Levels of mannan-binding lectin-associated serine protease-2 in healthy individuals.
The lectin pathway is part of the innate immune system providing a first line of defence against infections. Mannan-binding lectin (MBL) and ficolins, in complex with MBL-associated serine proteases (MASPs), are capable of activating the complement system, thus mediating the destruction of infectious agents. MASP-2 cleaves C4 and C2 and is thus crucial for the activation of downstream complement components. We present an assay for quantifying total MASP-2 in plasma and serum samples. The assay is a sandwich type assay using a combination of two monoclonal anti-MASP-2 antibodies, one directed against the N-terminal part of MASP-2 and the other against its C-terminal part. Based on a population of Danish blood donors, the average MASP-2 concentration was estimated at 534 (S.D.+/-213) ng per ml of plasma. Characterization of the MASP-2 protein in serum showed high stability at 4 degrees C and at ambient temperature but a rapid decline at 37 degrees C. Gel permeation chromatography (GPC) indicated that all MASP-2 in serum is present in complexes with MBL and ficolins.
Møller-Kristensen
Mette
M
Department of Medical Microbiology and Immunology, University of Aarhus, Aarhus C 8000, Denmark. mmk@microbiology.au.dk
Jensenius
Jens Chr
JC
Jensen
Lisbeth
L
Thielens
Nicole
N
Rossi
Véronique
V
Arlaud
Gerard
G
Thiel
Steffen
S
D000818:Animals; D002850:Chromatography, Gel; D005260:Female; D006801:Humans; D007118:Immunoassay; D050606:Mannose-Binding Protein-Associated Serine Proteases; D051381:Rats; D017208:Rats, Wistar; D012697:Serine Endopeptidases / Q000097:blood*
C105296:MASP2 protein, human; D050606:Mannose-Binding Protein-Associated Serine Proteases; D012697:Serine Endopeptidases