Role of Peroxiredoxins in Protecting Against Cardiovascular and Related Disorders
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Role of Peroxiredoxins in Protecting Against Cardiovascular and Related Disorders Y. Robert Li1 · Hong Zhu2 · Igor Danelisen3
© Springer Science+Business Media, LLC, part of Springer Nature 2020
Abstract Peroxiredoxin (Prx) refers to a family of thiol-dependent peroxidases that decompose hydrogen peroxide, lipid hydroperoxides, as well as peroxynitrite, and protect against oxidative and inflammatory stress. There are six mammalian Prx isozymes (Prx1–6), classified as typical 2-Cys, atypical 2-Cys, or 1-Cys Prxs based on the mechanism and the number of cysteine residues involved during catalysis. In addition to their well-established peroxide-scavenging activity, some Prxs also participate in the regulation of various cell signaling pathways. Extensive animal studies employing primarily gene knockout models provide substantial evidence supporting a critical protective role of Prxs in various disease processes involving oxidative and inflammatory stress. This review surveys recent research findings, published primarily in influential journals, on the involvement of various Prx isozymes in protecting against cardiovascular injury and related disorders, including diabetes, metabolic syndromes, and sepsis, whose pathophysiology all intimately involves oxidative stress and inflammation. Keywords Cardiovascular disease · Diabetes · Inflammation · Metabolic syndrome · Oxidative stress · Peroxiredoxin · Sepsis Abbreviations ApoE Apolipoprotein E LPS Lipopolysaccharide PDGF Platelet-derived growth factor Prx Peroxiredoxin Trx Thioredoxin
Handling Editor: Kurt J. Varner. * Y. Robert Li [email protected] 1
Department of Pharmacology, Campbell University Jerry Wallace School of Osteopathic Medicine, Buies Creek, NC 27506, USA
2
Department of Physiology and Pathophysiology, Campbell University School of Osteopathic Medicine, Buies Creek, NC 27506, USA
3
Department of Medical Education, Tufts University School of Medicine, Boston, MA 02111, USA
Introduction Peroxiredoxin (Prx) is a term referring to a family of small nonseleno-peroxidases currently known to possess six mammalian isozymes, namely, Prx1–6. The first Prx was discovered by E.R. Stadtman and coworkers in 1988 in Saccharomyces cerevisae, where it protected the enzyme glutamine synthase from oxidation in a system that serendipitously included thiols to generate hydrogen peroxide (H2O2). The enzyme was first named thiol-specific antioxidant due to its dependence on thiols [1]. The name was then changed to thioredoxin peroxidase as the protein was found to be oxidized by H2O2 and reduced back by thioredoxin (Trx). Subsequent studies showed homologous proteins in other species that shared the peroxidase activity, and the term peroxiredoxin was introduced, which has been widely adopted in the literature. The six Prxs expressed in mammalian cells are classified into the following three subgroups: (1) Typical 2-Cys Prxs including Prx1–4; (2) Atypical 2-Cys Prx with Prx5 as the only member; and (3) 1-Cys Prx with Prx6 as the only member. Prx isozymes
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