MBL-associated serine protease-3 circulates in high serum concentrations predominantly in complex with Ficolin-3 and regulates Ficolin-3 mediated complement activation

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningfagfællebedømt

Mikkel-Ole Skjoedt, Yaseelan Palarasah, Lea Munthe-Fog, Ying Jie Ma, Gudrun Weiss, Karsten Skjodt, Claus Koch, Peter Garred, Mikkel-Ole Skjoedt, Yaseelan Palarasah, Lea Munthe-Fog, Ying Jie Ma, Gudrun Weiss, Karsten Skjodt, Claus Koch, Peter Garred

The human lectin complement pathway (LCP) involves circulating complexes consisting of mannose-binding lectin (MBL) or ficolins in association with serine proteases named MASP-1, -2 and -3 and a non-enzymatic protein, sMAP. MASP-3 originates from the MASP1 gene through differential splicing and little is known about its biological characteristics. For this reason we expressed recombinant MASP-3 and generated specific monoclonal antibodies to establish biochemical characteristics and to determine the serum levels, the interactions with the LCP recognition molecules and the influence on complement activation of MASP-3.
OriginalsprogEngelsk
TidsskriftImmunobiology
Vol/bind215
Udgave nummer11
Sider (fra-til)921-31
Antal sider11
ISSN0171-2985
DOI
StatusUdgivet - 1 nov. 2010

ID: 32319788