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Jens Christian Jensenius

The mannan-binding lectin-associated serine proteases (MASPs) and MAp19: four components of the lectin pathway activation complex encoded by two genes

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Mannan-binding lectin (MBL) and ficolins (L-ficolin and H-ficolin) initiate the lectin pathway of complement activation upon binding to microbial carbohydrates. The activation is mediated by associated serine proteases, termed MASPs, since they were discovered as MBL-associated serine proteases. The MASP family comprises three serine proteases, MASP-1, MASP-2 and MASP-3 and a non-enzymatic protein, MAp19. The MASPs show identical domain structure, shared also with C1r and C1s. MASP-1 and MASP-3 are alternative splice products of a single gene, MASP1/3, and have identical A chains, whereas they have individual B chains, encompassing the serine protease domain. MASP2 and MAp19 are alternative splice products of the MASP-2 gene, with MAp19 consisting of the first two domains of MASP-2 plus additional four amino acid residues. MASP-2 is the protease responsible for activating C4 and C2 to generate the C3 convertase, C4bC2b. The biological function of the remaining three proteins has not yet been resolved.
Original languageEnglish
JournalImmunobiology
Volume205
Issue4-5
Pages (from-to)455-66
Number of pages12
ISSN0171-2985
Publication statusPublished - 2002

    Research areas

  • Animals, Complement Activation, Complement Pathway, Mannose-Binding Lectin, Humans, Mannose-Binding Protein-Associated Serine Proteases, Phylogeny, Serine Endopeptidases

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