Peroxiredoxin (PRx) exhibits thioredoxin-dependent peroxidase activity and constitutes a family of proteins. Four members of genes from rat tissues were isolated by PCR using degenerated primers based on the sequences which encode a pair of highly conserved Cys-containing domains, and were then cloned to full-length cDNAs. These included two genes which have previously been isolated in rats, PRx I and PRx II, and two rat homologues of PRx III and PRx IV. We showed, for the first time, the simultaneous expression of all four genes in various rat tissues by Northern blotting. Since a discrepancy exists regarding cellular distribution, we further characterized PRx IV by expressing it in COS-1 cells. This clearly demonstrates that PRx IV is a secretory form and functions within the extracellular space. Copyright (C) 1999 Federation of European Biochemical Societies.
Matsumoto, A., Okado, A., Fujii, T., Fujii, J., Egashira, M., Niikawa, N., & Taniguchi, N. (1999). Cloning of the peroxiredoxin gene family in rats and characterization of the fourth member. FEBS Letters, 443(3), 246–250. https://doi.org/10.1016/S0014-5793(98)01736-0