Download PDF
Thromb Haemost 1993; 70(01): 144-147
DOI: 10.1055/s-0038-1646176
State-of-the-Art Lecture
Plasminogen Activator Inhibitors
Schattauer GmbH Stuttgart

Biology and Facultative Secretion of Plasminogen Activator Inhibitor-2

Dominique Belin
Department of Pathology, University of Geneva Medical School, Geneva, SWITZERLAND
› Author Affiliations
Further Information

Publication History

Publication Date:
03 July 2018 (online)

Also available at
  PDF Download  Permissions and Reprints
 

  • References

  • 1 Vassalli J-D, Sappino AP, Belin D. The plasminogen activator/plasmin system. J Clin Invest 1991; 88: 1067-1072
    CrossrefPubMedGoogle Scholar
  • 2 Alexander CM, Werb Z. Extracellular matrix degradation. In: Cell Biology of Extracellular matrix. Hay ED. (ed). Plenum Press; New York: 1991. pp. 255-302
    CrossrefGoogle Scholar
  • 3 Danø K, Andreasen PA, Grondahl-Hansen J. etal: Plasminogen activators, tissue degradation, and cancer. Adv Cancer Res 1985; 44: 139-266
    PubMedGoogle Scholar
  • 4 Larsson LI, Skriver L, Nielsen LS, et al. Distribution of urokinase-type plasminogen activator immunoreactivity in the mouse. J Cell Biol 1984; 98: 894-903
    CrossrefPubMedGoogle Scholar
  • 5 Sappino AP, Huarte J, Vassalli JD. et al.: Sites of synthesis of urokinase and tissue-type plasminogen activators in the murine kidney. J Clin Invest 1991; 87: 962-970
    CrossrefPubMedGoogle Scholar
  • 6 Rifkin DB, Moscatelli D, Bizik J, et al. Growth factor control of extracellular proteolysis. Cell Differ Dev 1990; 32: 313-318
    CrossrefPubMedGoogle Scholar
  • 7 Naldini L, Tamagnone L, Vigna E. et al.: Extracellular proteolytic cleavage by urokinase is required for activation of hepatocyte growth factor/scatter factor. EMBO J 1992; 11: 4825-4833
    PubMedGoogle Scholar
  • 8 Vassalli JD, Wohlwend A, Belin D. Urokinase-catalyzed plasminogen activation at the monocyte/macrophage cell surface: A localized and regulated proteolytic system. Curr Top Microbiol Immunol 1992; 181: 65-86
    PubMedGoogle Scholar
  • 9 Pepper MS, Belin D, Montesano R. et al.: Transforming growth factor-beta 1 modulates basic fibroblast growth factor-induced proteolytic and angiogenic properties of endothelial cells in vitro . J Cell Biol 1990; 111: 743-755
    CrossrefPubMedGoogle Scholar
  • 10 Huber R, Carrell RW. Implications of the three-dimensional structure of alpha 1-antitrypsin for structure and function of serpins. Biochemistry 1989; 28: 8951-8966
    CrossrefPubMedGoogle Scholar
  • 11 Fay WP, Shapiro AD, Shih JL. et al.: Brief report: Complete deficiency of plasminogen-activator inhibitor type 1 due to a frame-shift mutation. N Engl J Med 1992; 327: 1729-1733
    CrossrefPubMedGoogle Scholar
  • 12 Erickson LA, Fici GJ, Lund JE. et al.: Development of venous occlusions in mice transgenic for the plasminogen activator inhibitor-1 gene. Nature 1990; 346: 74-76
    CrossrefPubMedGoogle Scholar
  • 13 Baker JB, Low DA, Simmer RL. et al.: Protease-nexin: a cellular component that links thrombin and plasminogen activator and mediates their binding to cells. Cell 1980; 21: 37-45
    CrossrefPubMedGoogle Scholar
  • 14 Vassalli JD, Huarte J, Bosco D, Sappino AP, Sappino N, Velardi A, Wohlwend A, Erno H, Monard D, Belin D. Protease nexin I as an androgen dependent secretory product of the seminal vesicle. EMBO J. 1993 in press
    PubMedGoogle Scholar
  • 15 Kawano T, Morimoto K, Uemura Y. Urokinase inhibitor in human placenta. Nature 1968; 217: 253-254
    CrossrefPubMedGoogle Scholar
  • 16 Chapman Jr HA, Vavrin Z, Hibbs Jr. JB. Macrophage fibrinolytic activity: identification of two pathways of plasmin formation by intact cells and of a plasminogen activator inhibitor. Cell 1982; 28: 653-662
    CrossrefPubMedGoogle Scholar
  • 17 Hashimoto K, Prystowsky JH, Baird J, Lazarus GS, Jensen PJ. Keratinocyte urokinase-type plasminogen activator is secreted as a single chain precursor. J Invest Dermatol 1988; 90: 823-828
    CrossrefPubMedGoogle Scholar
  • 18 Kruithof EKO, Tran-Thang C, Gudinchet A. et al.: Fibrinolysis in pregnancy: a study of plasminogen activator inhibitors. Blood 1987; 69: 460-466
    PubMedGoogle Scholar
  • 19 Schleuning W-D, Medcalf RL, Hession C. et al.: Plasminogen activator inhibitor 2: regulation of gene transcription during phorbol ester-mediated differentiation of U-937 human histiocytic lymphoma cells. Mol Cell Biol 1987; 7: 4564-4567
    CrossrefPubMedGoogle Scholar
  • 20 Ye RD, Wun TC, Sadler JE. cDNA cloning and expression in Escherichia coli of a plasminogen activator inhibitor from human placenta. J Biol Chem 1987; 262: 3718-3725
    PubMedGoogle Scholar
  • 21 Webb AC, Collins KL, Snyder SE, et al. Human monocyte Arg-Serpin cDNA. Sequence, chromosomal assignment, and homology to plasminogen activator-inhibitor. J Exp Med 1987; 166: 77-94
    CrossrefPubMedGoogle Scholar
  • 22 Belin D, Wohlwend A, Schleuning WD. et al.: Facultative polypeptide translocation allows a single mRNA to encode the secreted and cytosolic forms of plasminogen activators inhibitor 2. EMBO J 1989; 8: 3287-3294
    PubMedGoogle Scholar
  • 23 Ye RD, Ahern SM, Le Beau MM. et al.: Structure of the gene for human plasminogen activator inhibitor-2. The nearest mammalian homologue of chicken ovalbumin. J Biol Chem 1989; 264: 5495-5502
    PubMedGoogle Scholar
  • 24 Schwartz BS, Bradshaw JD. Regulation of plasminogen activator inhibitor mRNA levels in lipopolysaccharide-stimulated human monocytes. Correlation with production of the protein. J Biol Chem 1992; 267: 7089-7094
    PubMedGoogle Scholar
  • 25 Feinberg RF, Kao LC, Haimowitz JE. et al.: Plasminogen activator inhibitor types 1 and 2 in human trophoblasts. PAI-1 is an immunocytochemical marker of invading trophoblasts. Lab Invest 1989; 61: 20-26
    PubMedGoogle Scholar
  • 26 Sutter TR, Guzman K, Dold KM, et al. Targets for dioxin: Genes for plasminogen activator inhibitor-2 and interleukin-1. Science 1991; 254: 415-418
    CrossrefPubMedGoogle Scholar
  • 27 Medcalf RL. Cell- and gene-specific interactions between signal transduction pathways revealed by okadaic acid. Studies on the plasminogen activating system. J Biol Chem 1992; 267: 12220-12226
    PubMedGoogle Scholar
  • 28 Wohlwend A, Belin D, Vassalli JD. Plasminogen activator-specific inhibitors in mouse macrophages: in vivo and in vitro modulation of their synthesis and secretion. J Immunol 1987; 139: 1278-1284
    CrossrefPubMedGoogle Scholar
  • 29 Sawdey MS, Loskutoff DJ. Regulation of murine type 1 plasminogen activator inhibitor gene expression in vivo. Tissue specificity and induction by lipopolysaccharide, tumor necrosis factor-alpha, and transforming growth factor-beta. J Clin Invest 1991; 88: 1346-1353
    CrossrefPubMedGoogle Scholar
  • 30 Lawrence DA, Loskutoff DJ. Inactivation of plasminogen activator inhibitor by oxidants. Biochemistry 1986; 25: 6351-6355
    CrossrefPubMedGoogle Scholar
  • 31 Heiple JM, Ossowski L. Human neutrophil plasminogen activator is localized in specific granules and is translocated to the cell surface by exocytosis. J Exp Med 1986; 164: 826-840
    CrossrefPubMedGoogle Scholar
  • 32 Colvin RB, Johnson RA, Mihm Jr. MC. et al.: Role of the clotting system in cell-mediated hypersensitivity. I. Fibrin deposition in delayed skin reactions in man. J Exp Med 1973; 138: 686-698
    CrossrefPubMedGoogle Scholar
  • 33 Bertozzi P, Astedt B, Zenzius L. et al.: Depressed bronchoalveolar urokinase activity in patients with adult respiratory distress syndrome. N Engl J Med 1990; 322: 890-897
    CrossrefPubMedGoogle Scholar
  • 34 Marshall BC, Xu QP, Rao NV, Brown BR, Hoidal JR. Pulmonary epithelial cell urokinase-type plasminogen activator. J Biol Chem 1992; 267: 11462-11469
    PubMedGoogle Scholar
  • 35 Gyetko MR, Shollenberger SB, Sitrin RG. Urokinase expression in mononuclear phagocytes: Cytokine-specific modulation by interferon-gamma and tumor necrosis factor α. J Leukocyte Biol 1992; 51: 256-263
    CrossrefPubMedGoogle Scholar
  • 36 Kumar S, Baglioni C. Protection from tumor necrosis factor-mediated cytolysis by overexpression of plasminogen activator inhibitor type-2. J Biol Chem 1991; 266: 20960-20964
    PubMedGoogle Scholar
  • 37 Vassalli P. The pathophysiology of tumor necrosis factors. Ann Rev Immunol 1992; 10: 411-452
    CrossrefPubMedGoogle Scholar
  • 38 Piguet PF, Collart MA, Grau GE. et al.: Requirement of tumour necrosis factor for development of silica-induced pulmonary fibrosis. Nature 1990; 344: 245-247
    CrossrefPubMedGoogle Scholar
  • 39 Grondahl-Hansen J, Lund LR, Ralfkiaer E. et al.: Urokinase- and tissue-type plasminogen activators in keratinocytes during wound reepithelialization in vivo . J Invest Dermatol 1988; 90: 790-795
    CrossrefPubMedGoogle Scholar
  • 40 Wood GW, De M, Sanford T, Choudhuri R. Macrophage colony stimulating factor controls macrophage recruitment to the cycling mouse uterus. Dev Biol 1992; 152: 336-343
    CrossrefPubMedGoogle Scholar
  • 41 Sappino AP, Huarte J, Belin D. et al.: Plasminogen activators in tissue remodeling and invasion: mRNA localization in mouse ovaries and implanting embryos. J Cell Biol 1989; 109: 2471-2479
    CrossrefPubMedGoogle Scholar
  • 42 Herz J, Clouthier DE, Hammer RE. LDL receptor-related protein internalizes and degrades uPA-PAI-1 complexes and is essential for embryo implantation. Cell 1992; 71: 411-421
    CrossrefPubMedGoogle Scholar
  • 43 Remold-O'Donnell E. The ovalbumin family of serpin proteins. FEBS Lett 1993; 315: 105-108
    CrossrefPubMedGoogle Scholar
  • 44 Wohlwend A, Belin D, Vassalli JD. Plasminogen activator-specific inhibitors produced by human monocytes/macrophages. J Exp Med 1987; 165: 320-339
    CrossrefPubMedGoogle Scholar
  • 45 Genton C, Kruithof EKO, Schleuning WD. Phorbol ester induces the biosynthesis of glycosylated and nonglycosylated plasminogen activator inhibitor 2 in high excess over urokinase-type plasminogen activator in human U-937 lymphoma cells. J Cell Biol 1987; 104: 705-712
    CrossrefPubMedGoogle Scholar
  • 46 Ye RD, Wun TC, Sadler JE. Mammalian protein secretion without signal peptide removal. Biosynthesis of plasminogen activator inhibitor-2 in U-937 cells. J Biol Chem 1988; 263: 4869-4875
    PubMedGoogle Scholar
  • 47 Dubin A, Travis J, Enghild JJ. et al.: Equine leukocyte elastase inhibitor. Primary structure and identification as a thymosin-binding protein. J Biol Chem 1992; 267: 6576-6583
    PubMedGoogle Scholar
  • 48 Remold O'Donnell E, Chin J, Alberts M. Sequence and molecular characterization of human monocyte/neutrophil elastase inhibitor. Proc Natl Acad Sci USA 1992; 89: 5635-5639
    CrossrefPubMedGoogle Scholar
  • 49 Suminami Y, Kishi F, Sekiguchi K, Kato H. Squamous cell carcinoma antigen is a new member of the serine protease inhibitors. Biochem Biophys Res Comm 1991; 181: 51-58
    CrossrefPubMedGoogle Scholar
  • 50 Von Heijne G. Net N-C charge imbalance may be important for signal sequence function in bacteria. J Mol Biol 1986; 192: 287-290
    CrossrefPubMedGoogle Scholar
  • 51 Von Heijne G, Liljestrom P, Mikus P. et al.: The efficiency of the uncleaved secretion signal in the plasminogen activator inhibitor type 2 protein can be enhanced by point mutations that increase its hydrophobicity. J Biol Chem 1991; 266: 15240-15243
    PubMedGoogle Scholar
  • 52 Steven J, Cottingham IR, Berry SJ. et al.: Purification and characterisation of plasminogen activator inhibitor 2 produced in Saccharomyces cerevisiae. Eur J Biochem 1991; 196: 431-438
    CrossrefPubMedGoogle Scholar
  • 53 Medcalf RL, Kruithof EKO, Schleuning WD. Plasminogen activator inhibitor 1 and 2 are tumor necrosis factor/cachectin-responsive genes. J Exp Med 1988; 168: 751-759
    CrossrefPubMedGoogle Scholar
  • 54 Brodbeck RM, Brown JL. Secretion of alpha-1-proteinase inhibitor requires an almost full length molecule. J Biol Chem 1992; 267: 294-297
    PubMedGoogle Scholar
  • 55 Hogquist KA, Nett MA, Unanue ER. et al.: Interleukin 1 is processed and released during apoptosis. Proc Natl Acad Sci USA 1991; 88: 8485-8489
    CrossrefPubMedGoogle Scholar
  • 56 Ray CA, Black RA, Kronheim SR. et al.: Viral inhibition of inflammation: cowpox virus encodes an inhibitor of the interleukin-1 beta converting enzyme. Cell 1992; 69: 597-604
    CrossrefPubMedGoogle Scholar