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

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

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.

Publication types

  • Review

MeSH terms

  • Animals
  • Humans
  • Lectins / blood
  • Lectins / chemistry*
  • Lectins / metabolism*

Substances

  • Lectins
  • ficolin