin. Thromb Haemost 1993; 69: 1790-1790 (Abst.)
