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J Biomed Biotechnol. 2012;2012:138797. doi: 10.1155/2012/138797. Epub 2012 Feb 28.

Human L-ficolin (ficolin-2) and its clinical significance.

Author information

1
Scottish National Blood Transfusion Service, National Science Laboratory, Edinburgh, UK. david.kilpatrick@nhs.net

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.

PMID:
22500076
PMCID:
PMC3303570
DOI:
10.1155/2012/138797
[Indexed for MEDLINE]
Free PMC Article

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