Tethering of Ficolin-1 to cell surfaces through recognition of sialic acid by the fibrinogen-like domain

Christian Le Fèvre Honoré, Sara Rørvig, Tina Hummelshøj Glue, Mikkel-Ole Skjoedt, Niels Borregaard, Peter Garred

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningpeer review

Abstrakt

Three Ficolins have been identified in humans: Ficolin-1 (M-Ficolin), Ficolin-2 (L-Ficolin), and Ficolin-3 (H-Ficolin). Ficolin-1 is the least-described of the Ficolins and is expressed by monocytes, granulocytes, and in the lungs. Ficolin-1 is found circulating at low concentrations in serum but is regarded primarily as a secretory molecule that exerts its function locally in inflamed tissues. Ficolin-1 has been reported on the surface of monocytes and granulocytes and was suggested originally to function as a phagocytic receptor. However, the molecule does not contain any obvious transmembrane domain, and no binding partners have been identified. To gain further insight in the physiological role of Ficolin-1, we sought to identify the molecular mechanism responsible for the membrane association of Ficolin-1 to monocytes and granulocytes. We demonstrate that expression of Ficolin-1 on the cell surface is restricted to monocytes and granulocytes. Ficolin-1 is tethered to the cell surface of these cells through its fibrinogen-like domain, and the ligand involved in the binding of Ficolin-1 is shown to be sialic acid. Moreover, rFicolin-1 bound activated but not resting T lymphocytes. Together, these results demonstrate a novel self-recognition mechanism of leukocytes mediated by the fibrinogen-like domain of Ficolin-1.
OriginalsprogEngelsk
TidsskriftJournal of Leukocyte Biology
Vol/bind88
Udgave nummer1
Sider (fra-til)145-58
Antal sider14
ISSN0741-5400
DOI
StatusUdgivet - 1. jul. 2010

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