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 [binding]

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