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Thromb Haemost 1991; 66(01): 032-036
DOI: 10.1055/s-0038-1646369
Review Article
Schattauer GmbH Stuttgart

Cellular Regulation of Fibrinolysis

Edward F Plow
,
Jordi Felez
,
Lindsey A Miles
Further Information

Publication History

Publication Date:
25 July 2018 (online)

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Summary

By virtue of their capacity to bind plasminogen activators and plasminogen, to accelerate plasminogen activation and to protect bound plasmin from inactivation by α2 antiplasmin, cells can harness the broad proteolytic activity of plasmin to their surface. Most cells bind plasminogen with a very high capacity, a relatively low affinity (Kd~1 εM) and recognize the lysine binding sites of the molecule. Gangliosides serve as non-protein plasminogen binding sites, and a subset of membrane proteins with carboxy-terminal lysine residues also serve as receptors. The alpha isoform of enolase possesses a carboxy-terminal lysine and is a prominent plasminogen binding protein of cells. Cells of the monocytoid lineage, including peripheral blood monocytes, can markedly upregulate their expression of plasminogen receptors. The capacity to modulate expression of receptors for fibrinolytic components establishes an additional mechanism by which the cell-surface regulates the function of the plasminogen system.

 

  • References

  • 1 Collen D. On the regulation and control of fibrinolysis. Thromb Haemost 1980; 43: 77-89
    Article in Thieme ConnectPubMedGoogle Scholar
  • 2 Harpel PC, Chang T-S, Verderber E. Tissue plasminogen activator and urokinase mediate the binding of Glu-plasminogen of plasma fibrin I. J Biol Chem 1985; 2 60#7 4432-4440
    PubMedGoogle Scholar
  • 3 Wiman B, Collen D. Molecular mechanism of physiological fibrinolysis. Nature 1978; 272: 549-550
    CrossrefPubMedGoogle Scholar
  • 4 Blasi F. Surface receptors for urokinase plasminogen activator. Fibrinolysis 1988; 2: 73-84
    PubMedGoogle Scholar
  • 5 Miles LA, Plow EF. Plasminogen receptors: Ubiquitous sites for cellular regulation of fibrinolysis. Fibrinolysis 1988; 2: 61-71
    PubMedGoogle Scholar
  • 6 Hajjar KA, Hamel NM, Harpel PC, Nachman RL. Binding of tissue plasminogen activator to cultured human endothelial cells. J Clin Invest 1987; 80: 1712-1719
    CrossrefPubMedGoogle Scholar
  • 7 Verrall S, Seeds NW. Characterization of 125I-tissue plasminogen activator binding to cerebellar granule neurons. J Cell Biol 1989; 109: 265-271
    CrossrefPubMedGoogle Scholar
  • 8 Beebe DP. Binding of tissue plasminogen activator to human umbilical vein endothelial cells. Thromb Res 1987; 46: 241-254
    CrossrefPubMedGoogle Scholar
  • 9 Miles LA, Plow EF. Binding and activation of plasminogen on the platelet surface. J Biol Chem 1985; 260: 4303-4311
    PubMedGoogle Scholar
  • 10 Hajjar KA, Harpel PC, Jaffe EA, Nachman RL. Binding of plasminogen to cultured human endothelial cells. J Biol Chem 1986; 261: 11656-11662
    PubMedGoogle Scholar
  • 11 Stephens RW, Pollanen J, Tapiovaara H, Leung K-C, Sim P-S, Salonen E-M, Ronne E, Behrendt N, Dano K, Vaheri A. Activation of pro-urokinase and plasminogen on human sarcoma cells: a proteolytic system with surface-bound reactants. J Cell Biol 1989; 108: 1987-1995
    CrossrefPubMedGoogle Scholar
  • 12 Ellis V, Scully MF, Kakkar VV. Plasminogen activation initiated by single-chain urokinase-type plasminogen activator. J Biol Chem 1989; 264: 2185-2188
    PubMedGoogle Scholar
  • 13 Stricker RB, Wong D, Tak Shiu D, Reyes PT, Shuman MA. Activation of plasminogen by tissue plasminoagen activator on normal and thrombasthenic platelets: Effects on surface proteins and platelet aggregation. Blood 1986; 68: 275-280
    PubMedGoogle Scholar
  • 14 Camacho M, Fondaneche M-C, Burtin P. Limited proteolysis of tumor cells increase their plasmin-binding ability. FEBS Lett 1989; 245: 21-24
    CrossrefPubMedGoogle Scholar
  • 15 Miles LA, Dahlberg CM, Plescia J, Felez J, Kato K, Plow EF. Role of cell-surface lysines in plasminogen binding to cells: Identification of alpha-Enolase as a candidate plasminogen receptor. Biochemistry 1991; 30: 1682-1691
    CrossrefPubMedGoogle Scholar
  • 16 Plow EF, Freaney DE, Plescia J, Miles LA. The plasminogen system and cell surfaces: Evidence for plasminogen and urokinase receptors on the same cell type. J Cell Biol 1986; 103: 2411-2420
    CrossrefPubMedGoogle Scholar
  • 17 Bauer PI, Machovich R, Buki K, Csonka E, Koch S, Horvath I. Interaction of plasmin with endothelial cells. Biochem J 1984; 218: 119-124
    CrossrefPubMedGoogle Scholar
  • 18 Burtin P, Fondaneche M-C. Receptor for plasmin on human carcinoma cells. J Natl Cancer Inst 1988; 80: 762-765
    CrossrefPubMedGoogle Scholar
  • 19 Salonin E-M, Saksela O, Vartio T, Vaheri A, Nielsen LS, Zeuthen J. Plasminogen and tissue-type plasminogen activator bind to immobilized fibronectin. J Biol Chem 1985 260.
    PubMedGoogle Scholar
  • 20 Goldfarb RH, Liotta L. Proteolytic enzymes in cancer invasion and metastasis. Semin Thromb Hemost 1986; 12: 294-307
    Article in Thieme ConnectPubMedGoogle Scholar
  • 21 Paranjpe M, Engel L, Young N, Liotta LA. Activation of human breast carcinoma collagenase through plasminogen activator. Life Sci 1980; 26: 1223-1231
    CrossrefPubMedGoogle Scholar
  • 22 Gavrilovic J, Murphy G. The role of plasminogen in cell-mediated collagen degradation. Cell Biol Int Rep 1989; 13: 367-375
    CrossrefPubMedGoogle Scholar
  • 23 Rifkin DB, Moscatelli D. Recent developments in the cell biology of basic fibroblast growth factor. J Cell Biol 1989; 109: 1-6
    CrossrefPubMedGoogle Scholar
  • 24 Schlechte W, Murano G, Boyd D. Examination of the role of the urokinase receptor in human colon cancer mediated laminin degradation. Cancer Res 1989; 49: 6064-6069
    PubMedGoogle Scholar
  • 25 Cohen RL, Shuman MA. Tumor cells utilize cell-bound plasmin to degrade basement membranes. Clin Res 1990; 38: 466A
    PubMedGoogle Scholar
  • 26 Miles LA, Plow EF. Receptor mediated binding of the fibrinolytic components, plasminogen and urokinase, to peripheral blood cells. Thromb Haemost 1987; 58: 936-942
    Article in Thieme ConnectPubMedGoogle Scholar
  • 27 Miles LA, Levin EG, Plescia J, Collen D, Plow EF. Plasminogen receptors, urokinase receptors and their modulation on human endothelial cells. Blood 1988; 72: 628-635
    PubMedGoogle Scholar
  • 28 Hajjar KA, Nachman RL. Endothelial cell-mediated conversion of glu-plasminogen to lys-plasminogen. J Clin Invest 1988; 82: 1769-1778
    CrossrefPubMedGoogle Scholar
  • 29 Gonias SL, Braud LL, Geary WA, VandenBerg SR. Plasminogen binding to rat hepatocytes in primary culture and to thin slices of rat liver. Blood 1989; 74: 729-736
    PubMedGoogle Scholar
  • 30 Plow EF, Miles LA. Plasminogen receptors in the mediation of pericellular proteolysis. Cell Diff Dev 1991 (In Press)
    PubMedGoogle Scholar
  • 31 Miles LA, Dahlberg CM, Plow EF. The cell-binding domains of plasmimogen and their function in plasma. J Biol Chem 1988; 263: 11928-11934
    PubMedGoogle Scholar
  • 32 Adelman B, Rizk A, Hanners E. Plasminogen interactions with platelets in plasma. Blood 1988; 72: 1530-1535
    PubMedGoogle Scholar
  • 33 Miles LA, Ginsberg MH, White JG, Plow EF. Plasminogen interacts with human platelets through two distinct mechanisms. J Clin Invest 1986; 77: 2001-2009
    CrossrefPubMedGoogle Scholar
  • 34 Ryan TJ, Detmar DP, Perera TB. The effect of binding to U937 cells on the proteolytic activity of human plasmin. Fibrinolysis 1990; 4 (Suppl 3) 178
    PubMedGoogle Scholar
  • 35 Hall SW, VandenBerg SR, Gonias SL. Plasminogen carbohydrate side chains in receptor binding and enzyme activation: A study of C6 glioma cells and primary cultures of rat hepatocytes. J Cell Biochem 1990; 43: 213-227
    CrossrefPubMedGoogle Scholar
  • 36 Hall SW, VandenBerg SR, Gonias SL. Plasminogen carbohydrate side chains in receptor binding and enzyme ativation: A study of C6 glioma cells and primary cultures of rat hepatocytes. Blood 1989; 74 Suppl. 1 96a
    PubMedGoogle Scholar
  • 37 Silverstein RL, Friedlander Jr RJ, Nicholas RL, Nachman RL. Binding of lys-plasminogen to monocytes/macrophages. J Clin Invest 1988; 82: 1948-1955
    CrossrefPubMedGoogle Scholar
  • 38 Gonzales-Gronow M, Edelberg JM, Pizzo SV. Further characterization of the cellular plasminogen binding site: Evidence that plasminogen 2 and lipoprotein a compete for the same site. Biochemistry 1989; 28: 2374-2377
    CrossrefPubMedGoogle Scholar
  • 39 Edelberg JM, Enghild JJ, Pizzo SV, Gonzalez-Gronow M. Neonatal plasminogen displays altered cell surface binding and activation kinetics. Correlation with increased glycosylation of the protein. J Clin Invest 1990; 86: 107-112
    PubMedGoogle Scholar
  • 40 DesJardin LE, Boyle MDP, Lottenberg R. Group A streptococci bind human plasmin but not other structurally related proteins. Thromb Res 1989; 55: 187-193
    CrossrefPubMedGoogle Scholar
  • 41 Ullberg M, Kronvall G, Karlsson I, Wiman B. Receptors for human plasminogen on gram-negative bacteria. Infect Immun 1990; 58: 21-25
    PubMedGoogle Scholar
  • 42 Kuusela P, Saksela O. 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 1990; 193: 759-765
    CrossrefPubMedGoogle Scholar
  • 43 Miles LA, Dahlberg CM, Levin EG, Plow EF. Gangliosides interact directly with plasminogen and urokinase and may mediate binding of these components to cells. Biochemistry 1989; 280: 9337-9343
    PubMedGoogle Scholar
  • 44 Sugiyama N, Sasaki T, Iwamoto M, Abiko Y. Binding site of alpha2-plasmin inhibitor to plasminogen. Biochim Biophys Acta 1988; 952: 1-7
    CrossrefPubMedGoogle Scholar
  • 45 Hortin GL, Gibson BL, Fok KF. alpha2-antiplasmin's carboxy-terminal lysine residue is a major site of interaction with plasmin. Biochem Biophys Res Commun 1988; 155: 591-596
    CrossrefPubMedGoogle Scholar
  • 46 Auron PE, Webb AC, Rosenwasser LJ, Mucci SF, Rich A, Wolff SM, Dinarello CA. Nucleotide sequence of human monocyte interleukin 1 precurson cDNA. Proc Natl Acad Sci USA 1984; 81: 7907-7911
    CrossrefPubMedGoogle Scholar
  • 47 Abraham JA, Mergia A, Whang JL, Tumolo A, Friedman J, Hjerrild KA, Gospodarowicz D, Fiddes JC. Nucleotide sequence of a bovine clone encoding the angiogenic protein, basic fibroblast growth factor. Science 1986; 233: 545-548
    CrossrefPubMedGoogle Scholar
  • 48 Stopelli MP, Corti A, Soffientini A, Cassani G, Blasi F, Assoian RK. Differentiation-enhanced binding of the amino-terminal fragment of human urokinase plasminogen activator to a specific receptor on U937 monocytes. Proc Natl Acad Sci USA 1985; 82: 4939-4943
    CrossrefPubMedGoogle Scholar
  • 49 Li H, Lu H, Mirshahi Mc, Soria J, Mishal Z, Dosquet-Bernard C, Caen JP, Soria C. 1-25 OH vitamin D3 enhances plasmin generation on monoblastic cell line. Fibrinolysis 1988; 2 Supp. 1 151
    PubMedGoogle Scholar
  • 50 Felez J, Miles LA, Plescia J, Plow EF. Regulation of plasminogen receptor expression on human monocytes and monocytoid cell lines. J Cell Biol 1990; 111: 1673-1683
    CrossrefPubMedGoogle Scholar