Download PDF
Thromb Haemost 1988; 59(01): 049-053
DOI: 10.1055/s-0038-1642564
Review Article
Schattauer GmbH Stuttgart

Plasminogen San Antonio: An Abnormal Plasminogen with a More Cathodic Migration, Decreased Activation and Associated Thrombosis

Ying Liu
1   The Department of Pathology, Beth Israel Hospital and Harvard Medical School and the Charles A. Dana Research Institute, Beth Israel Hospital, Boston, MA and Southwest Texas Methodist Hospital, San Antonio, TX, USA
,
Roger M Lyons
1   The Department of Pathology, Beth Israel Hospital and Harvard Medical School and the Charles A. Dana Research Institute, Beth Israel Hospital, Boston, MA and Southwest Texas Methodist Hospital, San Antonio, TX, USA
,
Jan McDonagh
1   The Department of Pathology, Beth Israel Hospital and Harvard Medical School and the Charles A. Dana Research Institute, Beth Israel Hospital, Boston, MA and Southwest Texas Methodist Hospital, San Antonio, TX, USA
› Author Affiliations
Further Information

Publication History

Received 01 July 1987

Accepted after revision 29 September 1987

Publication Date:
18 April 2018 (online)

Also available at
  PDF Download  Permissions and Reprints

Summary

An abnormal plasminogen (San Antonio) has been isolated from a patient with axillary vein thrombosis. A decreased level of fibrinolytic activity was detected in both plasma and a purified system. The molecular abnormalities were investigated with both functional and immunological tests. Slightly decreased antigen concentration was noted in plasma. By crossed immunoelec-trophoresis, the patient and his two children had a second small arc and the primary arc migrated more eathodically. A distinct isozyme was detected in the abnormal plasminogen. Functionally, this abnormal plasminogen is characterized by failure to enhance maximal conversion to plasmin, especially by plasminogen activators, which are enhanced by fibrin or fibrin degradation products. The proband and his children are heterozygous for this abnormal plasminogen.

Keywords

Abnormal plasminogen - Axillary vein thrombosis - Fibrinolysis
 

  • References

  • 1 McDonagh CarrellN, Fibrinogen J. Chapel Hill II: defective in reactions with thrombin, factor XIIa, and plasmin. Br J Haematol 1982; 52: 35-47
    CrossrefPubMedSearch in Google Scholar
  • 2 Lijnen HR, Cohen D. Interaction of plasminogen activators and inhibitors with plasminogen and fibrin. Sem Thromb Haemostas 1982; 8: 2-10
    PubMedSearch in Google Scholar
  • 3 Lijnen HR, Soria J, Soria C, Cohen D, Caen JP. Dysfibrinogenemia (Fibrinogen Dusard) associated with impaired fibrin-enhanced plasminogen activation. Thromb Haemostas 1984; 51: 108-109
    PubMedSearch in Google Scholar
  • 4 Liu CY, Wallen R. Fibrinogen New York I: Defective fibrin potentiation of plasminogen activation by tissue plasminogen activator. Circulation 1984; 70 Supp II: 366
    PubMedSearch in Google Scholar
  • 5 D’Angelo A, Lockhart MS, D’Angelo SV, Taylor Jr FB. Protein S is a cofactor for activated protein C neutralization of an inhibitor of plasminogen activation released from platelets. Blood 1987; 69: 231-237
    PubMedSearch in Google Scholar
  • 6 Sakata Y, Loskutoff DJ, Gladson CL, Hekman CM, Griffin JH. Mechanism of protein C-dependent clot lysis: Role of plasminogen activator inhibitor. Blood 1986; 68: 1218-1223
    PubMedSearch in Google Scholar
  • 7 Bachmann F, Kruithof E KO. Tissue plasminogen activator: chemical and physiological aspects. Sem Thromb Haemostas 1984; 10: 6-17
    PubMedSearch in Google Scholar
  • 8 Aoki N, Moroi M, Sakata Y, Yoshida N, Matsuda M. Abnormal plasminogen. J Clin Invest 1978; 61: 1186-1195
    CrossrefPubMedSearch in Google Scholar
  • 9 Miyata T, Iwanaga S., Sakata Y, Aoki N. Plasminogen Tochigi: Inactive plasmin resulting from replacement of alanine-600 by threonine in the active site. Proc Natl Acad Sci USA 1982; 79: 6132-6136
    CrossrefPubMedSearch in Google Scholar
  • 10 Miyata T, Iwanaga S, Sakata Y, Aoki N, Takamatsu J, Kamiva T. Plasminogens Tochigi II and Nagoya: two additional molecular defects with Ala-600 → Thr replacement found in plasmin light chain variants. J Biochem 1984; 96: 277-287
    CrossrefPubMedSearch in Google Scholar
  • 11 Sakata Y, Aoki N. Molecular abnormality of plasminogen. J Biol Chem 1980; 255: 5442-5447
    PubMedSearch in Google Scholar
  • 12 Wohl RC, Summaria L, Robbins KC. Physiological activation of the human fibrinolytic system. Isolation and characterization of human plasminogen variants, Chicago I and Chicago II. J Biol Chem 1979; 254: 9063-9069
    PubMedSearch in Google Scholar
  • 13 Wohl RC, Summaria L, Chediak J, Rosenfeld S, Robbins KC. Human plasminogen variant Chicago III. Thromb Haemostas 1982; 48: 146-152
    PubMedSearch in Google Scholar
  • 14 Scharrer IM, Wohl RC, Hach V, Sinio L, Boreisha I, Robbins KC. Investigation of a congenital abnormal plasminogen, Frankfurt I, and its relationship to thrombosis. Thromb Haemostas 1986; 55: 396-401
    PubMedSearch in Google Scholar
  • 15 Soria J, Soria C, Bertrand O, Dunn F, Drouet L, Caen JP. Plasminogen Paris I: Congenital abnormal plasminogen and its incidence in thrombosis. Thromb Res 1983; 32: 229-238
    CrossrefPubMedSearch in Google Scholar
  • 16 Kazama M, Tahara C, Suzuki Z, Gohchi K, Abe T. Abnormal plasminogen, a case of recurrent thrombosis. Thromb Res 1981; 21: 517-522
    CrossrefPubMedSearch in Google Scholar
  • 17 Deutsch DG, Mertz ET. Plasminogen: Purification from human plasma by affinity chromatography. Science 1970; 170: 1095-1096
    CrossrefPubMedSearch in Google Scholar
  • 18 Friberger P, Knös M. Functional assays of the components of the fibrinolytic system using a plasmin sensitive substrate - a review. In: Developments in Hematology. Synthetic Substrates in Clinical Blood Coagulation Assays. Lijnen HR, Cohen D, Verstraete M. ((Eds).; Vol. 1). 73-92 Martinus Nijhoff; The Hague/Boston/London: 1980
    Search in Google Scholar
  • 19 Laemmli UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970; 227: 680-685
    CrossrefPubMedSearch in Google Scholar
  • 20 Laurell CB. Quantitative estimation of proteins by electrophoresis in agarose gel containing antibodies. Anal Biochem 1966; 15: 45-52
    CrossrefPubMedSearch in Google Scholar
  • 21 Saravis CA, Zamcheck N. Isoelectric focusing in agarose. J Immunol Meth 1979; 29: 91-96
    CrossrefPubMedSearch in Google Scholar
  • 22 Black JA. A silver stain for isoelectric focusing in agarose gel and its application for analyzing unconcentrated cerebrospinal fluid. Electrophoresis 1985; 6: 27-29
    CrossrefPubMedSearch in Google Scholar
  • 23 Confavreux C, Gianazza E, Chazot G, Lasne Y, Arnaud P. Silver stain after isoelectric focusing of unconcentrated cerebrospinal fluid: Visualization of total protein and direct immunofixation of immunoglobulin G. Electrophoresis 1982; 3: 206-210
    CrossrefPubMedSearch in Google Scholar
  • 24 Kaczmarek E, Kaminski M, McDonagh J. Fibrinogen-Sepharose interaction with prothrombin, prethrombin 1, prethrombin 2 and thrombin. Biochim Biophys Acta 1987; 914: 275-282
    CrossrefPubMedSearch in Google Scholar
  • 25 Dayhoff MO. Serine proteases (Chapter 7).. In: Atlas of Protein Sequence and Structure Vol. 5 (Suppl. 3), pp. 73-93 National Biomedical Research Foundation, Georgetown University Medical Center; Washington, D.C.: 1978
    Search in Google Scholar
  • 26 Lucas MA, Straight DL, Fretto LJ, McKee PA. The effects of fibrinogen and its cleavage products on the kinetics of plasminogen activation by urokinase and subsequent plasmin activity. J Biol Chem 1983; 258: 12171-12177
    PubMedSearch in Google Scholar
  • 27 Cohen D. On the regulation and control of fibrinolysis. Thromb Haemostas 1980; 43: 77-89
    PubMedSearch in Google Scholar