Disease relevance of FCN1

• Indeed, M-ficolin bound to Staphylococcus aureus through GlcNAc [1].
• 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 [2].

High impact information on FCN1

• Both FCN1 and FCN2 contained polymorphisms in the promoters and structural parts of the genes, but only polymorphisms in FCN2 resulted in amino acid exchanges [3].
• For comparison, FCN1 and FCN3 were also investigated [3].
• The ficolin 1, 2 and 3 (derived from the FCN1, 2 and 3 genes, respectively) are homologous soluble pattern recognition molecules of importance for innate immunity, comprising collagen-like and fibrinogen-like domains, binding to sugar groups on different types of microorganisms [3].
• Trivalent Recognition Unit of Innate Immunity System: CRYSTAL STRUCTURE OF TRIMERIC HUMAN M-FICOLIN FIBRINOGEN-LIKE DOMAIN [4].
• M-ficolin-MASP complexes activated complement on N-acetylglucosamine (GlcNAc)-coated microplates in a C4 deposition assay [1].

Biological context of FCN1

• Human M-ficolin is a secretory protein that activates the lectin complement pathway [1].
• By flow cytometry, surface biotinylation and immunoprecipitation, we showed that M-ficolin was associated with the surface of promonocytic U937 cells [2].

Anatomical context of FCN1

• Another human ficolin, M-ficolin, is a nonserum ficolin that is expressed in leukocytes and lung; however, little is known about its physiologic roles [1].
• M-ficolin was localized in secretory granules in the cytoplasm of neutrophils, monocytes, and type II alveolar epithelial cells in lung [1].
• Less is known about M-ficolin, but it is thought to be present only on monocytes [5].
• M-ficolin transiently expressed in COS-7 cells was also clearly detected on the cell surface by immunoprecipitation [2].
• By flow cytometry, M-ficolin was detected on peripheral blood monocytes but not on lymphocytes or granulocytes [2].

Associations of FCN1 with chemical compounds

• M-ficolin bound to several neoglycoproteins bearing GlcNAc, N-acetylgalactosamine, and sialyl-N-acetyllactosamine, suggesting that M-ficolin can recognize the common carbohydrate residues found in microbes [1].
• In the present study, the FBG domain of M-ficolin was expressed and shown to bind to N-acetyl-D-glucosamine [2].
• Strain FCR-7/Kenya, isolated from a clinically chloroquine-resistant case, was more resistant to the drug in vitro than the two other strains (FCR-8/West Africa and FCN-1/Nigeria, both isolated from chloroquine-sensitive cases) [6].

Other interactions of FCN1

• Upon binding to M-ficolin ligands, the associated MASP-2 zymogen is activated and cleaves C4, thus triggering the complement system [5].

References