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.

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

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

Harvard

Skjoedt, M, Palarasah, Y, Munthe-fog, L, Jie Ma, Y, Weiss, G, Skjodt, K, Koch, C & Garred, P 2010, 'MBL-associated serine protease-3 circulates in high serum concentrations predominantly in complex with Ficolin-3 and regulates Ficolin-3 mediated complement activation', Immunobiology, vol. 215, no. 11, pp. 921-931. https://doi.org/10.1016/j.imbio.2009.10.006

APA

Skjoedt, M., Palarasah, Y., Munthe-fog, L., Jie Ma, Y., Weiss, G., Skjodt, K., Koch, C., & Garred, P. (2010). MBL-associated serine protease-3 circulates in high serum concentrations predominantly in complex with Ficolin-3 and regulates Ficolin-3 mediated complement activation. Immunobiology, 215(11), 921-931. https://doi.org/10.1016/j.imbio.2009.10.006

Vancouver

Skjoedt M, Palarasah Y, Munthe-fog L, Jie Ma Y, Weiss G, Skjodt K et al. MBL-associated serine protease-3 circulates in high serum concentrations predominantly in complex with Ficolin-3 and regulates Ficolin-3 mediated complement activation. Immunobiology. 2010 Nov 1;215(11):921-931. https://doi.org/10.1016/j.imbio.2009.10.006

Author

Skjoedt, Mikkel-ole ; Palarasah, Yaseelan ; Munthe-fog, Lea ; Jie Ma, Ying ; Weiss, Gudrun ; Skjodt, Karsten ; Koch, Claus ; Garred, Peter. / MBL-associated serine protease-3 circulates in high serum concentrations predominantly in complex with Ficolin-3 and regulates Ficolin-3 mediated complement activation. In: Immunobiology. 2010 ; Vol. 215, No. 11. pp. 921-931.

Bibtex

@article{494f7ae285be4432be9073f56aca13aa,

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 Skjoedt and Yaseelan Palarasah and Lea Munthe-fog and {Jie Ma}, Ying and Gudrun Weiss and Karsten Skjodt and Claus Koch and Peter Garred",

year = "2010",

month = nov,

day = "1",

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

language = "English",

volume = "215",

pages = "921--931",

journal = "Immunobiology",

issn = "0171-2985",

publisher = "Urban und Fischer Verlag",

number = "11",

}

RIS

TY - JOUR

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

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

Department of Clinical Medicine