title: Human L-ficolin (ficolin-2) and its clinical significance.
abstract: Human L-ficolin (P35, ficolin-2) is synthesised in the liver and secreted into the bloodstream where it is one of the major pattern recognition molecules of plasma/serum. Like other ficolins, it consists of a collagen-like tail region linked to a fibrinogen-related globular head; a basic triplet subunit arises via a collagen-like triple helix, and this then forms higher multimers (typically a 12-mer, Mr 400K). Unlike other ficolins, it has a complex set of binding sites arranged within an internal cleft enabling it to recognise a variety of molecular patterns including acetylated sugars and certain 1,3-β-glucans. It is one of the few molecules known to activate the lectin pathway of complement. Recently, some disease association studies (at either the DNA or protein level) have implicated L-ficolin in innate immunity, where it might cooperate with pentraxins and collectins. Emerging lines of evidence point to a role for L-ficolin in respiratory immunity, where its affinity for Pseudomonas aeruginosa could be significant.
authors.affiliation: Scottish National Blood Transfusion Service, National Science Laboratory, Edinburgh, UK. david.kilpatrick@nhs.net
authors.forename: David C
authors.initials: DC
authors.lastname: Kilpatrick
authors.forename: James D
authors.initials: JD
authors.lastname: Chalmers
mesh_terms: D000818:Animals; D006801:Humans; D037102:Lectins / Q000097:blood / Q000737:chemistry* / Q000378:metabolism*; D000097604:Ficolins
chemical_list: D037102:Lectins; D000097604:Ficolins