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 Skjødt; 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 Skjødt, Yaseelan Palarasah, Lea Munthe-Fog, Ying Jie Ma, Gudrun Weiss, Karsten Skjodt, Claus Koch, Peter Garred

Afdeling for Klinisk Immunologi

48 Citationer (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.

Originalsprog	Engelsk
Tidsskrift	Immunobiology
Vol/bind	215
Udgave nummer	11
Sider (fra-til)	921-31
Antal sider	11
ISSN	0171-2985
DOI	https://doi.org/10.1016/j.imbio.2009.10.006
Status	Udgivet - 1 nov. 2010

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10.1016/j.imbio.2009.10.006

Citationsformater

MBL-associated serine protease-3 circulates in high serum concentrations predominantly in complex with Ficolin-3 and regulates Ficolin-3 mediated complement activation. / Skjødt, Mikkel-Ole; Palarasah, Yaseelan; Munthe-Fog, Lea et al.
I: Immunobiology, Bind 215, Nr. 11, 01.11.2010, s. 921-31.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › peer review

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

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.",

author = "Mikkel-Ole Skj{\o}dt and Yaseelan Palarasah and Lea Munthe-Fog and Ma, {Ying Jie} and Gudrun Weiss and Karsten Skjodt and Claus Koch and Peter Garred",

year = "2010",

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doi = "10.1016/j.imbio.2009.10.006",

language = "English",

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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 - Skjødt, Mikkel-Ole

AU - Palarasah, Yaseelan

AU - Munthe-Fog, Lea

AU - Ma, Ying Jie

AU - Weiss, Gudrun

AU - Skjodt, Karsten

AU - Koch, Claus

AU - Garred, Peter

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

SN - 0171-2985

VL - 215

SP - 921

EP - 931

JO - Immunobiology

JF - Immunobiology

IS - 11

ER -

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

Abstract

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