Abstract
The broad-spectrum protease inhibitor alpha-2-macroglobulin (α2M) is widely found in vertebrates and invertebrates. However, no research regarding α2M has been described in sea cucumbers to date. In this study, the first sea cucumber α2M named Stmα2M was identified from Stichopus monotuberculatus, a tropical species with high edible and economic values in Southern China. The Stmα2M cDNA is 5276 bp in length, containing a 5′-untranslated region (UTR) of 279 bp, a 3′-UTR of 344 bp and an open reading frame of 4653 bp that encodes a protein of 1550 amino acids. The Stmα2M possesses all the three characteristics of known α2M proteins, including the bait region domain, thioester domain and receptor-binding domain. Higher levels of mRNA expression were noticed in intestine, respiratory tree, coelomocytes and tentacle of S. monotuberculatus. Transcriptional expression of Stmα2M showed the strongest response to lipopolysaccharides (LPS, 8.19-fold up-regulation) after 6 h post-challenge in coelomocytes. In addition, the α2M activity was detected in S. monotuberculatus and protein activity of α2M increased remarkably at 6 h after LPS stimulation. As a whole, this study indicated that Stmα2M is an important immune-related molecule, and the study on functions of Stmα2M may provide some new and valuable ideas for preventing and controlling diseases of cultured sea cucumbers.
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