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The Rat and Mouse Homologues of MASP-2 and MAp19, components of the Lectin Activation Pathway of Complement^{1 ,2 ,3}

Cordula M. Stover^*, Steffen Thiel, Nicholas J. Lynch and Wilhelm J. Schwaeble^4,*,

^* Department of Microbiology and Immunology, University of Leicester, Leicester, United Kingdom; Department of Medical Microbiology and Immunology, University of Aarhus, Aarhus, Denmark; and Institute for Anatomy and Cell Biology, University of Marburg, Marburg, Germany

Recently, we described two novel constituents of the multimolecular initiation complex of the mannan-binding lectin (MBL) pathway of complement activation, a serine protease of 76 kDa, termed MASP-2, and a MASP-2 related plasma protein of 19 kDa, termed MAp19. Upon activation of the MBL/MASPs/MAp19 complex, MASP-2 cleaves the fourth complement component C4, while the role of MAp19 within the MBL/MASP-1/MASP-2/MAp19 complex remains to be clarified. In humans, the mRNA species encoding MASP-2 (2.6 kb) and MAp19 (1.0 kb) arise by an alternative polyadenylation/splicing mechanism from a single structural MASP-2 gene. Here, we report the complete primary structures of the rat homologue of MASP-2 and of rat and mouse MAp19. We show that both MASP-2 and MAp19 are part of the rat MBL pathway activation complex and demonstrate their exclusively hepatic biosynthesis. Southern blot and PCR analyses of rat genomic DNA indicate that as in humans, rat MASP-2 and MAp19 are encoded by a single structural gene.

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