cDNA Cloning of a Mannose-Binding Lectin-Associated Serine Protease (MASP) Gene from Hagfish (Eptatretus burgeri)

Song, Liqiu; Takamune, Kazufumi; Sugawara, Yu; Fujii, Tamotsu

doi:10.2108/zsj.22.897

Cited by 6 publications

(1 citation statement)

References 57 publications

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“…It is, therefore, possible that lamprey MASP-1 is involved in C3 activation in the MBL-MASP complex and that MASP-A and MASP-B have other functions such as the activation of pro-factor D of the alternative pathway ( 20 ). The MASP-1 cDNA with TCN type was identified from hagfish ( 21 ). As with MBL, CL-L1, and CL-K1 belong to the collectin family, whose members contain both a collagen-like domain and a CRD ( 22 ).…”

Section: Mbl and Maspmentioning

confidence: 99%

The Complement System of Agnathans

Matsushita

2018

Front. Immunol.

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Agnathans (lamprey and hagfish) are a group of primitive jawless fish. Jawed vertebrates possess adaptive immunity including immunoglobulins, while agnathans lack immunoglobulins but have alternative adaptive immunity in which variable lymphocyte receptors (VLRs) function as antibodies. The complement system consists of many proteins involved in the elimination of pathogens. In mammals, it is activated via the three different pathways, resulting in the generation of C3b followed by the lytic pathway. Complement components including C3, mannose-binding lectin (MBL), and MBL-associated serine proteases (MASP) of the lectin pathway and factor B of the alternative pathway have been identified from lamprey and/or hagfish, while lytic pathway components have not been identified. In mammals, C1q binds to IgM/IgG-antigen complexes and activates the classical pathway in association with C1r and C1s. Lamprey also has C1q (LC1q), but its function differs from that of mammalian C1q. LC1q acts as a lectin and activates C3 in association with MASP via the lectin pathway. Furthermore, LC1q may interact with a secreted type of VLR (VLRB) in complex with antigens and mediate activation of C3, potentially via MASP, leading to cytolysis. Cytolysis is mediated by a newly identified serum protein named lamprey pore-forming protein (LPFP). In conclusion, lamprey has a complement activation pathway, which could be regarded as the classical pathway and also has a cytolytic system that is distinct from the mammalian lytic pathway. Thus, it appears that the complement system of agnathans is very unique and may have developed independently from jawed vertebrates.

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Section: Mbl and Maspmentioning

confidence: 99%

The Complement System of Agnathans

Matsushita

2018

Front. Immunol.

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Genomic view of the evolution of the complement system

2006

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The recent accumulation of genomic information of many representative animals has made it possible to trace the evolution of the complement system based on the presence or absence of each complement gene in the analyzed genomes. Genome information from a few mammals, chicken, clawed frog, a few bony fish, sea squirt, fruit fly, nematoda and sea anemone indicate that bony fish and higher vertebrates share practically the same set of complement genes. This suggests that most of the gene duplications that played an essential role in establishing the mammalian complement system had occurred by the time of the teleost/mammalian divergence around 500 million years ago (MYA). Members of most complement gene families are also present in ascidians, although they do not show a one-to-one correspondence to their counterparts in higher vertebrates, indicating that the gene duplications of each gene family occurred independently in vertebrates and ascidians. The C3 and factor B genes, but probably not the other complement genes, are present in the genome of the cnidaria and some protostomes, indicating that the origin of the central part of the complement system was established more than 1,000 MYA.

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Lamprey (Lethenteron japonicum) IL-17 upregulated by LPS-stimulation in the skin cells

2007

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We report here the first evidence for interleukin-17, a pro-inflammatory cytokine, in cyclostomes. To detect the novel molecules involved in the immune response in the skin of the lamprey Lethenteron japonicum, subtractive hybridization was performed with 6-h-cultured skin cells with or without lipopolysaccharide (LPS). In approximately 100 partially sequenced clones analyzed, we identified an interesting sequence similar to that of the IL-17 genes in teleosts and mammals. Subsequent rapid amplification of cDNA ends was used to obtain the cDNA of lamprey IL-17 (LampIL-17) that contains a 519-bp open reading frame encoding a mature protein of 154 amino acids and a 19-residue NH2-terminal signal peptide. The phylogenetic tree indicated that LampIL-17 is clustered into IL-17D, which is a subgroup of the IL-17 family. Southern blot analysis showed that the lamprey harbors a single copy of the LampIL-17 gene in its genome. The LampIL-17 gene was constitutively expressed in most tissues examined as well as in the skin, where the basal layer epithelial cells expressed LampIL-17 mRNA. Real-time-polymerase chain reaction (RT-PCR) demonstrated that the LampIL-17 gene expression in LPS-stimulated skin cells tended to be greater than that in non-stimulated cells. These results suggest that LampIL-17 is responsible for defense against bacterial infections in the lamprey skin.

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cDNA Cloning of a Mannose-Binding Lectin-Associated Serine Protease (MASP) Gene from Hagfish (Eptatretus burgeri)

Cited by 6 publications

References 57 publications

The Complement System of Agnathans

The Complement System of Agnathans

Genomic view of the evolution of the complement system

Lamprey (Lethenteron japonicum) IL-17 upregulated by LPS-stimulation in the skin cells

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