Abstract
Thioredoxin-2 (Trx2) is a mitochondrial protein using a dithiol active site to reduce protein disulfides. In addition to the cytoprotective function of this enzyme, several studies have highlighted the implication of Trx2 in cellular signaling events. In particular, growing evidence points to such roles of redox enzymes in developmental processes taking place in the central nervous system. Here, we investigate the potential implication of Trx2 in embryonic development of chick spinal cord. To this end, we first studied the distribution of the enzyme in this tissue and report strong expression of Trx2 in chick embryo post-mitotic neurons at E4.5 and in motor neurons at E6.5. Using in ovo electroporation, we go on to highlight a cytoprotective effect of Trx2 on the programmed cell death (PCD) of neurons during spinal cord development and in a novel cultured spinal cord explant model. These findings suggest an implication of Trx2 in the modulation of developmental PCD of neurons during embryonic development of the spinal cord, possibly through redox regulation mechanisms.
Highlights
Reactive oxygen (ROS) and nitrogen species (RNS) are molecules generated by the cell in pathophysiological situations and as natural byproducts of their metabolism
Alignment of protein sequence predicted from the 642-bp chick Trx2 cDNA amplified in this work with human and mouse Trx2 NCBI reference sequences, accession numbers Q99757 and P97493, respectively, revealed important identity between amino acid sequences, in particular when omitting the predicted mitochondrial targeting sequence which displays a lower degree of conservation than the enzyme per se (Fig 2B)
We report the cloning of Gallus gallus Trx2 cDNA and considerable immunoreactivity associated to the enzyme in post-mitotic neurons at E4.5 as well as in motor neurons at E6.5 during chick embryonic spinal cord development
Summary
Reactive oxygen (ROS) and nitrogen species (RNS) are molecules generated by the cell in pathophysiological situations and as natural byproducts of their metabolism. These molecules can oxidize different cell components such as proteins, lipids or DNA, causing oxidative damage which can lead to cell death. Trxs use two reactive cysteine residues located in a conserved WCGPC motive to accomplish their reduction cycles. These ubiquitous enzymes act as disulfide bond reductants and, notably, serve as the main reductant for ROS/RNS scavengers peroxiredoxins (Prdxs).
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