Download PDF
Thromb Haemost 1997; 77(04): 718-724
DOI: 10.1055/s-0038-1656040
Fibrinolysis
Schattauer GmbH Stuttgart

Monoclonal Antibodies against the Human Mannose Receptor that Inhibit the Binding of Tissue-type Plasminogen Activator

Marrie Barrett-Bergshoeff
The Gaubius Laboratory, TNO Prevention and Health, Leiden, The Netherlands
,
Femke Noorman
The Gaubius Laboratory, TNO Prevention and Health, Leiden, The Netherlands
,
Rogier Bos
The Gaubius Laboratory, TNO Prevention and Health, Leiden, The Netherlands
,
Dingeman C Rijken
The Gaubius Laboratory, TNO Prevention and Health, Leiden, The Netherlands
› Author Affiliations
Further Information

Publication History

Received 05 July 1996

Accepted after resubmission 03 December 1996

Publication Date:
11 July 2018 (online)

  PDF Download  Permissions and Reprints

Summary

To study the role of the mannose receptor in cellular uptake and degradation of tissue-type plasminogen activator (t-PA), a set of five monoclonal antibodies (Moab) was generated against the mannose receptor isolated from human placental tissue.

All Moab specifically recognised the 175 kDa mannose receptor in a crude placenta extract, as shown in Western blot analysis. By use of im- munohistochemistry, we showed that in human placenta only the Hof- bauer cells (fetal macrophages) express the mannose receptor. Epitope competition experiments indicated that the Moab bound to at least two different epitopes on the receptor molecule. Moab 14-3, 14-5, and 15-2, which are directed against one of these epitopes, strongly inhibited the interaction between the purified mannose receptor and t-PA. These Moab also inhibited mannose receptor-mediated degradation of t-PA by cultured human macrophages. The low density lipoprotein receptor-related protein (LRP) mediated t-PA degradation was not affected by the Moab.

It is concluded that the Moab are useful for studying the expression of the human mannose receptor in Western blot and in immunohisto-chemistry, and for studying the interactions between the human mannose receptor and the mannose-containing ligand t-PA.

 

  • References

  • 1 Stahl PD. The mannose receptor and other macrophage lectins. Curr Opin Immunol 1992; 4: 49-52
    CrossrefPubMedGoogle Scholar
  • 2 Magnusson S, Berg T. Extremely rapid endocytosis mediated by the mannose receptor of sinusoidal endothelial liver cells. Biochem J 1989; 257: 651-656
    CrossrefPubMedGoogle Scholar
  • 3 Taylor ME, Conary JT, Lennartz MR, Stahl PD, Drickamer K. Primary structure of the mannose receptor contains multiple motifs resembling car-bohydrate-recognition domains. J Biol Chem 1990; 265: 12156-12162
    PubMedGoogle Scholar
  • 4 Taylor ME, Bezouska K, Drickamer K. Contribution to ligand binding by multiple carbohydrate-recognition domains in the macrophage mannose receptor. J Biol Chem 1992; 267: 1719-1726
    PubMedGoogle Scholar
  • 5 Taylor ME, Drickamer K. Structural requirements for high affinity binding of complex ligands by the macrophage mannose receptor. J Biol Chem 1993; 268: 399-404
    PubMedGoogle Scholar
  • 6 Rijken DC, Wijngaards G, Zaal-De Jong M, Welbergen J. Purification and partial characterization of plasminogen activator from human uterine tissue. Biochim Biophys Acta 1979; 580: 140-153
    CrossrefPubMedGoogle Scholar
  • 7 Rijken DC, Collen D. Purification and characterization of the plasminogen activator secreted by human melanoma cells in culture. J Biol Chem 1981; 256: 7035-7041
    PubMedGoogle Scholar
  • 8 Bachmann F. Fibrinolytic agents. Fibrinolysis 1995; suppl. 1 9-15
    PubMedGoogle Scholar
  • 9 Collen D. Fibrin-selective thrombolytic therapy for acute myocardial infarction. Circulation 1996; 93: 857-865
    CrossrefPubMedGoogle Scholar
  • 10 Spellman MW, Basa LJ, Leonard CK, Chakel JA, Connor JV, Wilson S, Van HalbeekH. Carbohydrate structures of human tissue-type plasminogen activator expressed in Chinese hamster ovary cells. J Biol Chem 1989; 264: 14100-14111
    PubMedGoogle Scholar
  • 11 Otter M, Kuiper J, van Berkel TJC, Rijken DC. Mechanisms of tissue-type plasminogen activator (t-PA) clearance by the liver. Ann NY Acad Sci 1992; 667: 431-442
    CrossrefPubMedGoogle Scholar
  • 12 Warshawsky I, Bu G, Schwartz AL. 39-kD protein inhibits tissue-type plasminogen activator clearance in vivo. J Clin Invest 1993; 92: 937-944
    CrossrefPubMedGoogle Scholar
  • 13 Smedsrød B, Einarsson M. Clearance of tissue plasminogen activator by mannose and galactose receptors in the liver. Thromb Haemost 1990; 63: 60-66
    Article in Thieme ConnectPubMedGoogle Scholar
  • 14 Narita M, Bu G, Herz J, Schwartz AL. Two receptor systems are involved in the plasma clearance of tissue-type plasminogen activator (t-PA) in vivo. J Clin Invest 1995; 96: 1164-1168
    CrossrefPubMedGoogle Scholar
  • 15 Noorman F, Braat EAM, Rijken DC. Degradation of tissue-type plasminogen activator (t-PA) by human monocyte derived macrophages is mediated by the mannose receptor and by the low density lipoprotein receptor-related protein (LRP). Blood 1995; 86: 3421-3427
    PubMedGoogle Scholar
  • 16 Hasapes JP, Daugherty A, Saffitz JE, Sobel BE. Determinants of the distribution of radiolabeled congeners of tissue-type plasminogen activator and its modification for improved clot imaging. Cor Art Dis 1992; 03: 641-649
    CrossrefPubMedGoogle Scholar
  • 17 Kuiper J, Otter M, Rijken DC, Van BerkelThJC. Characterization of the interaction in vivo of tissue-type plasminogen activator with liver cells. J Biol Chem 1988; 263: 18220-18224
    PubMedGoogle Scholar
  • 18 Mori K, Kawasaki T, Yamshina I. Isolation and characterization of endogenous ligands for liver mannan-binding protein. Arch Biochem Biophys 1988; 264: 647-656
    CrossrefPubMedGoogle Scholar
  • 19 Brock J, Schulze HA, Neels P, Fischer A, Bremer H, Walzel H. Detection of mannose-binding proteins on mouse lymphocytes. Eur J Cell Biol 1991; 54: 90-94
    PubMedGoogle Scholar
  • 20 Noorman F, Barrett-Braat EAM, van Bergshoeff MM, Barbé E, Leeuwen A, Lindeman J, Rijken DC. Monoclonal antibodies against the human mannose receptor as a specific marker in flow cytometry and immunohistochemistry for macrophages. J Leukocyte Biol 1997; 61: 63-72
    CrossrefPubMedGoogle Scholar
  • 21 Otter M, Barrett-Bergshoeff MM, Rijken DC. Binding of tissue-type plasminogen activator by the mannose receptor. J Biol Chem 1991; 266: 13931-13935
    PubMedGoogle Scholar
  • 22 Otter M, Zockova P, Kuiper Jm, van Berkel TJC, Barrett-Bergshoeff MM, Rijken DC. Isolation and characterization of the mannose receptor from human liver potentially involved in the plasma clearance of tissue-type plasminogen activator. Hepatology 1992; 16: 54-59
    CrossrefPubMedGoogle Scholar
  • 23 Lennartz MR, Wileman TE, Stahl PD. Isolation and characterization of a mannose-specific endocytosis receptor from rabbit alveolar macrophages. Biochem J 1987; 245: 705-711
    CrossrefPubMedGoogle Scholar
  • 24 Lennartz MR, Cole FS, Shepherd VL, Wileman TE, Stahl PD. Isolation and characterization of a mannose-specific endocytosis receptor from human placenta. J Biol Chem 1987; 262: 9942-9944
    PubMedGoogle Scholar
  • 25 Bos R, Siegel K, Otter M, Nieuwenhuizen W. Production and characterization of a set of monoclonal antibodies against tissue-type plasminogen activator (t-PA). Fibrinolysis 1992; 6: 173-182
    PubMedGoogle Scholar
  • 26 Westerwoud RJ. Improved fusion methods IV. Technical aspects J Immunol Meth 1984; 77: 181-196
    PubMedGoogle Scholar
  • 27 Browne MJ, Dodd I, Carey JE, Chapman CG, Robinson JH. Increased yield of human tissue-type plasminogen activator obtained by means of recombinant DNA technology. Thromb Haemost 1985; 54: 422-424
    Article in Thieme ConnectPubMedGoogle Scholar
  • 28 Kluft C, Van WezelA L, Van derVelden CAM, Emeis JJ, Verheijen JH, Wijngaards G. Large scale production of extrinsic (tissue-type) plasminogen activator from human melanoma cells. In: Advances in biotechnological processes, vol 2. Mizrahi A, Van WezelA L. eds Alan R Liss Inc; New York USA: 1983. pp 97-110
    Google Scholar
  • 29 Bos ES, Van derDoelen A A, Van RooyN, Schuurs AHWM. 3,3’, 5,5’-Tet-ramethylbenzidine as an Ames test negative chromogen for horse-radish peroxidasein enzyme.immunoassay. 2019; J Immunoassay 1981; 2: 187-204
    PubMedGoogle Scholar
  • 30 Dixon M, Webb EC. Chapter VIII Enzyme inhibitors. In: Enzymes. ed. second. Academic press Inc; New York USA: 1964. pp 315-359
    Google Scholar
  • 31 Haltiwanger H, Hill RL. The ligand specificity and tissue localisation of a rat alveolar macrophage lectin. J Biol Chem 1986; 261: 15696-15702
    PubMedGoogle Scholar
  • 32 Reise Sousa C, Stahl PD, Austyn JM. Phagocytosis of antigens by Lan-gerhans cells in vitro. J Exp Med 1993; 178: 509-519
    CrossrefPubMedGoogle Scholar
  • 33 Steinbach F, Thiele B. Phenotypic investigation of mononuclear phagocytes by flow cytometry. J Immunol Meth 1994; 174: 109-122
    CrossrefPubMedGoogle Scholar
  • 34 Jiang W, Swiggard WJ, Heufler C, Peng M, Mirza A, Steinman RM, Nus-senzweig MC. The receptor DEC-205 expressed by dendritic cells and thymic epithelial cells is involved in antigen processing. Nature 1995; 375: 151-154
    CrossrefPubMedGoogle Scholar
  • 35 Ishizaki J, Hanasaki K, Higashino K, Kishino J, Kikuchi N, Ohara O, Arita H. Molecular cloning of pancreatic group I phospholipase A2 receptor. J Biol Chem 1994; 8: 5897-5904
    PubMedGoogle Scholar
  • 36 Hanasaki K, Arita H. Characterization of a high affinity binding site for pancreatic-type phospholipase A2 in the rat. Its cellular and tissue distribution. J Biol Chem 1992; 9: 6414-6420
    PubMedGoogle Scholar
  • 37 Goldstein J, Braverman M, Salafia C, Buckley P. The phenotype of human placental macrophages and its variation with gestational age. Am J Pathol 1988; 133: 648-659
    PubMedGoogle Scholar
  • 38 Jones CJP, Fox H. Ultrastructure of the normal human placenta. Electron Microsc Rev 1991; 4: 129-178
    CrossrefPubMedGoogle Scholar
  • 39 Sallusto F, Celia M, Danieli C, Lanzavecchia A. Dendritic cells use macro-pinocytosis and the mannose receptor to concentrate macromolecules in the major histocompatibility complex class II compartment: Downregulation by cytokines and bacterial products. J Exp Med 1995; 182: 389-400
    CrossrefPubMedGoogle Scholar
  • 40 Ezekowitz RAB. The mannose receptor and phagocytosis. In: Mononuclear phagocytes: biology of monocytes and macrophages. van Furth R. ed. Kluwer Acedemic publishers group; Dordrecht The Netherlands: 1992. pp 208-213
    Google Scholar
  • 41 Ofek I, Goldhar J, Keisari Y. Nonopsonic phagocytosis of microorganisms. Annu Rev Microbiol 1995; 49: 239-276
    CrossrefPubMedGoogle Scholar
  • 42 Biessen EAL, Noorman F, van TeylingenM, Kuiper J, Barrett-Bergshoeff MM, Rijken DC, Bijsterbosch MK, van Berkel ThJC. Design of cluster mannosides as high affinity ligands for the human mannose receptor. J Biol Chem 1996; 271: 28024-28030
    CrossrefPubMedGoogle Scholar
  • 43 Noorman F, Barrett-Bergshoeff MM, Biessen EAL, van deBilt E, van Berkel, Th JC, Rijken DC. Cluster mannosides are able to inhibit mannose receptor mediated tissue-type plasminogen activator (t-PA) degradation by rat and human cells. Hepatology, submitted.
    PubMedGoogle Scholar
  • 44 Binder BR. Physiology and pathophysiology of the fibrinolytic system. Fibrinolysis 1995; (Suppl. 01) 9: 3-8
    PubMedGoogle Scholar