A novel murine complement-related gene encoding a C1r-like serum protein
| Autor: | John E. Volanakis, Gérard Garnier, Antonella Circolo |
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| Rok vydání: | 2003 |
| Předmět: |
Lipopolysaccharides
Proteases TMPRSS6 DNA Complementary Molecular Sequence Data Immunology Biology Mice Open Reading Frames Classical complement pathway Gene Duplication Sequence Homology Nucleic Acid Complementary DNA Chlorocebus aethiops Gene duplication Animals Humans Amino Acid Sequence RNA Messenger Molecular Biology Gene Sequence Deletion Serine protease Sequence Homology Amino Acid Complement C1r Serine Endopeptidases Chromosome Mapping Blood Proteins Exons Molecular biology Introns Protein Structure Tertiary Open reading frame Genes Liver Multigene Family COS Cells biology.protein Sequence Alignment |
| Zdroj: | Molecular Immunology. 39:899-906 |
| ISSN: | 0161-5890 |
| DOI: | 10.1016/s0161-5890(02)00283-3 |
| Popis: | C1r and C1s are highly specific serine proteases that initiate the classical pathway of complement activation. We recently demonstrated that, in the mouse, the genes encoding these proteins are duplicated. Analysis of the 5'-flanking region of the murine C1rA gene, the homologue of human C1r, revealed the presence of a novel gene encoding a C1r-like protein (c1r-LP). Although this gene carries a large deletion, it shows an overall structure similar to that of c1rA, suggesting that it may have arisen from a duplication of the C1r gene. The c1r-LP gene is expressed primarily in the liver, and is not regulated by lipopolysaccharide. The open reading frame of full-length cDNA clones encodes a pre-protein with a calculated molecular mass of 50.6 kDa which, except for an internal deletion of several modules, has a modular organization similar to that of C1r and shows 51% overall amino acid identity to corresponding regions of C1rA. Western blot analysis demonstrates the presence of C1r-LP in mouse serum. The serine protease domain of C1r-LP displays 60% amino acid residue identity to that of C1rA, however, certain atypical features of the active center, and primarily the absence of the activation/cleavage site, suggest that C1r-LP is either an atypical enzyme, or it lacks proteolytic activity, perhaps serving a regulatory function in the classical pathway. |
| Databáze: | OpenAIRE |
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