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Thromb Haemost 1995; 74(01): 129-133
DOI: 10.1055/s-0038-1642665
DOI: 10.1055/s-0038-1642665
Symposium
Thrombin - Bilogical Activities
Thrombin Specificity
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
› Author Affiliations
Further Information
Publication History
Publication Date:
09 July 2018 (online)
-
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.)