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

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