Multiple functions of 2-Cys peroxiredoxins, I and II, and their regulations via post -translational modifications
- 주제(키워드) Peroxiredoxin , Peroxidase , Chaperone , 2 O 2 ) , Intracellular messenger , Thiol oxidation , Phosphorylation , Acetylation , Glutathionylation , S-Nitrosylation
- 주제(기타) Biochemistry & Molecular Biology
- 주제(기타) Endocrinology & Metabolism
- 설명문(일반) [Rhee, Sue Goo] Yonsei Univ, Yonsei Biomed Res Inst, Coll Med, Seoul 120749, South Korea; [Rhee, Sue Goo] NHLBI, Biochem & Biophys Ctr, NIH, Bldg 10, Bethesda, MD 20892 USA; [Woo, Hyun Ae] Ewha Womans Univ, Coll Pharm, Seoul 120750, South Korea; [Woo, Hyun Ae] Ewha Womans Univ, Coll Nat Sci, Seoul 120750, South Korea
- 등재 SCIE, SCOPUS
- OA유형 hybrid
- 발행기관 ELSEVIER SCIENCE INC
- 발행년도 2020
- 총서유형 Journal
- URI http://www.dcollection.net/handler/ewha/000000168922
- 본문언어 영어
- PubMed https://pubmed.ncbi.nlm.nih.gov/32151745
초록/요약
Peroxiredoxins (Prxs) are an unusual family of thiol-specific peroxidases that possess a binding site for H 2 O 2 and rely on a conserved cysteine residue for rapid reaction with H 2 O 2 . Among 6 mammalian isoforms (Prx I to VI), Prx I and Prx II are mainly found in the cytosol and nucleus. Prx I and Prx II function as antioxidant enzymes and protein chaperone under oxidative distress conditions. Under oxidative eustress conditions, Prx I and Prx II regulate the levels of H 2 O 2 at specific area of the cells as well as sense and transduce H 2 O 2 signaling to target proteins. Prx I and Prx II are known to be covalently modified on multiple sites: Prx I is hyperoxidized on Cys 52 ; phosphorylated on Ser 32 , Thr 90 , and Tyr 194 ; acetylated on Lys 7 , Lys 16 , Lys 27 , Lys 35 , and Lys 197 ; glutathionylated on Cys 52 , Cys 83 , and Cys 173 ; and nitrosylated on Cys 52 and Cys 83 , whereas Prx II is hyperoxidized on Cys 51 ; phosphorylated on Thr 89 , Ser 112 , and Thr 182 ; acetylated on Ala 2 and Lys 196 ; glutathionylated on Cys 51 and Cys 172 ; and nitrosylated on Cys 51 and Cys 172 . In this review, we describe how these post -translational mod- ifications affect various functions of Prx I and Prx II.
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