A truncated form of mannose-binding lectin-associated serine protease (MASP)-2 expressed by alternative polyadenylation is a component of the lectin complement pathway.
Int Immunol
; 11(5): 859-63, 1999 May.
Article
en En
| MEDLINE
| ID: mdl-10330290
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.
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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Complemento C1
/
ARN Mensajero
/
Serina Endopeptidasas
/
Proteínas Portadoras
/
Lectinas
Tipo de estudio:
Risk_factors_studies
Límite:
Humans
Idioma:
En
Revista:
Int Immunol
Asunto de la revista:
ALERGIA E IMUNOLOGIA
Año:
1999
Tipo del documento:
Article
País de afiliación:
Japón