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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Alternative Splicing
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Amino Acid Sequence
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Animals
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Base Sequence
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Blood Proteins / chemistry
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Carrier Proteins / chemistry
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Carrier Proteins / genetics*
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Carrier Proteins / immunology*
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Collectins
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Complement Activation / genetics*
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Exons
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Genes / immunology*
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Humans
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Introns
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Lectins / metabolism*
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Mannans / metabolism*
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Mannose-Binding Protein-Associated Serine Proteases
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Molecular Sequence Data
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Molecular Weight
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RNA, Messenger / chemistry
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Rats
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Sequence Analysis, DNA
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Serine Endopeptidases / chemistry
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Serine Endopeptidases / genetics*
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Serine Endopeptidases / immunology
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Transcription, Genetic / immunology
Substances
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Blood Proteins
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Carrier Proteins
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Collectins
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Lectins
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Mannans
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RNA, Messenger
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MASP2 protein, human
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Mannose-Binding Protein-Associated Serine Proteases
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Serine Endopeptidases
Associated data
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GENBANK/Y18281
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GENBANK/Y18282
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GENBANK/Y18283
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GENBANK/Y18284
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GENBANK/Y18285
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GENBANK/Y18286
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GENBANK/Y18287