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  • Title: Activation of the lectin complement pathway by ficolins.
    Author: Matsushita M, Endo Y, Hamasaki N, Fujita T.
    Journal: Int Immunopharmacol; 2001 Mar; 1(3):359-63. PubMed ID: 11367522.
    Abstract:
    Mannose-binding lectin (MBL), a serum lectin specific for mannose or N-acetylglucosamine (GlcNAc), which contains both a collagen-like domain and a carbohydrate-recognition domain (CRD), plays a role in innate immunity by acting as an opsonin and activating complement in association with MBL-associated serine protease (MASP) via the lectin pathway. Another type of GlcNAc-binding lectins termed "ficolins" exist in serum. They are characterized by the presence of both a collagen-like domain and a fibrinogen-like domain. Investigations of two types of human serum ficolins, ficolin/P35 and Hakata antigen, revealed that they are associated with MASPs and sMAP, a truncated protein of MASP-2, and activate complement. These findings indicate that, like MBL, serum ficolins are collagenous lectins capable of activating the lectin pathway and thus have a role in innate immunity.
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