Abstract

Typical 2-Cys peroxiredoxins (2-Cys Prdxs) are proteins with antioxidant properties belonging to the thioredoxin peroxidase family. With their peroxidase activity, they contribute to the homeostatic control of reactive oxygen species (ROS) and, therefore, participate in various physiological functions, such as cell proliferation, differentiation, and apoptosis. Although Prdxs have been shown to be potential biomarkers for monitoring aquatic environments, minimal scientific attention has been devoted to describing their molecular architecture and function in marine invertebrates. Our study aims to clarify the protective role against stress induced by exposure to metals (Cu, Zn, and Cd) of three Prdxs (Prdx2, Prdx3, and Prdx4) in the solitary ascidian Ciona robusta, an invertebrate chordate. Here, we report a detailed pre- and post-translational regulation of the three Prdx isoforms. Data on intestinal mRNA expression, provided by qRT-PCR analyses, show a generalized increase for Prdx2, -3, and -4, which is correlated to metal accumulation. Furthermore, the increase in tissue enzyme activity observed after Zn exposure is slower than that observed with Cu and Cd. The obtained results increase our knowledge of the evolution of anti-stress proteins in invertebrates and emphasize the importance of the synthesis of Prdxs as an efficient way to face adverse environmental conditions.

Highlights

  • Received: 30 November 2021Industrial and mining activities, including the unwise use of pesticides, are considered the primary pollution sources of aquatic bodies

  • The gene is organized in four exons and three introns, with the ATG start codon located in the first exon, 114 nt long, and the TAA stop codon located in the last one, 278 nt long

  • Our data on the time course of the transcription levels and active proteins levels highlight that Cr-Prdx2, Cr-Prdx3, and Cr-Prdx4 perform their antioxidant function in an integrated way

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Summary

Introduction

Received: 30 November 2021Industrial and mining activities, including the unwise use of pesticides, are considered the primary pollution sources of aquatic bodies. Prdxs are thiol-specific antioxidant enzymes that have recently received significant attention for their role in stress responses, characterized by an imbalance between the reactive oxygen species (ROS) production rate and their removal from the cell. These proteins can modulate various physiological functions, such as cell proliferation, differentiation, and apoptosis, by decreasing peroxide levels and the risk of ROS-related damages [11,12].

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