Reactome | Ficolin-1 binds to molecular patterns on the target cell surface

Ficolin-1 binds to molecular patterns on the target cell surface

Stable Identifier

R-HSA-2855125

Type

Reaction

Species

Homo sapiens

Compartment

extracellular region, plasma membrane

Locations in the PathwayBrowser

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Immune System (Homo sapiens)

- Innate Immune System (Homo sapiens)
  - Complement cascade (Homo sapiens)
    - Initial triggering of complement (Homo sapiens)
      - Creation of C4 and C2 activators (Homo sapiens)
        
        Lectin pathway of complement activation (Homo sapiens)
        
        Ficolins bind to repetitive carbohydrate structures on the target cell surface (Homo sapiens)
        
        Ficolin-1 binds to molecular patterns on the target cell surface (Homo sapiens)

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Ficolin-1 binds to molecular patterns on the target cell surface

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Ficolin-1 (M-ficolin or FCN1) was shown to localize at the cell surface of circulating monocytes and granulocytes, despite lacking an obvious transmembrane domain, (Teh C et al. 2000; Honore C et al. 2010). Ficolin-1 has also been found in human plasma (Honore C et al. 2008; Wittenborn T et al. 2010; Kjaer TR et al. 2011). Monocytes and macrophages, but not immature dendritic cells were reported to secrete Ficolin-1 into the serum (Honore C et al. 2010). Moreover, early studies revealed its presence in secretory granules of peripheral blood monocytes and granulocytes (Liu Y et al. 2005). Soluble Ficolin-1 was found to form a complex with MASP2, while cell surface-bound Ficolin-1 did not associate with MASP (Honore C et al. 2010; Kjaer TR et al. 2011).

Ficolin-1 specifically recognizes sialic acid and can bind to acetylated compounds such as N-acetylglucosamine (GlcNAc) and N-acetylgalactosamine (GalNAc) (Garlatti V et al. 2007; Gout E et al. 2010; Kjaer TR et al. 2011).

Literature References

PubMed ID	Title	Journal	Year
20375634	Characteristics and biological variations of M-ficolin, a pattern recognition molecule, in plasma Wittenborn, T, Nielsen, HJ, Jensen, L, Jensenius, JC, Thiel, S	J Innate Immun	2010
17897951	Structural basis for innate immune sensing by M-ficolin and its control by a pH-dependent conformational switch Reiser, JB, Martin, L, Thielens, NM, Garlatti, V, Gaboriaud, C, Arlaud, GJ, Gout, E, Fujita, T	J. Biol. Chem.	2007
20032467	Carbohydrate recognition properties of human ficolins: glycan array screening reveals the sialic acid binding specificity of M-ficolin Martin, L, Arlaud, GJ, Dumestre-Pérard, C, Garlatti, V, Lacroix, M, Gaboriaud, C, Cesbron, JY, Thielens, NM, Lunardi, T, Smith, DF, Gout, E	J Biol Chem	2010
16116205	Human M-ficolin is a secretory protein that activates the lectin complement pathway Endo, Y, Nakata, M, Wada, I, Matsushita, M, Munakata, M, Liu, Y, Inoue, K, Fujita, T, Iwaki, D	J. Immunol.	2005
11012776	M-ficolin is expressed on monocytes and is a lectin binding to N-acetyl-D-glucosamine and mediates monocyte adhesion and phagocytosis of Escherichia coli Le, Y, Lu, J, Teh, C, Lee, SH	Immunology	2000
20400674	Tethering of Ficolin-1 to cell surfaces through recognition of sialic acid by the fibrinogen-like domain Rørvig, S, Honoré, C, Borregaard, N, Garred, P, Hummelshøj, T, Skjoedt, MO	J. Leukoc. Biol.	2010
21730084	Investigations on the pattern recognition molecule M-ficolin: quantitative aspects of bacterial binding and leukocyte association Sørensen, UB, Hansen, AG, Nielsen, O, Kjaer, TR, Jensenius, JC, Thiel, S	J. Leukoc. Biol.	2011
18343499	The innate pattern recognition molecule Ficolin-1 is secreted by monocytes/macrophages and is circulating in human plasma Rørvig, S, Madsen, HO, Honoré, C, Borregaard, N, Garred, P, Hummelshøj, T, Munthe-Fog, L	Mol. Immunol.	2008