Binding and Activation of Plasminogen on the Surface of Staphylococcus Aureus and Group A, C, and G Streptococci

  • Pentti Kuusela
  • Måns Ullberg
  • Göran Kronvall
  • Olli Saksela
Part of the Federation of European Microbiological Societies Symposium Series book series (FEMS, volume 61)

Abstract

The native form of plasminogen, a single-chain glycoprotein with a molecular mass of 91 kDa, occurs in plasma and many tissue fluids. Characteristic features of its structure are five loops in the aminoterminal portion of the molecule. These so-called kringles contain lysine-binding sites involved in interactions of plasminogen with fibrin, plasmin inhibitors and eukaryotic cell surfaces. As in other serine proteases, the carboxyterminal portion of plasmin contains the enzymatically active site. Plasminogen is converted to plasmin by the action of eukaryotic activators such as urokinase (u-PA) and tissue-type plasminogen activator (t-PA) as well as of prokaryotic activators staphylokinase and streptokinase. The action of eukaryotic activators is due to direct proteolysis of a single Arg-Val peptide bond. The formed plasmin is composed of two polypeptide chains (a 65-kDa A heavy chain and a 25-kDa B light chain) held together by two disulphide bonds (see Figure 1). Prokaryotic activators, which lack direct proteolytic activity, and plasminogen form a complex which converts plasminogen to plasmin (for reviews, see references 1 and 2). Plasmin is able to modify itself by cleaving a small 8-kDa activation peptide off the aminoterminus of the molecule, thus converting native glu-plasmin (glu = glutamic acid) to the lys-form (lys = lysine) (see Figure 1).

Keywords

Plasminogen Activator Activation Peptide Plasminogen Activation Plasmin Activity Kringle Domain 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. 1.
    K. Danø, P.A. Andreasen, J. Grondahl-Handen, R. Kristensen, L.S. Nielsen, and L. Skriver, Plasminogen activators, tissue degradation and cancer, Adv. Cancer Res. 44:139 (1985).PubMedCrossRefGoogle Scholar
  2. 2.
    O. Saksela and D. Rifkin, Cell-associated plasminogen activation, Ann. Rev. Cell Biol. 4:93 (1988).PubMedCrossRefGoogle Scholar
  3. 3.
    C.M. Hekman and D. J. Loskutoff, Fibrinolytic pathways and the endothelium, Semin. Throm. Haemost. 13:514 (1987).CrossRefGoogle Scholar
  4. 4.
    R. Lottenberg, C.C. Broder, and M.D.P. Boyle, Identification of a specific receptor for plasmin on a group A streptococcus, Infect. Immun. 55:1914 (1987).PubMedGoogle Scholar
  5. 5.
    C.C. Broder, R. Lottenberg, and, M.D.P. Boyle, Mapping of the human plasmin domain recognized by the unique plasmin receptor of group A streptococci, Infect. Immun. 57:2597 (1989).PubMedGoogle Scholar
  6. 6.
    M. Ullberg, G. Kronvall, and B. Wiman, New receptor for human plasminogen on gram positive cocci, APMIS 97:996 (1989).PubMedCrossRefGoogle Scholar
  7. 7.
    J. Parkkinen and T.K. Korhonen, Binding of plasminogen to Esherichia coli adhesion proteins, FEBS Lett.250:437 (1989).PubMedCrossRefGoogle Scholar
  8. 8.
    M. Ullberg, G. Kronvall, I. Karlsson, and B. Wiman, Receptors for human plasminogen of gram-negative bacteria, Infect. Immun. 58:21 (1990).PubMedGoogle Scholar
  9. 9.
    P. Kuusela and O. Saksela, Binding and activation of plasminogen at the surface of Staphylococcus aureus, Increase in affinity after conversion to the Lys form of the ligand, Eur. J. Biochem. 193:759 (1990).PubMedCrossRefGoogle Scholar
  10. 10.
    J. Parkkinen, J. Hacker, and T.K. Korhonen, Enhancement of tissue plasminogen activator-catalyzed activation by Escherichia coil S-fimbria associated with neonatal septicaemia and meningitis, Thromb. Hemost. 65:483 (1991).Google Scholar
  11. 11.
    P. Kuusela, M. Ullberg, O. Saksela, and G. Kronvall, Tissue type plasminogen activator (t-PA) mediated activation of plasminogen on the surface of group A, C and G streptococci, Manuscript submitted.Google Scholar
  12. 12.
    T.A. Broeseker, M.D.P. Boyle, and R. Lottenberg, Characterization of the interaction of human plasmin with its receptor on a Group A streptococcus, Microb. Pathogen. 5:19 (1988).CrossRefGoogle Scholar
  13. 13.
    M. Ullberg, I. Karlsson, B. Wiman and G. Kronvall, Two types of receptors for human plasminogen on group G streptococci, APMIS, 100:21 (1992).PubMedCrossRefGoogle Scholar
  14. 14.
    I. Sjöholm, B. Wiman, and P. Wallén, Studies on the conformational changes of plasminogen induced during activation to plasmin and by 6-aminohexanoid acid, Eur. J. Biochem. 39:471 (1973).PubMedCrossRefGoogle Scholar
  15. 15.
    C.C. Broder, R. Lottenberg, G.O. von Mering, K.H. Johnston, and M.D.P. Boyle, Isolation of a prokaryotic plasmin receptor, Relationship to a plasminogen activator produced by the same microorganism, J. Biol. Chem. 266:4922 (1991).PubMedGoogle Scholar
  16. 16.
    R. Lottenberg, C.C. Broder, M.B. Streoff, and M.D.P. Boyle, A group A streptococcal plasmin receptor demonstrates homology with glyceraldehyde-3-phosphate dehydrogenase, Abstr. 91th Gen. Meet. Amer. Soc. Microbiol. B-30 (1991).Google Scholar

Copyright information

© Springer Science+Business Media New York 1992

Authors and Affiliations

  • Pentti Kuusela
    • 1
  • Måns Ullberg
    • 3
  • Göran Kronvall
    • 3
  • Olli Saksela
    • 2
  1. 1.Department of Bacteriology and ImmunologyUniversity of HelsinkiHelsinkiFinland
  2. 2.Department of VirologyUniversity of HelsinkiHelsinkiFinland
  3. 3.Department of Clinical MicrobiologyKarolinska HospitalStockholmSweden

Personalised recommendations