Abstract
Mannan-binding lectin (MBL) forms a multimolecular complex with at least two MBL-associated serine proteases, MASP-1 and MASP-2. This complex initiates the MBL pathway of complement activation by binding to carbohydrate structures present on bacteria, yeast, and viruses. MASP-1 and MASP-2 are composed of modular structural motifs similar to those of the C1q-associated serine proteases C1r and C1s. Another protein of 19 kDa with the same N-terminal sequence as the 76-kDa MASP-2 protein is consistently detected as part of the MBL/MASP complex. In this study, we present the primary structure of this novel MBL-associated plasma protein of 19 kDa, MAp19, and demonstrate that MAp19 and MASP-2 are encoded by two different mRNA species generated by alternative splicing/polyadenylation from one structural gene.
| Original language | English |
|---|---|
| Journal | Journal of Immunology |
| Volume | 162 |
| Issue | 6 |
| Pages (from-to) | 3481-90 |
| Number of pages | 10 |
| ISSN | 0022-1767 |
| Publication status | Published - 1999 |
Keywords
- Alternative Splicing
- Amino Acid Sequence
- Animals
- Base Sequence
- Blood Proteins
- Carrier Proteins
- Collectins
- Complement Activation
- Exons
- Genes
- Humans
- Introns
- Lectins
- Mannans
- Mannose-Binding Protein-Associated Serine Proteases
- Molecular Sequence Data
- Molecular Weight
- RNA, Messenger
- Rats
- Sequence Analysis, DNA
- Serine Endopeptidases
- Transcription, Genetic