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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MBL-associated serine protease-3 circulates in high serum concentrations predominantly in complex with Ficolin-3 and regulates Ficolin-3 mediated complement activation. / Skjoedt, Mikkel-ole; Palarasah, Yaseelan; Munthe-fog, Lea; Jie Ma, Ying; Weiss, Gudrun; Skjodt, Karsten; Koch, Claus; Garred, Peter.
I: Immunobiology, Bind 215, Nr. 11, 01.11.2010, s. 921-931.Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt
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T1 - MBL-associated serine protease-3 circulates in high serum concentrations predominantly in complex with Ficolin-3 and regulates Ficolin-3 mediated complement activation
AU - Skjoedt, Mikkel-ole
AU - Palarasah, Yaseelan
AU - Munthe-fog, Lea
AU - Jie Ma, Ying
AU - Weiss, Gudrun
AU - Skjodt, Karsten
AU - Koch, Claus
AU - Garred, Peter
N1 - Copyright © 2009 Elsevier GmbH. All rights reserved.
PY - 2010/11/1
Y1 - 2010/11/1
N2 - 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.
AB - 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.
U2 - 10.1016/j.imbio.2009.10.006
DO - 10.1016/j.imbio.2009.10.006
M3 - Journal article
C2 - 19939495
VL - 215
SP - 921
EP - 931
JO - Immunobiology
JF - Immunobiology
SN - 0171-2985
IS - 11
ER -
ID: 32319788