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Journal of Biomedicine and Biotechnology
Volume 2012 (2012), Article ID 138797, 10 pages
Review Article

Human L-Ficolin (Ficolin-2) and Its Clinical Significance

1Scottish National Blood Transfusion Service, National Science Laboratory, Ellen’s Glen Road, Edinburgh EH17 7QT, UK
2MRC Centre for Inflammation Research, University of Edinburgh, 47 Little France Crescent, Edinburgh EH16 4TJ, UK

Received 15 September 2011; Accepted 14 November 2011

Academic Editor: Misao Matsushita

Copyright © 2012 David C. Kilpatrick and James D. Chalmers. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.


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.