International Immunology, Vol. 11, No. 5, 859-863,
May 1999
© 1999 Japanese Society for Immunology
A truncated form of mannose-binding lectin-associated serine protease (MASP)-2 expressed by alternative polyadenylation is a component of the lectin complement pathway
Department of Biochemistry, Fukushima Medical University School of Medicine, 1 Hikarigaoka, Fukushima 960-1295, Japan
Correspondence to: M. Matsushita
The lectin complement pathway is initiated by binding of mannose-binding lectin (MBL) and MBL-associated serine protease (MASP) to carbohydrates. In the human lectin pathway, MASP-1 and MASP-2 are involved in the proteolysis of C4, C2 and C3. Here we report that the human MBL–MASP complex contains a new 22 kDa protein [small MBL-associated protein (sMAP)] bound to MASP-1. Analysis of the nucleotide sequence of sMAP cDNA revealed that it is a truncated form of MASP-2, consisting of the first two domains (i.e. the first internal repeat and the epidermal growth factor-like domain) with four different C-terminal amino acids. sMAP mRNAs are expressed in liver by alternative polyadenylation of the MASP-2 gene, in which a sMAP-specific exon containing an in-frame stop codon and a polyadenylation signal is used. The involvement of sMAP in the MBL–MASP complex suggests that the activation mechanism of the lectin pathway is more complicated than that of the classical pathway.
Keywords: alternative polyadenylation, lectin complement pathway, MASP-2
Transmitting editor: K. Sugamura
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