Abstract:
:TNFα converting enzyme (TACE) is responsible for converting membrane-anchored TNFα to its soluble form in mammalian. However, the function and characteristics of TACE in teleosts is unclear. In this study, we report the cloning of a cDNA sequence of the PaTACE from ayu, Plecoglossus altivelis. PaTACE encodes an 865-aa polypeptide, which is closest to the TACE gene found in pufferfish (Takifugu rubripes). PaTACE mRNA was detected in all the tissues tested, although it was considerably higher in liver, spleen, and brain tissues following infection with Listonella anguillarum. The recombinant region including the PaTACE catalytic domain was used to produce anti-PaTACE IgG. Western blot results revealed two bands for PaTACE from monocytes/macrophages. PNGase F digestion confirmed that the high molecular mass of PaTACE was caused by glycosylation. TACE activity in cell homogenates from ayu monocytes/macrophages increased following L. anguillarum infection. Moreover, PaTACE neutralization led to downregulation of TNFα expression in the supernatant of ayu monocyte/macrophages. Anti-PaTACE IgG also decreased respiratory burst in monocytes/macrophages. In conclusion, we report for the first time the TNFα-converting activity of TACE from a teleost. More investigation is needed to illustrate PaTACE-shedding activity in other immune regulators.
journal_name
Mol Immunoljournal_title
Molecular immunologyauthors
Lu XJ,Chen Q,Yang GJ,Chen Jdoi
10.1016/j.molimm.2014.10.010subject
Has Abstractpub_date
2015-02-01 00:00:00pages
497-504issue
2eissn
0161-5890issn
1872-9142pii
S0161-5890(14)00275-2journal_volume
63pub_type
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pub_type: 临床试验,杂志文章
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pub_type: 杂志文章,评审
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