Encyclopedia of Signaling Molecules

2018 Edition
| Editors: Sangdun Choi


  • Péter GálEmail author
  • József Dobó
Reference work entry
DOI: https://doi.org/10.1007/978-3-319-67199-4_101691


Historical Background

In the late 1980s, a new activation pathway of the complement system, the lectin pathway, was discovered. The complement system is a proteolytic cascade system which forms an effector arm of innate immunity (Ricklin et al. 2010). The complement system is capable of labeling and eliminating invading pathogens (e.g., bacteria, fungi) and dangerously altered host cells (e.g., cancer cells, apoptotic cells). In this way, the complement system contributes to the protection against infection and to the maintenance of the homeostasis of the body. There are three ways through which the complement cascade can be activated. The classical and the alternative pathways of complement activation had been known for decades, when (in 1987)...

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  1. Ambrus G, Gál P, Kojima M, Szilágyi K, Balczer J, Antal J, Gráf L, Laich A, Moffatt BE, Schwaeble W, Sim RB, Závodszky P. Natural substrates and inhibitors of mannan-binding lectin-associated serine protease-1 and -2: a study on recombinant catalytic fragments. J Immunol. 2003;170:1374–82.CrossRefPubMedGoogle Scholar
  2. Degn SE, Jensen L, Hansen AG, Duman D, Tekin M, Jensenius JC, Thiel S. Mannan-binding lectin-associated serine protease (MASP)-1 is crucial for lectin pathway activation in human serum, whereas neither MASP-1 nor MASP-3 is required for alternative pathway function. J Immunol. 2012;189:3957–69.CrossRefPubMedGoogle Scholar
  3. Degn SE, Kjaer TR, Kidmose RT, Jensen L, Hansen AG, Tekin M, Jensenius JC, Andersen GR, Thiel S. Complement activation by ligand-driven juxtaposition of discrete pattern recognition complexes. Proc Natl Acad Sci U S A. 2014;111:13445–50.PubMedPubMedCentralCrossRefGoogle Scholar
  4. Dobó J, Harmat V, Beinrohr L, Sebestyén E, Závodszky P, Gál P. MASP-1, a promiscuous complement protease: structure of its catalytic region reveals the basis of its broad specificity. J Immunol. 2009;183(2):1207–14.CrossRefPubMedGoogle Scholar
  5. Dobó J, Major B, Kékesi KA, Szabó I, Megyeri M, Hajela K, Juhász G, Závodszky P, Gál P. Cleavage of kininogen and subsequent bradykinin release by the complement component: mannose-binding lectin-associated serine protease (MASP)-1. PLoS One. 2011;6(5):e20036.PubMedPubMedCentralCrossRefGoogle Scholar
  6. Dobó J, Szakács D, Oroszlán G, Kortvely E, Kiss B, Boros E, Szász R, Závodszky P, Gál P, Pál G. MASP-3 is the exclusive pro-factor D activator in resting blood: the lectin and the alternative complement pathways are fundamentally linked. Sci Rep. 2016;6:31877.PubMedPubMedCentralCrossRefGoogle Scholar
  7. Gál P, Barna L, Kocsis A, Závodszky P. Serine proteases of the classical and lectin pathways: similarities and differences. Immunobiology. 2007;212:267–77.CrossRefPubMedGoogle Scholar
  8. Hajela K, Kojima M, Ambrus G, Wong KH, Moffatt BE, Ferluga J, Hajela S, Gál P, Sim RB. The biological functions of MBL-associated serine proteases (MASPs). Immunobiology. 2002;205:467–75.CrossRefPubMedGoogle Scholar
  9. Héja D, Kocsis A, Dobó J, Szilágyi K, Szász R, Závodszky P, Pál G, Gál P. Revised mechanism of complement lectin-pathway activation revealing the role of serine protease MASP-1 as the exclusive activator of MASP-2. Proc Natl Acad Sci U S A. 2012;109:10498–503.PubMedPubMedCentralCrossRefGoogle Scholar
  10. Hess K, Ajjan R, Phoenix F, Dobó J, Gál P, Schroeder V. Effects of MASP-1 of the complement system on activation of coagulation factors and plasma clot formation. PLoS One. 2012;7(4):e35690.PubMedPubMedCentralCrossRefGoogle Scholar
  11. Ikeda K, Sannoh T, Kawasaki N, Kawasaki T, Yamashina I. Serum lectin with known structure activates complement through the classical pathway. J Biol Chem. 1987;262:7451–4.PubMedGoogle Scholar
  12. Jani PK, Kajdácsi E, Megyeri M, Dobó J, Doleschall Z, Futosi K, Tímár CI, Mócsai A, Makó V, Gál P, Cervenak L. MASP-1 induces a unique cytokine pattern in endothelial cells: a novel link between complement system and neutrophil granulocytes. PLoS One. 2014;9:e87104.PubMedPubMedCentralCrossRefGoogle Scholar
  13. Jani PK, Schwaner E, Kajdácsi E, Debreczeni ML, Ungai-Salánki R, Dobó J, Doleschall Z, Rigó Jr J, Geiszt M, Szabó B, Gál P, Cervenak L. Complement MASP-1 enhances adhesion between endothelial cells and neutrophils by up-regulating E-selectin expression. Mol Immunol. 2016;75:38–47.CrossRefPubMedGoogle Scholar
  14. Jenny L, Dobó J, Gál P, Schroeder V. MASP-1 induced clotting – the first model of prothrombin activation by MASP-1. PLoS One. 2015;10:e0144633.PubMedPubMedCentralCrossRefGoogle Scholar
  15. La Bonte LR, Pavlov VI, Tan YS, Takahashi K, Takahashi M, Banda NK, Zou C, Fujita T, Stahl GL. Mannose-binding lectin-associated serine protease-1 is a significant contributor to coagulation in a murine model of occlusive thrombosis. J Immunol. 2012;188(2):885–91.CrossRefPubMedGoogle Scholar
  16. Matsushita M, Fujita T. Cleavage of the third component of complement (C3) by mannose-binding protein-associated serine protease (MASP) with subsequent complement activation. Immunobiology. 1995;194:443–8.CrossRefPubMedGoogle Scholar
  17. Megyeri M, Harmat V, Major B, Végh Á, Balczer J, Héja D, Szilágyi K, Datz D, Pál G, Závodszky P, Gál P, Dobó J. Quantitative characterization of the activation steps of mannan-binding lectin (MBL)-associated serine proteases (MASPs) points to the central role of MASP-1 in the initiation of the complement lectin pathway. J Biol Chem. 2013;288:8922–34.PubMedPubMedCentralCrossRefGoogle Scholar
  18. Megyeri M, Makó V, Beinrohr L, Doleschall Z, Prohászka Z, Cervenak L, Závodszky P, Gál P. Complement protease MASP-1 activates human endothelial cells: PAR4 activation is a link between complement and endothelial function. J Immunol. 2009;183:3409–16.CrossRefPubMedGoogle Scholar
  19. Paréj K, Dobó J, Závodszky P, Gál P. The control of the complement lectin pathway activation revisited: both C1-inhibitor and antithrombin are likely physiological inhibitors, while α2-macroglobulin is not. Mol Immunol. 2013;54:415–22.CrossRefPubMedGoogle Scholar
  20. Ricklin D, Hajishengallis G, Yang K, Lambris JD. Complement: a key system for immune surveillance and homeostasis. Nat Immunol. 2010;11:785–97.PubMedPubMedCentralCrossRefGoogle Scholar
  21. Takahashi K, Chang WC, Takahashi M, Pavlov V, Ishida Y, La Bonte L, Shi L, Fujita T, Stahl GL, Van Cott EM. Mannose-binding lectin and its associated proteases (MASPs) mediate coagulation and its deficiency is a risk factor in developing complications from infection, including disseminated intravascular coagulation. Immunobiology. 2011;216:96–102.CrossRefPubMedGoogle Scholar

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© Springer International Publishing AG 2018

Authors and Affiliations

  1. 1.Institute of Enzymology, Research Centre for Natural SciencesHungarian Academy of SciencesBudapestHungary