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Jens Christian Jensenius

MASP-3 and its association with distinct complexes of the mannan-binding lectin complement activation pathway

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The mannan-binding lectin (MBL) pathway of complement activation is part of the innate immune defense. The binding of MBL to microbial carbohydrates activates the MBL-associated serine proteases (MASPs), which recruit the complement factors, C4 and C2, to generate the C3 convertase or directly activate C3. We present a phylogenetically highly conserved member of the MBL complex, MASP-3, which is generated through alternative splicing of the MASP-1/3 gene. The designation of MASP-3 as a protease is based on homology to known MASPs. Different MBL oligomers were found to have distinct MASP composition and biological activities. MASP-1, MAp19, and direct C3-cleaving activity are associated with smaller oligomers whereas MASP-3 is found together with MASP-2 on larger oligomers. MASP-3 downregulate the C4 and C2 cleaving activity of MASP-2.
Original languageEnglish
Pages (from-to)127-35
Number of pages9
Publication statusPublished - 2001

    Research areas

  • Alternative Splicing, Amino Acid Sequence, Carrier Proteins, Cloning, Molecular, Collectins, Complement Activation, Humans, Mannose-Binding Protein-Associated Serine Proteases, Molecular Sequence Data, Serine Endopeptidases

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