Identification and Functional Analysis of Interleukin-1? in the Chinese Soft-Shelled Turtle Pelodiscus sinensis.

ABSTRACT: Chinese soft-shelled turtle (Pelodiscus sinensis) is commercially cultured in East and Southeast Asia for its nutritional and medicinal values. In this study, we identified interleukin-1? (IL-1?) from Chinese soft-shelled turtle. The full-length cDNA of Pelodiscus sinensis IL-1? (tIL-1?) consists of 1529 base pairs with an 831-base-pair open reading frame, encoding 277 amino acids. The guanine-cytosine (GC) content in the coding sequence and 3' untranslated region of tIL-1? is considerably higher than that of other vertebrates. Its mRNA expression level increased significantly during Aeromonas hydrophila infection. The tIL-1? lacks the typical IL-1?-converting enzyme (ICE) cut site found in mammalian IL-1?, but still could be cleaved by turtle caspase-1. By mutating the potential cleavage sites, we identified aspartic acid (Asp/D) 130 as the ICE cut site in tIL-1?. The peptide truncated at D130 was expressed using the baculovirus expression system; its bioactivity is confirmed by the ability to induce cyclooxygenase-2 (COX-2) and tIL-1? itself in peripheral blood monocytes. In conclusion, we characterized IL-1? from Chinese soft-shelled turtle and identified its D130 as a non-typical ICE cut size.

SUBMITTER: Liang Q 

PROVIDER: S-EPMC4880838 | biostudies-literature | 2016

REPOSITORIES: biostudies-literature