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Gene Review

FCN2  -  ficolin (collagen/fibrinogen domain...

Homo sapiens

Synonyms: 37 kDa elastin-binding protein, Collagen/fibrinogen domain-containing protein 2, EBP-37, FCNL, Ficolin-2, ...
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Disease relevance of FCN2


High impact information on FCN2


Chemical compound and disease context of FCN2


Biological context of FCN2


Anatomical context of FCN2

  • L-ficolin and H-ficolin are molecules of the innate immune system [3].
  • The sequences of exons in the P35-related gene were identical to the cDNA sequence reported for "human ficolin." Northern blotting revealed that the P35 gene is expressed mainly in liver, whereas the P35-related gene is expressed in lung and peripheral blood leukocytes, demonstrating tissue-specific expression of these two genes [14].
  • Cord blood samples had significantly lower levels of P35 (median 2.5 microg/ml) than adults, and cord P35 concentrations correlated with gestational age [15].
  • We developed a monoclonal rat anti-human-M/L-ficolin antibody and verified by flow cytometric analysis the presence of ficolin on the surface of peripheral blood monocytes [16].
  • By using ficolin B-specific antibodies and confocal microscopy, we show that ficolin B is expressed within mouse peritoneal exudate macrophages and is co-localized with Lamp-1, a marker for lysosomes and late endosomes [17].

Associations of FCN2 with chemical compounds

  • MASPs that were complexed with ficolin/P35 exhibited proteolytic activities against complement components C4, C2, and C3 [10].
  • Characterization of the interaction between L-ficolin/p35 and mannan-binding lectin-associated serine proteases-1 and -2 [18].
  • FCN2 promoter polymorphisms were associated with marked changes in the Ficolin-2 serum concentration, whereas two polymorphisms clustered in the exon encoding the fibrinogen-like domain were associated with increased and decreased GlcNAc binding, respectively [7].
  • We conclude that binding of L-ficolin/MASP complexes to the CPS generates C3 convertase C4b2a, which deposits C3b on GBS [19].
  • The column was loaded in the presence of EDTA and high salt, and L-ficolin was eluted by decreasing the salt concentration [3].

Physical interactions of FCN2

  • Preincubation of the MASPs with soluble MBL inhibited subsequent binding to immobilized L-ficolin/P35 and, conversely, suggesting that these lectins compete with each other for binding to the MASPs in vivo [18].

Other interactions of FCN2

  • When H-ficolin preparations were bound to anti-H-ficolin Ab which had been coated on ELISA plates, they activated C4, although no C4 activation was noted when anti-MBL and anti-L-ficolin/P35 were used [20].
  • It has been reported recently that L-ficolin/P35 associates with mannan-binding lectin (MBL)-associated serine proteases (MASP-1 and -2) and MBL-associated protein 19 (MAp19) in serum and forms complexes able to activate complement [18].
  • We report here that ficolin/P35, a human serum ficolin, was found to copurify with MASPs and sMAP [10].
  • We previously cloned a novel human lectin, designated P35, with both collagen-like and fibrinogen-like domains [14].
  • The overall structure of P35 closely resembles those of two pig ficolins that are putative TGF-beta 1-binding proteins [14].

Analytical, diagnostic and therapeutic context of FCN2

  • Purified MBL and L-ficolin were associated with MBL-associated serine proteases-1 and -2 (MASPs) and small MBL-associated protein as determined by Western blot analysis [21].
  • As shown by surface plasmon resonance spectroscopy, it associated with both MBL (K(D) = 2.6 nM) and L-ficolin (K(D) = 7.2 nM) [22].
  • Northern blots of various human tissues showed that the major product of the 1.3-kilobase-long P35 transcript is expressed in liver [2].
  • Based on the selectivity of L-ficolin we developed a new purification procedure involving affinity chromatography on N-acetylcysteine-derivatized Sepharose [3].
  • SDS-PAGE analysis under reducing and non-reducing conditions revealed hucolin was a disulphide-linked complex of 35-kDa and 75-kDa subunits [23].


  1. L-ficolin specifically binds to lipoteichoic acid, a cell wall constituent of Gram-positive bacteria, and activates the lectin pathway of complement. Lynch, N.J., Roscher, S., Hartung, T., Morath, S., Matsushita, M., Maennel, D.N., Kuraya, M., Fujita, T., Schwaeble, W.J. J. Immunol. (2004) [Pubmed]
  2. A novel human serum lectin with collagen- and fibrinogen-like domains that functions as an opsonin. Matsushita, M., Endo, Y., Taira, S., Sato, Y., Fujita, T., Ichikawa, N., Nakata, M., Mizuochi, T. J. Biol. Chem. (1996) [Pubmed]
  3. L-ficolin is a pattern recognition molecule specific for acetyl groups. Krarup, A., Thiel, S., Hansen, A., Fujita, T., Jensenius, J.C. J. Biol. Chem. (2004) [Pubmed]
  4. Polyglutamine-expanded human huntingtin transgenes induce degeneration of Drosophila photoreceptor neurons. Jackson, G.R., Salecker, I., Dong, X., Yao, X., Arnheim, N., Faber, P.W., MacDonald, M.E., Zipursky, S.L. Neuron (1998) [Pubmed]
  5. Structural insights into the innate immune recognition specificities of L- and H-ficolins. Garlatti, V., Belloy, N., Martin, L., Lacroix, M., Matsushita, M., Endo, Y., Fujita, T., Fontecilla-Camps, J.C., Arlaud, G.J., Thielens, N.M., Gaboriaud, C. EMBO J. (2007) [Pubmed]
  6. The baculovirus antiapoptotic p35 gene also functions via an oxidant-dependent pathway. Sah, N.K., Taneja, T.K., Pathak, N., Begum, R., Athar, M., Hasnain, S.E. Proc. Natl. Acad. Sci. U.S.A. (1999) [Pubmed]
  7. Polymorphisms in the FCN2 gene determine serum variation and function of Ficolin-2. Hummelshoj, T., Munthe-Fog, L., Madsen, H.O., Fujita, T., Matsushita, M., Garred, P. Hum. Mol. Genet. (2005) [Pubmed]
  8. Opsonic function and concentration of human serum ficolin/P35. Taira, S., Kodama, N., Matsushita, M., Fujita, T. Fukushima journal of medical science. (2000) [Pubmed]
  9. Baculovirus P35 inhibits the glucocorticoid-mediated pathway of cell death. Robertson, N.M., Zangrilli, J., Fernandes-Alnemri, T., Friesen, P.D., Litwack, G., Alnemri, E.S. Cancer Res. (1997) [Pubmed]
  10. Cutting edge: complement-activating complex of ficolin and mannose-binding lectin-associated serine protease. Matsushita, M., Endo, Y., Fujita, T. J. Immunol. (2000) [Pubmed]
  11. Human M-ficolin is a secretory protein that activates the lectin complement pathway. Liu, Y., Endo, Y., Iwaki, D., Nakata, M., Matsushita, M., Wada, I., Inoue, K., Munakata, M., Fujita, T. J. Immunol. (2005) [Pubmed]
  12. 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]
  13. Single nucleotide polymorphisms of Ficolin 2 gene in Behçet's disease. Chen, X., Katoh, Y., Nakamura, K., Oyama, N., Kaneko, F., Endo, Y., Fujita, T., Nishida, T., Mizuki, N. J. Dermatol. Sci. (2006) [Pubmed]
  14. Cloning and characterization of the human lectin P35 gene and its related gene. Endo, Y., Sato, Y., Matsushita, M., Fujita, T. Genomics (1996) [Pubmed]
  15. P35, an opsonic lectin of the ficolin family, in human blood from neonates, normal adults, and recurrent miscarriage patients. Kilpatrick, D.C., Fujita, T., Matsushita, M. Immunol. Lett. (1999) [Pubmed]
  16. M-ficolin, an innate immune defence molecule, binds patterns of acetyl groups and activates complement. Frederiksen, P.D., Thiel, S., Larsen, C.B., Jensenius, J.C. Scand. J. Immunol. (2005) [Pubmed]
  17. Localization of the mouse defense lectin ficolin B in lysosomes of activated macrophages. Runza, V.L., Hehlgans, T., Echtenacher, B., Zähringer, U., Schwaeble, W.J., Männel, D.N. J. Endotoxin Res. (2006) [Pubmed]
  18. Characterization of the interaction between L-ficolin/p35 and mannan-binding lectin-associated serine proteases-1 and -2. Cseh, S., Vera, L., Matsushita, M., Fujita, T., Arlaud, G.J., Thielens, N.M. J. Immunol. (2002) [Pubmed]
  19. Role of L-ficolin/mannose-binding lectin-associated serine protease complexes in the opsonophagocytosis of type III group B streptococci. Aoyagi, Y., Adderson, E.E., Min, J.G., Matsushita, M., Fujita, T., Takahashi, S., Okuwaki, Y., Bohnsack, J.F. J. Immunol. (2005) [Pubmed]
  20. 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]
  21. Human mannose-binding lectin and L-ficolin function as specific pattern recognition proteins in the lectin activation pathway of complement. Ma, Y.G., Cho, M.Y., Zhao, M., Park, J.W., Matsushita, M., Fujita, T., Lee, B.L. J. Biol. Chem. (2004) [Pubmed]
  22. Characterization of recombinant mannan-binding lectin-associated serine protease (MASP)-3 suggests an activation mechanism different from that of MASP-1 and MASP-2. Zundel, S., Cseh, S., Lacroix, M., Dahl, M.R., Matsushita, M., Andrieu, J.P., Schwaeble, W.J., Jensenius, J.C., Fujita, T., Arlaud, G.J., Thielens, N.M. J. Immunol. (2004) [Pubmed]
  23. Hucolin, a new corticosteroid-binding protein from human plasma with structural similarities to ficolins, transforming growth factor-beta 1-binding proteins. Edgar, P.F. FEBS Lett. (1995) [Pubmed]
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