Thromb Haemost 1995; 74(01): 473-481
DOI: 10.1055/s-0038-1642724
Symposium
New Antithrombins
Schattauer GmbH Stuttgart

Comparative Pharmacology of Site Directed Antithrombin Agents. Implication in Drug Development

Demetra Callas
Departments of Pharmacology and Pathology, Loyola University Medical Center, Maywood, IL, USA
,
Jawad Fareed
Departments of Pharmacology and Pathology, Loyola University Medical Center, Maywood, IL, USA
› Author Affiliations
Further Information

Publication History

Publication Date:
09 July 2018 (online)

 
  • References

  • 1 De Fouw NJ, van Hinsberg VW, de Jong YF, Haverkate F, Bertina RBertina. he interaction of activated protein C and thrombin with the plasminogen activator inhibitor released from human endothelial cells. Thromb Haemost 1987; 57: 176
  • 2 Dichek D, Quertermous T. hrombin regulation of mRNA levels of tissue plasminogen activator inhibitor-1 in cultured human umbilical vein endothelial cells. Blood 1989; 74: 222-228
  • 3 Collen D, Lijnen HR, Todd PA, Goa KGoa. issue-type plasminogen activator: A review of its pharmacology and therapeutic use as a thrombolytic agent. Drugs 1989; 38: 346-388
  • 4 Pannell R, Gurewich V. ro-urokinase: a study of its stability in plasma and of a mechanism for its selective fibrinolytic effect. Blood 1986; 67: 1215-1223
  • 5 Hoylaerts M, Rijken D, Lijnen HR, Collen D. inetics of the activation of plasminogen by human tissue plasminogen activator, role of fibrin. J Biol Chem 1982; 257: 2912-2919
  • 6 Coleman RColeman. ctivation of plasminogen by human plasma kallikrein. Biochem Biophys Res Commun 1968; 35: 273-279
  • 7 Goldsmith GH, Saito H, Ratnoff ORatnoff. he activation of plasminogen by Hageman factor fragments. J Clin Invest 1978; 62: 54-60
  • 8 Sakata Y, Curriden S, Lawrence D, Griffin JH, Loskutoff DLoskutoff. ctivated protein C stimulates the fibrinolytic activity of cultured endothelial cells and decreases antiactivator activity. Proc Natl Acad Sci USA 1985; 82: 1121-1125
  • 9 Callas D, Bacher P, Iqbal O, Hoppensteadt D, Fareed J. ibrinolytic compromise by simultaneous administration of site-directed inhibitors of thrombin. Thromb Res 1994; 74 (03) 193-205
  • 10 Gilboa N, Villannueva Fenton II JW. Inhibition of fibrinolytic enzymes by thrombin inhibitors. Enzyme 1988; 40: 144-148
  • 11 Barabas E, Szell E, Bajusz S. creening for fibrinolysis inhibitory effect of synthetic thrombin inhibitors. Blood Coagulation and Fibrinolysis 1993; 4: 243-248
  • 12 Bock LC, Griffin LC, Latham JA, Veimaas EH, Toole JToole. Selection of single-stranded DNA molecules that bind and inhibit human thrombin. Nature 1992; 355 6360 564-566
  • 13 Macaya RF, Schultze P, Smith FW, Roe JA, Feigon J. hrombin-binding DNA aptamer forms a unimolecular quadruplex structure in solution. Proc Natl Acad Sci USA 1993; 90: 3745-3749
  • 14 Paborsky LR, McCurdy SN, Griffin LC, Toole JJ, Leung LL K. The single-stranded DNA aptamer binding-site of human thrombin. J Biol Chem 1993; 268: 20808
  • 15 Li WX, Kaplan AV, Grant GW, Toole JJ, Leung LL K. A novel nucleotide- based thrombin inhibitor inhibits clot-bound thrombin and reduces arterial platelet thrombus formation. Blood 1994; 83 (03) 677-682
  • 16 Latham JA, Johnson R, Toole JToole. he application of a modified nucleotide in aptamer selection: novel thrombin aptamers containing 5-(l-pentynyl)- 2'-deoxyuridine. Nucleic Acids Research 1994; 22 (14) 2817-2822
  • 17 Kubik MF, Stephens AW, Schneider D, Marlar R, Tasset D. High-affinity RNA ligands to human a-thrombin. Nucleic Acids Research 1994; 22 (13) 2619-2626
  • 18 Petersen TE, Roberts HR, Sottrup-Jensen L, Magnusson S. Primary structure of hirudin, a thrombin-specific inhibitor. In: Peptides of the Biological Fluids. Peters H. ed. Pergamon, Oxford; 1976: 145-149
  • 19 Harvey RP, Degryse E, Stefani L, Schamber F, Cazenave JP, Courtney M, Tolstoshev P, Lecocq JLecocq. loning and expression of cDNA coding for the anticoagulant hirudin from the bloodsucking leech Hirudo medicinalis:. Proc Natl Acad Sci USA 1986; 83: 1084-1088
  • 20 Dodt J, Kohler S, Schmitz T, Wilhelm B. istinct binding sites of Ala48-hiradin 1 -47 and Ala48-hiradin48-65 on a thrombin. J Biol Chem 1990; 265: 713-718
  • 21 Scharf M, Engels J, Tripier D. rimary structures of new “isohirudins”. FEES Lett 1989; 225: 105-110
  • 22 Kurfurst MKurfurst. Detection and molecular weight determination of polyethylene glycol-modified hirudin by staining after sodium dodecyl sulfate - polyacrylamide gel electrophoresis. Analytical Biochemistry 1992; 200 (02) 244-248
  • 23 Zawilska K, Zozulinska M, Turowiecka Z, Blahut M, Drobnik L, Vinalzer H. he effect of a long-acting recombinant hirudin (PEG-hirudin) on experimental disseminated intravascular coagulation (DIC) in rabbits. Thromb Res 1993; 69 (03) 315-320
  • 24 DiMaio J, Gibbs B, Munn D, Lefebvre J, Ni F, Konishi Y. ifunctional thrombin inhibitors based on the sequence of hirudin. J Biol Chem 1990; 265 (35) 21698-21703
  • 25 Maraganore JM, Bourdon P, Jablonski J, Ramachandran KL, Fenton II JM. esign and characterization of hirulogs: A novel class of bivalent peptide inhibitors of thrombin. Biochemistry 1990; 29: 7095-7101
  • 26 Topol EJ, Bonan R, Jewitt D, Sigwart U, Kakkar VV, Rothman M, de Bono D, Ferguson J, Willerson JT, Strony J, Ganz P, Cohen MD, Raymond R, Fox I, Maraganore J, Adelman B. se of a direct antithrombin, hirulog, in place of heparin during coronary angioplasty. Circulation 1993; 87 (05) 1622-1629
  • 27 Cannon CP, Maraganore JM, Loscalzo J. nticoagulant effects of hirulog, a novel thrombin inhibitor, in patients with coronary artery disease. Am J Cardiol 1993; 71: 778-782
  • 28 Theroux P, Lidon R. nticoagulants and their use in acute ischemic syndromes. In: Textbook of Interventional Cardiology. Topol EJ. ed. WB Saunders Co; Philadelphia, PA: 1994: 23-45
  • 29 Vlasuk G, Vallar PL, Weinhouse MI, Bergum PW, Tran HS, Weitz JI, Tulinsky A, Krishnan R, Rote WE, Oldeschulte GL, Pearson DPearson. novel inhibitor of thrombin containing multiple recognition sequences linked by a-keto amide transition state. Circulation 1994; 90 (04) 1-348
  • 30 Hijikata-Okunomiya A, Okamoto S. strategy for a rational approach to designing synthetic selective inhibitors. Sem Thromb Hemost 1992; 18 (01) 135-149
  • 31 Tamao Y, Yamamoto T, Kimumoto R, Itoh J, Hirata T, Mineo K, Okamoto S. ffect of a selective thrombin-inhibitor MCI-903 8 on fibrinolysis in vitro and in vivo . Thromb Haemost 1986 562: 28-34
  • 32 Tamao Y, Yamamoto T, Hirata T, Kinugasa M, Kimumoto M. ffect of argipidine (MD-805) on blood coagulation. Jpn Phaimacol Ther 1986; 14: 869-874
  • 33 Mamyama I. ynthetic anticoagulants. Jpn J Clin Hematol 1990; 31: 776-781
  • 34 Yonekawa Y, Handa H, Okamoto S, Kamijo Y, Oda Y, Ishikawa J, Tsuda H, Shimizu Y, Satoh M, Yamaguchi T, Yano I, Horikawa Y, Tsuda E. reatment of cerebral infarction in the acute stage with synthetic antithrombin MD805 Clinical study among multiple institutions. Arch Jpn Chir 1986; 55: 711-726
  • 35 Kumon K, Tanaka K, Nakajima N, Naito Y, Fijuta T. nticoagulation with a synthetic thrombin inhibitor after cardiovascular surgery and for treatment of disseminated intravascular coagulation. Crit Care Med 1984; 12: 1039-1043
  • 36 Oshiro T, Kanbayashi J, Kosaki G. ntithrombotic therapy of patient with peripheral arterial reconstruction-clinical study on MD805. Blood & Vessel 1983; 14: 216-218
  • 37 Matsuo T, Kario K, Kodama K, Okamoto S. linical applications of the synthetic thrombin inhibitor, Argatroban (MD-805). Sem Thromb Hemost 1992; 18 (02) 155-160
  • 38 Bang NU, Mattler LMattler. hrombin sensitivity and specificity of three chromogenic peptide substrates. p305-310. In: Chemistry and Biology of thrombin. Lundblad RL, Fenton JW, Mann KG. eds. Ann Arbor Science. Ann Arbor, MI: 1977
  • 39 Fareed J, Messmore HL, Kindel G, Balis JBalis. nhibition of serine proteases by low molecular weight peptides and their derivatives. NY Acad Sci 1981; 370: 765-784
  • 40 Bajusz S, Barabas E, Szell E, Bagdy D. eptide aldehyde inhibitors of the fibrinogen-thrombin reaction. In: Peptides - Chemistry, Structure and Biology. Meienhofer J. ed. Ann Arbor Sci. Publ. Inc.m; Ann Arbor, MI: 1975: 603-608
  • 41 Bajusz S, Barabas E, Tolnay P, Szell E, Bagdy D. nhibition of thrombin and trypsin by tripeptide aldehydes. Int J Peptide Protein Res 1978; 12: 217-221
  • 42 Bajusz S, Szell E, Bagdy D, Barabas E, Dioszegi M, Fittler Z, Josza F, Horvath G, Tomori E. US Patent No. 4,703,036,, 1987
  • 43 Bajusz S, Szell E, Bagdy D, Barabas E, Horvath E, Dioszegi M, Fittler Z, Szabo G, Juhasz A, Tomori E, Szilagyi G. ighly active and selective anticoagulants: D-Phe-Pro-Arg-H, a free tripeptide aldehyde prone to spontaneous inactivation, and its stable N-methyl derivative, D-MePhe- Pro-Arg-H. J Med Chem 1990; 33: 1729-1735
  • 44 Bagdy D, Barabas E, Bajusz S, Szell E. n vitro inhibition of blood coagulation by tripeptide aldehydes -a retrospective screening study focused on the stable D-MePhe-Pro-Arg-H4LS04 . Throm Hemost 1992; 67 (03) 325-330
  • 45 Kettner C, Shaw E. he selective inactivation of thrombin by peptides of chloromethyl ketone, pi29-144. In: Chemistry and Biology of thrombin. Lundblad RL, Fenton JW, Mann KG. eds. Ann Arbor Science. Ann Arbor, MI: 1977
  • 46 Stiiber W, Kosina H, Heimburger N. ynthesis of a tripeptide with a C- terminal moiety and the inhibition of proteinases. Int J Peptide Protein Res 1988; 31: 63-70
  • 47 Neises B, Tamus C. hrombin inhibition by the tripeptide trifluoromethyl ketone D-Phe-Pro-Arg-CF3 (MDL73756). ThrombHaemost 1991; 65: 1290
  • 48 Cheng L, Scully MF, Goodwin CA, Kakkar VV, Claeson G. eptide a- aminophosphonic acids. A new type of thrombin inhibitors. Thromb Haemost 1991; 65: 1289
  • 49 Kettner C, Mesinger L, Knabb R. The selective inhibition of thrombin by peptides of boroarginine. J Biol Chem 1990; 265: 18289-18297
  • 50 Tapparelli C, Mettemich R, Ehrhardt C, Zurinin M, Claeson G, Scully MF, Stone SStone. n vitro and in vivo characterization of a neutral boron-containing thrombin inhibitor. J Biol Chem 1993; 268 (07) 4734-4741
  • 51 Kaiser B, Farced J, Hoppensteadt D, Birdsong B, Walenga JM, Markwardt F. Influence of recombinant hirudin and unfractionated heparin on thrombin and factor Xa generation in extrinsic and intrinsic activated systems. Thromb Res 1992; 65 (02) 157-164
  • 52 Kaiser B, Callas D, Hoppensteadt D, Malinowska K, Fareed J. Comparative studies on the inhibitory spectrum of recombinant hirudin, DuP 714 and heparin on the generation of thrombin and factor Xa generation in biochemically defined systems. Thromb Res 1994; 73 (05) 327-335
  • 53 Fareed J, Walenga JM, Kumar A, Rock A. modified stasis thrombosis model to study the antithrombotic actions of heparin and its fractions. Semin Thromb Hemost 1985; 11: 227-236
  • 54 Cade JF, Buchanan MR, Boneu B, Ockelford P, Carter CJ, Cerkus AL, Hirsh J. comparison of the antithrombotic and hemorrhagic effects of low molecular weight heparin fractions: the influence on the method of preparation. Thromb Res 1984; 35: 613-625