Modulation of plasma protein expression in bullfrog (Rana catesbeiana) tadpoles during seasonal acclimatization and thermal acclimation.

Biological activities in ectothermic vertebrates depend to a great extent on ambient temperature. Adapting their biological systems to annual or short-term alterations in temperature may play an important role in thermal resistance or overwintering survival. Using SDS-PAGE and western blot, we examined plasma proteins in bullfrog (Rana catesbeiana) tadpoles that were seasonally acclimatized (winter vs. summer) or thermally acclimated (4 °C vs. 21 °C) and identified two season-responsive proteins. The first, transthyretin (TTR), is a plasma thyroid hormone distributor protein that was abundant in summer, and the second is a protein containing C-type lectin-like domain (CTLD) that was abundant in winter and cold acclimation of 4 weeks. Sequence analysis revealed that the C-terminal carbohydrate recognition domain of this CTLD protein (termed collectin X) was highly similar to those of the collectin family members, which participate in complement activation of the innate immune system; however, it lacked most of collagen-like domain. Among the hepatic genes involved in the thyroid system, ttr and dio3 were up-regulated, whereas thra and thrb were down-regulated, in summer acclimatization or warm acclimation. In contrast, the collectin X gene (colectx), as well as colect10 and colect11 in the collectin family involved in the innate immune system, were down-regulated during warm acclimation, although fcn2 in the ficolin family was up-regulated during summer acclimatization and warm acclimation. These findings indicate that seasonal acclimatization and thermal acclimation differentially affect some components of the thyroid and innate immune systems at protein and transcript levels.

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Declaration of Competing Interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.