7. Conclusions
Ficolins are proteins that consist mainly of two domains: an N-terminal collagen- like domain and a C-terminal fibrinogen-like domain. This domain structure is related to MBL or C1q, a subcomponent of the complement C1 complex in having a collagenous stalk. Like MBL and C1q, the ficolin monomer assembles the multimeric form via the trimers. Accumulating data indicate that one of the most important functions of ficolin is to bind carbohydrates, which are responsible for the fibrinogen-like domain. The carbohydrate specificities have suggested that ficolin is able to distinguish between pathogens and self. Indeed, ficolin binds to certain kinds of bacteria through its lectin activity. Interestingly, like MBL, some of the ficolins form complexes with MASPs and the complexes can activate complements through the lectin pathway. All these results suggest that ficolin functions to eliminate the non-self in innate immunity as a recognition molecule.
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Endo, Y., Liu, Y., Fujita, T. (2006). Structure and Function of Ficolins. In: Lambris, J.D. (eds) Current Topics in Complement. Advances in Experimental Medicine and Biology, vol 586. Springer, Boston, MA. https://doi.org/10.1007/0-387-34134-X_18
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