PuSH - Publikationsserver des Helmholtz Zentrums München: Murine serine proteases MASP-1 and MASP-3, components of the lechtin pathway activation complex of complement, are encoded by a single structural gene.

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Stover, C.M.* ; Lynch, N.J.* ; Dahl, M.R.* ; Hanson, S.* ; Takahashi, M.* ; Frankenberger, M. ; Ziegler-Heitbrock, L. ; Eperon, I.* ; Thiel, S.* ; Schwaeble, W.J.*

Murine serine proteases MASP-1 and MASP-3, components of the lechtin pathway activation complex of complement, are encoded by a single structural gene.

Genes Immun. 4, 374-384 (2003)

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Activation of the lectin pathway of complement is initiated by the binding to microbial carbohydrate structures of a multimolecular fluid-phase complex composed of a carbohydrate recognition subcomponent that associates with three specific serine proteases and an enzymatically inert protein of 19 kDa. The first carbohydrate recognition subcomponent of the lectin pathway identified was mannan-binding lectin (MBL), hence the serine proteases were named MBL-associated serine proteases (MASPs) and numbered according to the sequence of their discovery. Here we describe the primary structures of the two distinct serine proteases MASP-1 and MASP-3 in the rat (and of MASP-3 in the mouse), show their association with plasma MBL complexes, and demonstrate that in rat and mouse, as in man, MASP-1 and MASP-3 are encoded by a single structural gene. For both species, we present the genomic region and regulatory elements responsible for the processing of either MASP-1 or MASP-3 mRNA by alternative splicing/alternative polyadenylation. Furthermore, we demonstrate the evolutionary conservation of MASP-3 mRNA in cDNA transcripts from guinea pig, rabbit, pufferfish, and cow.

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