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Multiple functions of 2-Cys peroxiredoxins, I and II, and their regulations via post-translational modifications

Authors
 Sue Goo Rhee  ;  Hyun Ae Woo 
Citation
 FREE RADICAL BIOLOGY AND MEDICINE, Vol.152 : 107-115, 2020-05 
Journal Title
FREE RADICAL BIOLOGY AND MEDICINE
ISSN
 0891-5849 
Issue Date
2020-05
MeSH
Animals ; Cysteine* / metabolism ; Hydrogen Peroxide / metabolism ; Oxidation-Reduction ; Peroxiredoxins* / genetics ; Peroxiredoxins* / metabolism ; Protein Processing, Post-Translational
Keywords
Peroxiredoxin ; Peroxidase ; Chaperone ; 2 O 2 ) ; Intracellular messenger ; Thiol oxidation ; Phosphorylation ; Acetylation ; Glutathionylation ; S-Nitrosylation
Abstract
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.
Files in This Item:
T9992020336.pdf Download
DOI
10.1016/j.freeradbiomed.2020.02.028
Appears in Collections:
1. College of Medicine (의과대학) > BioMedical Science Institute (의생명과학부) > 1. Journal Papers
Yonsei Authors
Rhee, Sue Goo(이서구)
URI
https://ir.ymlib.yonsei.ac.kr/handle/22282913/190113
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