Download PDF
Thromb Haemost 1995; 74(06): 1389-1397
DOI: 10.1055/s-0038-1649952
Review Article
Schattauer GmbH Stuttgart

Standards in Fibrinolysis – Current Status and Future Challenges

Patrick J Gaffney
The Division of Haematology, National Institute for Biological Standards and Control, South MImms, Potters Bar, Hertfordshire, UK
› Author Affiliations
Further Information

Publication History

Received: 19 August 1995

Accepted after resubmission 25 August 1995

Publication Date:
10 July 2018 (online)

  PDF Download  Permissions and Reprints
 

  • References

  • 1 Barrowcliffe TW. The use of standards in blood coagulation. In: Blood Coagulation and Haemostasis. Thompson H. ed. Churchill Livingstone; Edinburgh, UK: 1985: 410-432
    Google Scholar
  • 2 Barrowcliffe TW, Curtis AD. Principles of bioassay. In: Haemostasis and Thrombosis. Bloom AL, Thomas DP. eds Churchill Livingstone; Edinburgh, UK: 1987: 996-1004
    Google Scholar
  • 3 Verstraete M. A far-reaching programme; rapid, safe and predictable thrombolysis in man. In: Fibrinolysis. Kline DL, Reddy NN. eds. CRC Press, Boca Raton; Florida, USA: 1980: 129-149
    Google Scholar
  • 4 Camiolo SM, Thorsen S, Astrup T. Fibrinogenolysis and fibrinolysis with tissue plasminogen activator, urokinase, streptokinase-activated human globulin and plasmins. Proc Soc Exp Biol Med 1971; 38: 277-280
    PubMedGoogle Scholar
  • 5 Pennica D, Holmes WE, Kohr WJ, Harkins RN, Vehar GA, Ward CA, Bennett WF, Yelverton E, Seeburg PH, Heyneker HL, Goeddel DV, Collen D. Cloning and expression of human tissue-type plasminogen activator cDNA in E. coli.. Nature 1983; 301: 214-221
    CrossrefPubMedGoogle Scholar
  • 6 Krause J. Catabolism of tissue-type plasminogen activator (t-PA), its variants, mutants and hybrids. A review Fibrinolysis 1988; 2: 133-142
    PubMedGoogle Scholar
  • 7 Hoylaerts M, Rijken DC, Lijnen HR, Collen D. Kinetics of the activation of plasminogen by human tissue plasminogen activator. Role of fibrin J Biol Chem 1982; 257: 2912-2919
    PubMedGoogle Scholar
  • 8 Verstraete M, Bleifeld W, Brower RW, Charbonnier B, Collen D, de Bono DP, Dunning AJ, Lennane RJ, Lubsen J, Mathey DG, Michel PL, Raynaud Ph, Schofer J, Vahanian A, Vanhaecke J, Van de Kley GA, Van de Werf F, Von Essen R. Double-blind randomised trial of intravenous tissue-type plasminogen activator versus placebo in acute myocardial infarction. Lancet 1985; 2: 965-969
    PubMedGoogle Scholar
  • 9 Wilcox RG, von der Lippe G, Olsson CG, Jensen G, Skene AM, Hampton JR. Trial of tissue plasminogen activator for mortality reduction in acute myocardial infarction. Anglo-Scandinavian Study of Early Thrombolysis (ASSET) Lancet 1988; 2: 525-539
    PubMedGoogle Scholar
  • 10 Gaffney PJ, Curtis AD. A collaborative study of a proposed international standard for tissue plasminogen activator (t-PA). Thromb Haemost 1985; 53: 134-136
    Article in Thieme ConnectPubMedGoogle Scholar
  • 11 Gaffney PJ, Curtis AD. A collaborative study to establish the 2nd International Standard for tissue plasminogen activator (t-PA). Thromb Haemost 1987; 58: 1085-1087
    Article in Thieme ConnectPubMedGoogle Scholar
  • 12 Parekh RB, Dwek RA, Thomas JR, Opdenakker G, Rademacher TW, Wittwer AJ, Howard SC, Nelson R, Siegel NR, Jennings MG, Harakas NK, Feder J. Cell-type specific and site specific N-glycosylation of Type I and Type II human tissue plasminogen activator. Biochemistry 1989; 28: 7644-7662
    CrossrefPubMedGoogle Scholar
  • 13 Chan AL, Morris HR, Panico M, Etienne AT, Rogers ME, Gaffney PJ, Creighton-Kempsford L, Dell A. A novel sialylated N-acetylgalactosamine containing oligosaccharide is the major complex-type structure present in Bowes melanoma tissue plasminogen activator. Glycobiology 1991; 1: 173-185
    CrossrefPubMedGoogle Scholar
  • 14 Burck PJ, Berg DH, Warrick MW, Berg DT, Walls JD, Jaskunas SR, Crisel RM, Weigel B, Vlajos CJ, McClure DB, Grinnell BW. Characterisation of a modified human tissue plasminogen activator comprising a kringle-2 and a protease domain. J Biol Chem 1990; 265: 5170-5177
    PubMedGoogle Scholar
  • 15 Kohnert U, Rudolph R, Verheijen JH, Weening-Verhoeff EJ, Stem A, Opitz U, Martin U, Lill H, Prinz H, Lechner M, Kresse G-B, Buckel P, Fischer S. Deletion of the three N-terminal domains still maintains the biochemical properties of the protease and the kringle-2 in the refolded t-PA deletion mutant BM 06.022. Prot Engineering 1992; 5: 93-100
    CrossrefPubMedGoogle Scholar
  • 16 Martin U, Fischer S, Kohnert U, Rudolph R, Sponer G, Stem A, Strein K. Pharmacokinetic properties of an Escherichia coli-produced recombinant plasminogen activator (BM 06.022) in rabbits. Thromb Res 1991; 62: 137-146
    CrossrefPubMedGoogle Scholar
  • 17 Gaffney PJ, Creighton-Kempsford LJ, Pring JB. Assessment of the international standard for tissue plasminogen activator as a standard for domainally-deleted mutants. Thromb Haemost 1993; 69: 1264 (abstract)
    PubMedGoogle Scholar
  • 18 Kratzschmar J, Haendler B, Langer G, Boidol W, Bringmann P, Alagon A, Donner P, Schleuning WD. The plasminogen activator family from the salivary gland of the vampire bat Desmodus rotundus: cloning and expression. Gene 1991; 105: 229-237
    CrossrefPubMedGoogle Scholar
  • 19 Castellino FJ. A unique enzyme-protein substrate modifier reaction: plasmin/streptokinase interaction. Trends Biochem Sci 1979; 4: 1-5
    CrossrefPubMedGoogle Scholar
  • 20 Heath AB, Gaffney PJ. A collaborative study to establish the second international standard for streptokinase. Thromb Haemost 1990; 64: 267-269
    Article in Thieme ConnectPubMedGoogle Scholar
  • 21 Collen D, Silence K, Demarsin E, De Mol M, Lijnen HR. Isolation and characterisation of natural and recombinant staphylokinase. Fibrinolysis 1992; 6: 203-213
    PubMedGoogle Scholar
  • 22 Collcn D, De Cock F, Vanlinthoul I, Dcclcrck PJ, Lijncn HR, Stassen JM. Comparative thrombolytic and immunogenic properties of staphylokinase and streptokinase. Fibrinolysis 1992; 6: 232-242
    PubMedGoogle Scholar
  • 23 Husain S, Clurewieh V, Lipinski B. Purification and partial characterisation of a single chain high molecular weight form of urokinase from human urine. Arch Bioehem Biophys 1983; 220: 31-38
    CrossrefPubMedGoogle Scholar
  • 24 Urano T, de Serrano SV, Gaffney PJ, Castellino FJ. Activation of human (glu*) plasminogen by human single chain urokinase. Arch Bioehem Biophys 1988; 264: 222-230
    CrossrefPubMedGoogle Scholar
  • 25 Priini Trial Study Group. Randomised double-blind trial of recombinant prourokinase against streptokinase in acute myocardial infarction. Lancet 1989; 1: 863-867
    PubMedGoogle Scholar
  • 26 Lijnen HR, Nelles L, Holmes WE, Collcn D. Biochemical and thrombolytic properties of a low molecular weight form (comprising leu144 through leu411) of recombinant single chain urokinase-type plasminogen activator. J Biol Chcm 1988; 263: 5594-5598
    PubMedGoogle Scholar
  • 27 Philo RD, Gaffney PJ. Assay methodology for urokinase. Its use in assessing the composition of mixtures of high- and low-molecular weight urokinases. Thromb Res 1981; 21: 81-88
    CrossrefPubMedGoogle Scholar
  • 28 World Health Organisation. Twenty-first Meeting. Hxpert Committee on Biological Standardisation WHO Tech Rep Ser No 413 1968
    PubMedGoogle Scholar
  • 29 Philo RD, Gaffney PJ. Relative potencies of different molecular weight forms of urokinase. In: Prog Fibrinolysis Thrombolysis. Davidson JF, Nilsson I-M, Samama MM, Dcsnoycrs PC. eds. Churchill Livingstone; Edingburgh: 1981. Vol 5 220-2
    Google Scholar
  • 30 Gaffney PJ, Heath AB. A collaborative study to establish a standard for high molecular weight urinary-type plasminogen activator (HMW/u-PA). Thromb Haemost 1990; 64: 398-401
    Article in Thieme ConnectPubMedGoogle Scholar
  • 31 Hanbueken FW, Schneider J, Gunzler WA. Selective fibrinolytic activity of recombinant non-glycosylated human prourokinase (single chain urokinase-type plasminogen activator) from bacteria. Drug Res 1987; 37: 993-997
    PubMedGoogle Scholar
  • 32 Nolli ML, Sarubbi E, Robbiati F, Soffientini A, Blasi F, Parenti F, Cassani G. Production and characterisation of human recombinant single chain urokinase-type plasminogen activator from mouse cells. Fibrinolysis 1989; 3: 101-6
    PubMedGoogle Scholar
  • 33 Report of the Fibrinolysis Subcommittee of the Scientific and Standardisation Committee of the International Society on Thrombosis and Haemostasis (Chairman HR Lijnen. 1993
    PubMed
  • 34 Clough AM, Gaffney PJ, Longstaff C. Comparison of high and low molecular weight urokinase activities in a variety of assay systems. Fibrinolysis 1992; 6 suppl (Suppl. 02) 210 (abstract)
    PubMedGoogle Scholar
  • 35 Gallimore MJ, Nulkar MV, Shaw JT B. A comparative study of the inhibitors of fibrinolysis in human, dog and rabbit blood. Thromb Diath Haemorrh 1965; 14: 145-158
    PubMedGoogle Scholar
  • 36 Fibrinolysis BrakmanP. A standardised fibrin plate method and a fibrinolytic assay of plasminogen. Scheltema and Holkema; Amsterdam: 1967
    Google Scholar
  • 37 Mahmoud M, Gaffney PJ. Bioimmunoassay (BIA) of tissue plasminogen activator (t-PA) and its specific inhibitor (t-PA/INH). Thromb Haemost 1985; 53: 356-359
    Article in Thieme ConnectPubMedGoogle Scholar
  • 38 Gaffney PJ, Wong M-Y. Collaborative study of a proposed international reference reagent (IRR) for human plasma fibrinogen. Thromb Haemost 1992; 68: 428-432
    Article in Thieme ConnectPubMedGoogle Scholar
  • 39 Gaffney PJ. Interlaboratory evaluation of the International Standard for plasma fibrinogen in the automated Clauss procedure. (Mss in preparation)
    PubMedGoogle Scholar
  • 40 Meade TW. Hypercoagulability and ischaemic heart disease. Blood Rev 1987; 1: 2-8
    CrossrefPubMedGoogle Scholar
  • 41 Philo RD, Gaffney PJ. Plasmin potency estimates. Influence of the substrate used in the assay Thromb Haemost 1981; 45: 107-109
    Article in Thieme ConnectPubMedGoogle Scholar
  • 42 Hamsten A, Wiman B, de Faire U, Blombilck M. Increased plasma levels of a rapid inhibitor of tissue plasminogen activator in young survivors of myocardial infarction. N ling J Med 1985; 313: 1557-1563
    PubMedGoogle Scholar
  • 43 Declerck PJ, Moreau I I, Jespersen J, Gram J, Kluft C. Multicenter evaluation of commercially available methods lor the immunological determination of plasminogen activator inhibitor-1 (PAI-I). Thromb Haemost 1993; 70: 858-863
    Article in Thieme ConnectPubMedGoogle Scholar
  • 44 Gram J, Declerck PJ, Sidclmann J, Jespersen J, Kluft C. Multicenter evaluation of commercial kit methods: plasminogen activator inhibitor activity. Thromb Haemost 1993; 70: 852-857
    Article in Thieme ConnectPubMedGoogle Scholar
  • 45 Wagner OF, Binder B. Purification of an active plasminogen activator inhibitor immunologically related to the endothelial type plasminogen activator inhibitor from the conditioned media of a human melanoma cell line. J Biol Chem 1986; 261: 14474-14481
    PubMedGoogle Scholar
  • 46 Alessi MC, Declerck PJ, De Mol M, Nelles L, Collcn D. Purification and characterisation of natural and recombinant human plasminogen activator inhibitor-1 (PAI-I). Eur J Bioch 1988; 175: 531-40
    CrossrefPubMedGoogle Scholar
  • 47 Donati M-B. Assays for fibrinogen/fibrin degradation products in biological fluids: some methodological aspects. Thromb Diath Haemorrh 1975; 34: 652-660
    PubMedGoogle Scholar
  • 48 Rylatt DB, Blake AS, Cottis LE, Massingham DA, Fletcher WA, Masci PP, Whitaker AN, Elms M, Bunce I, Webber AJ, Wyatt D, Bundeson PG. An immunoassay for human D dimer using monoclonal antibodies. Thromb Res 1983; 31: 767-778
    CrossrefPubMedGoogle Scholar
  • 49 Gaffney PJ. FDP. Lancet 1972; 2: 1422
    PubMedGoogle Scholar
  • 50 Gaffney PJ. Structure of fibrinogen and degradation products of fibrinogen and fibrin. Brit Med Bull 1977; 33: 245-52
    CrossrefPubMedGoogle Scholar
  • 51 Gaffney PJ, Edgell TA, Creighton-Kempsford LJ, Wheeler S, Tarelli E. Fibrin degradation product (FnDP) assays. Analysis of standardisation issues and target antigens in plasma Br J Haem 1995; 90: 187-194
    CrossrefPubMedGoogle Scholar
  • 52 Creighton LJ, Gaffney PJ. Appraisal of an ELISA procedure for the measurement of FDP in plasma. Fibrinolysis 1988; 2 suppl (Suppl. 01) 39 (abstract)
    PubMedGoogle Scholar
  • 53 Graeff H, Hafter R. Detection and relevance of crosslinked fibrin derivatives in blood. Sem Thromb Haemost 1982; 8: 57-68
    Article in Thieme ConnectPubMedGoogle Scholar
  • 54 Gaffney PJ, Gascoine PS, Creighton LJ, Tymkewycz PM. Monoclonal antibodies for the detection of thrombosis. Adv Exp Med Biol 1990; 281: 419-427
    PubMedGoogle Scholar
  • 55 Creighton-Kempsford LJ, Pring JB, Gaffney PJ. A comparison of the plasminogen activator activity units of urinary-type plasminogen activator (u-PA) and tissue plasminogen activator (t-PA). Blood Coag Fibrinolysis 1992; 3: 481-483
    CrossrefPubMedGoogle Scholar
  • 56 Smith RA C, Dupe RJ, English PD, Green J. Fibrinolysis with acyl- enzymes: a new approach to thrombolytic therapy. Nature 1981; 290: 505-508
    CrossrefPubMedGoogle Scholar
  • 57 Longstaff C, Wong M-Y, Gaffney PJ. An international collaborative study to investigate the standardisation of hirudin potency. Thromb Haemost 1993; 69: 430-435
    Article in Thieme ConnectPubMedGoogle Scholar
  • 58 Gaffney PJ, Heath AB, Fenton II JW. A collaborative study to establish an international standard for a-thrombin. Thromb Haemost 1992; 67: 424-427
    Article in Thieme ConnectPubMedGoogle Scholar
  • 59 Gaffney PJ, Creighton LC, Mahmoud-Alexandroni M. Assays associated with fibrinolysis. In: Fibrinolysis. Current Prospects Gaffney PJ, Castellino FJ, Plow E, Takada A. eds. John Libby and Son; London: 1988: 129-140
    Google Scholar