A truncated form of mannose-binding lectin-associated serine protease (MASP)-2 expressed by alternative polyadenylation is a component of the lectin complement pathway.

Abstract:

: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.

journal_name

Int Immunol

journal_title

International immunology

authors

Takahashi M,Endo Y,Fujita T,Matsushita M

doi

10.1093/intimm/11.5.859

subject

Has Abstract

pub_date

1999-05-01 00:00:00

pages

859-63

issue

5

eissn

0953-8178

issn

1460-2377

journal_volume

11

pub_type

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