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

Mikkel-ole Skjoedt; Yaseelan Palarasah; Lea Munthe-fog; Ying Jie Ma; Gudrun Weiss; Karsten Skjodt; Claus Koch; Peter Garred

doi:10.1016/j.imbio.2009.10.006

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

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

Research output: Contribution to journal › Journal article › Research › peer-review

48 Citations (Scopus)

Abstract

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.

Original language	English
Journal	Immunobiology
Volume	215
Issue number	11
Pages (from-to)	921-931
ISSN	0171-2985
DOIs	https://doi.org/10.1016/j.imbio.2009.10.006
Publication status	Published - 1 Nov 2010

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10.1016/j.imbio.2009.10.006

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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.

In: Immunobiology, Vol. 215, No. 11, 01.11.2010, p. 921-931.

Research output: Contribution to journal › Journal article › Research › peer-review

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abstract = "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.",

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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

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DO - 10.1016/j.imbio.2009.10.006

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JO - Immunobiology

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