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Two constituents of the initiation complex of the mannan-binding lectin activation pathway of complement are encoded by a single structural gene

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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 languageEnglish
JournalJournal of Immunology
Pages (from-to)3481-90
Number of pages10
Publication statusPublished - 1999

    Research areas

  • 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

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