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Gene Review

MASP2  -  mannan-binding lectin serine peptidase 2

Homo sapiens

Synonyms: MAP19, MASP-2, MASP1P1, MBL-associated serine protease 2, Mannan-binding lectin serine protease 2, ...
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Disease relevance of MASP2


High impact information on MASP2

  • MASP-1, MAp19, and direct C3-cleaving activity are associated with smaller oligomers whereas MASP-3 is found together with MASP-2 on larger oligomers [6].
  • MASP-3 downregulate the C4 and C2 cleaving activity of MASP-2 [6].
  • Lectin Pathway of Bony Fish Complement: Identification of Two Homologs of the Mannose-Binding Lectin Associated with MASP2 in the Common Carp (Cyprinus carpio) [7].
  • Molecular cloning and phylogenetic analysis revealed this C4-activating protease to be carp MASP2, indicating that MASP2 arose before the emergence of bony fish [7].
  • Upon activation of the lectin pathway, MASP-2 cleaves C4 and C2 [8].

Chemical compound and disease context of MASP2

  • The mannan-binding lectin pathway and lung disease in cystic fibrosis-dysfunction of mannan-binding lectin-associated serine protease 2 (MASP-2) may be a major modifier [9].

Biological context of MASP2

  • The MASP1 gene is located on chromosome 3q27, the MASP2 gene on chromosome 1p36.23-31 [10].
  • RESULTS: Ten percent of the donors and 11% of the recipients carried the MBL-low (O/O, LXA/O) genotypes; 7% of the donors and 3% of the recipients were heterozygous for the MASP2 Asp105Gly variant [11].
  • A comparison of the MASP2 gene with the previously characterised C1s gene revealed identical positions of introns separating orthologous coding sequences, underlining the hypothesis that the C1s and MASP2 genes arose by exon shuffling from one ancestral gene [10].
  • The stimulatory effects of IL-1beta on MASP1/3 and MASP2 gene expression were abolished by the simultaneous presence of IL-6 [12].
  • Mammals and Xenopus possess two distinct MASPs, MASP1 and MASP2, with different substrate specificity [13].

Anatomical context of MASP2


Associations of MASP2 with chemical compounds

  • Complexes of MBL-MASP2 are able to activate the complement system in an Ab and C1-independent fashion after binding of the lectin to appropriate microbial sugar arrays [18].
  • We have shown that the MASP2 gene encodes two gene products, the 76 kDa MASP-2 serine protease and a plasma protein of 19 kDa, termed MAp19 or sMAP [10].
  • It is likely that human MASP1 is able to activate C3, while human MASP2 cleaves C4, although further functional studies are required to confirm this [19].
  • On an anti-MASP-1 column, MASP-2 passed through the column in the presence of EDTA and high salt concentration, whereas MASP-1 was retained [20].
  • Western blotting analysis showed the presence of MASP-1, MASP-2, MASP-3, and sMAP in H-ficolin preparations isolated from Cohn Fraction III [21].

Physical interactions of MASP2


Enzymatic interactions of MASP2

  • We have demonstrated that MASP-2 is a C4 cleaving component of the MBL/MASP complex [23].

Regulatory relationships of MASP2


Other interactions of MASP2

  • Isolated MASP-1 and MASP-2 exhibited proteolytic activities against C3 and C4, respectively [20].
  • C1 inhibitor (C1 INH), an inhibitor for C1r and C1s, formed equimolar complexes with MASP-1 and MASP-2 and inhibited their proteolytic activities [20].
  • We report here that ficolin/P35, a human serum ficolin, was found to copurify with MASPs and sMAP [1].
  • Both enzymes cleaved C3i 10- to 20-fold faster, but still at only approximately 1% of the efficiency of MASP-2 cleavage of C2 [26].
  • We suspect total MASP-2 dysfunction to be a major modifier of CF lung disease [9].

Analytical, diagnostic and therapeutic context of MASP2


  1. Cutting edge: complement-activating complex of ficolin and mannose-binding lectin-associated serine protease. Matsushita, M., Endo, Y., Fujita, T. J. Immunol. (2000) [Pubmed]
  2. Functional MASP2 single nucleotide polymorphism plays no role in psoriasis. Stover, C., Barrett, S., Lynch, N.J., Barker, J.N., Burden, D., Trembath, R., Schwaeble, W., Veal, C. Br. J. Dermatol. (2005) [Pubmed]
  3. Substrate specificities of recombinant mannan-binding lectin-associated serine proteases-1 and -2. Rossi, V., Cseh, S., Bally, I., Thielens, N.M., Jensenius, J.C., Arlaud, G.J. J. Biol. Chem. (2001) [Pubmed]
  4. Serum mannan-binding lectin-associated serine protease 2 levels in colorectal cancer: relation to recurrence and mortality. Ytting, H., Christensen, I.J., Thiel, S., Jensenius, J.C., Nielsen, H.J. Clin. Cancer Res. (2005) [Pubmed]
  5. Clinical significance of mannose-binding lectin-associated serine protease-2 expression in esophageal squamous cell carcinoma. Verma, A., Matta, A., Shukla, N.K., Deo, S.V., Gupta, S.D., Ralhan, R. Int. J. Cancer (2006) [Pubmed]
  6. MASP-3 and its association with distinct complexes of the mannan-binding lectin complement activation pathway. Dahl, M.R., Thiel, S., Matsushita, M., Fujita, T., Willis, A.C., Christensen, T., Vorup-Jensen, T., Jensenius, J.C. Immunity (2001) [Pubmed]
  7. Lectin Pathway of Bony Fish Complement: Identification of Two Homologs of the Mannose-Binding Lectin Associated with MASP2 in the Common Carp (Cyprinus carpio). Nakao, M., Kajiya, T., Sato, Y., Somamoto, T., Kato-Unoki, Y., Matsushita, M., Nakata, M., Fujita, T., Yano, T. J. Immunol. (2006) [Pubmed]
  8. Small mannose-binding lectin-associated protein plays a regulatory role in the lectin complement pathway. Iwaki, D., Kanno, K., Takahashi, M., Endo, Y., Lynch, N.J., Schwaeble, W.J., Matsushita, M., Okabe, M., Fujita, T. J. Immunol. (2006) [Pubmed]
  9. The mannan-binding lectin pathway and lung disease in cystic fibrosis-dysfunction of mannan-binding lectin-associated serine protease 2 (MASP-2) may be a major modifier. Olesen, H.V., Jensenius, J.C., Steffensen, R., Thiel, S., Schi??tz, P.O. Clin. Immunol. (2006) [Pubmed]
  10. The human gene for mannan-binding lectin-associated serine protease-2 (MASP-2), the effector component of the lectin route of complement activation, is part of a tightly linked gene cluster on chromosome 1p36.2-3. Stover, C., Endo, Y., Takahashi, M., Lynch, N.J., Constantinescu, C., Vorup-Jensen, T., Thiel, S., Friedl, H., Hankeln, T., Hall, R., Gregory, S., Fujita, T., Schwaeble, W. Genes Immun. (2001) [Pubmed]
  11. Mannan-binding lectin pathway deficiencies and invasive fungal infections following allogeneic stem cell transplantation. Granell, M., Urbano-Ispizua, A., Suarez, B., Rovira, M., Fernández-Avilés, F., Martínez, C., Ortega, M., Uriburu, C., Gaya, A., Roncero, J.M., Navarro, A., Carreras, E., Mensa, J., Vives, J., Rozman, C., Montserrat, E., Lozano, F. Exp. Hematol. (2006) [Pubmed]
  12. Functional characterization of human mannose-binding lectin-associated serine protease (MASP)-1/3 and MASP-2 promoters, and comparison with the C1s promoter. Endo, Y., Takahashi, M., Kuraya, M., Matsushita, M., Stover, C.M., Schwaeble, W.J., Fujita, T. Int. Immunol. (2002) [Pubmed]
  13. A novel truncated isoform of the mannose-binding lectin-associated serine protease (MASP) from the common carp (Cyprinus carpio). Nagai, T., Mutsuro, J., Kimura, M., Kato, Y., Fujiki, K., Yano, T., Nakao, M. Immunogenetics (2000) [Pubmed]
  14. Assignment of the gene encoding mannan-binding lectin-associated serine protease 2 (MASP2) to human chromosome 1p36.3-->p36.2 by in situ hybridization and somatic cell hybrid analysis. Stover, C.M., Schwaeble, W.J., Lynch, N.J., Thiel, S., Speicher, M.R. Cytogenet. Cell Genet. (1999) [Pubmed]
  15. Mannose-binding lectin binds IgM to activate the lectin complement pathway in vitro and in vivo. McMullen, M.E., Hart, M.L., Walsh, M.C., Buras, J., Takahashi, K., Stahl, G.L. Immunobiology (2006) [Pubmed]
  16. Lectin complement system and pattern recognition. Endo, Y., Takahashi, M., Fujita, T. Immunobiology (2006) [Pubmed]
  17. Mannose-binding lectin (MBL) in health and disease. Turner, M.W. Immunobiology (1998) [Pubmed]
  18. Enhancement of complement activation and opsonophagocytosis by complexes of mannose-binding lectin with mannose-binding lectin-associated serine protease after binding to Staphylococcus aureus. Neth, O., Jack, D.L., Johnson, M., Klein, N.J., Turner, M.W. J. Immunol. (2002) [Pubmed]
  19. MASP1 (MBL-associated serine protease 1). Matsushita, M., Endo, Y., Fujita, T. Immunobiology (1998) [Pubmed]
  20. Proteolytic activities of two types of mannose-binding lectin-associated serine protease. Matsushita, M., Thiel, S., Jensenius, J.C., Terai, I., Fujita, T. J. Immunol. (2000) [Pubmed]
  21. Activation of the lectin complement pathway by H-ficolin (Hakata antigen). Matsushita, M., Kuraya, M., Hamasaki, N., Tsujimura, M., Shiraki, H., Fujita, T. J. Immunol. (2002) [Pubmed]
  22. Novel MASP2 variants detected among North African and Sub-Saharan individuals. Lozano, F., Suárez, B., Muñoz, A., Jensenius, J.C., Mensa, J., Vives, J., Horcajada, J.P. Tissue Antigens (2005) [Pubmed]
  23. MASP-2, the C3 convertase generating protease of the MBLectin complement activating pathway. Vorup-Jensen, T., Jensenius, J.C., Thiel, S. Immunobiology (1998) [Pubmed]
  24. The mannan-binding lectin-associated serine proteases (MASPs) and MAp19: four components of the lectin pathway activation complex encoded by two genes. Schwaeble, W., Dahl, M.R., Thiel, S., Stover, C., Jensenius, J.C. Immunobiology (2002) [Pubmed]
  25. Characterization of an equine mannose-binding lectin and its roles in disease. Podolsky, M.J., Lasker, A., Flaminio, M.J., Gowda, L.D., Ezekowitz, R.A., Takahashi, K. Biochem. Biophys. Res. Commun. (2006) [Pubmed]
  26. Natural substrates and inhibitors of mannan-binding lectin-associated serine protease-1 and -2: a study on recombinant catalytic fragments. Ambrus, G., Gál, P., Kojima, M., Szilágyi, K., Balczer, J., Antal, J., Gráf, L., Laich, A., Moffatt, B.E., Schwaeble, W., Sim, R.B., Závodszky, P. J. Immunol. (2003) [Pubmed]
  27. Interaction properties of human mannan-binding lectin (MBL)-associated serine proteases-1 and -2, MBL-associated protein 19, and MBL. Thielens, N.M., Cseh, S., Thiel, S., Vorup-Jensen, T., Rossi, V., Jensenius, J.C., Arlaud, G.J. J. Immunol. (2001) [Pubmed]
  28. Deficiency of the mannan-binding lectin pathway of complement and poor outcome in cystic fibrosis: bacterial colonization may be decisive for a relationship. Carlsson, M., Sjöholm, A.G., Eriksson, L., Thiel, S., Jensenius, J.C., Segelmark, M., Truedsson, L. Clin. Exp. Immunol. (2005) [Pubmed]
  29. The rat and mouse homologues of MASP-2 and MAp19, components of the lectin activation pathway of complement. Stover, C.M., Thiel, S., Lynch, N.J., Schwaeble, W.J. J. Immunol. (1999) [Pubmed]
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