Mostrar el registro sencillo del ítem
dc.contributor.author
Randall, Lía M.
dc.contributor.author
Dalla Rizza, Joaquín
dc.contributor.author
Parsonage, Derek
dc.contributor.author
Santos, Javier
![Se ha confirmado la validez de este valor de autoridad por un usuario](/themes/CONICETDigital/images/authority_control/invisible.gif)
dc.contributor.author
Mehl, Ryan A.
dc.contributor.author
Lowther, W. Todd
dc.contributor.author
Poole, Leslie B.
dc.contributor.author
Denicola, Ana
dc.date.available
2022-07-19T10:48:01Z
dc.date.issued
2019-09
dc.identifier.citation
Randall, Lía M.; Dalla Rizza, Joaquín; Parsonage, Derek; Santos, Javier; Mehl, Ryan A.; et al.; Unraveling the effects of peroxiredoxin 2 nitration; role of C-terminal tyrosine 193; Elsevier Science Inc.; Free Radical Biology and Medicine; 141; 9-2019; 492-501
dc.identifier.issn
0891-5849
dc.identifier.uri
http://hdl.handle.net/11336/162440
dc.description.abstract
Peroxiredoxins (Prx) are enzymes that efficiently reduce hydroperoxides through active participation of cysteine residues (CP, CR). The first step in catalysis, the reduction of peroxide substrate, is fast, 107 - 108 M−1s−1 for human Prx2. In addition, the high intracellular concentration of Prx positions them not only as good antioxidants but also as central players in redox signaling pathways. These biological functions can be affected by post-translational modifications that could alter the peroxidase activity and/or interaction with other proteins. In particular, inactivation by hyperoxidation of CP, which occurs when a second molecule of peroxide reacts with the CP in the sulfenic acid form, modulates their participation in redox signaling pathways. The higher sensitivity to hyperoxidation of some Prx has been related to the presence of structural motifs that disfavor disulfide formation at the active site, making the CP sulfenic acid more available for hyperoxidation or interaction with a redox protein target. We previously reported that treatment of human Prx2 with peroxynitrite results in tyrosine nitration, a post-translational modification on non-catalytic residues, yielding a more active peroxidase with higher resistance to hyperoxidation. In this work, studies on various mutants of hPrx2 confirm that the presence of the tyrosyl side-chain of Y193, belonging to the C-terminal YF motif of eukaryotic Prx, is necessary to observe the increase in Prx2 resistance to hyperoxidation. Moreover, our results underline the critical role of this structural motif on the rate of disulfide formation that determines the differential participation of Prx in redox signaling pathways.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Elsevier Science Inc.
![Se ha confirmado la validez de este valor de autoridad por un usuario](/themes/CONICETDigital/images/authority_control/invisible.gif)
dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
dc.subject
HYDROGEN PEROXIDE
dc.subject
HYPEROXIDATION
dc.subject
OXIDATIVE STRESS
dc.subject
PEROXIREDOXIN
dc.subject
PEROXYNITRITE
dc.subject
POST‐TRANSLATIONAL MODIFICATION (PTM)
dc.subject
REDOX SIGNALING
dc.subject
TYROSINE NITRATION
dc.subject.classification
Bioquímica y Biología Molecular
![Se ha confirmado la validez de este valor de autoridad por un usuario](/themes/CONICETDigital/images/authority_control/invisible.gif)
dc.subject.classification
Ciencias Biológicas
![Se ha confirmado la validez de este valor de autoridad por un usuario](/themes/CONICETDigital/images/authority_control/invisible.gif)
dc.subject.classification
CIENCIAS NATURALES Y EXACTAS
![Se ha confirmado la validez de este valor de autoridad por un usuario](/themes/CONICETDigital/images/authority_control/invisible.gif)
dc.title
Unraveling the effects of peroxiredoxin 2 nitration; role of C-terminal tyrosine 193
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2022-07-15T14:54:28Z
dc.journal.volume
141
dc.journal.pagination
492-501
dc.journal.pais
Países Bajos
![Se ha confirmado la validez de este valor de autoridad por un usuario](/themes/CONICETDigital/images/authority_control/invisible.gif)
dc.journal.ciudad
Amsterdam
dc.description.fil
Fil: Randall, Lía M.. Universidad de la República; Uruguay
dc.description.fil
Fil: Dalla Rizza, Joaquín. Universidad de la Republica; Uruguay
dc.description.fil
Fil: Parsonage, Derek. Wake Forest School of Medicine; Estados Unidos
dc.description.fil
Fil: Santos, Javier. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Química y Físico-Química Biológicas "Prof. Alejandro C. Paladini". Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Físico-Química Biológicas; Argentina
dc.description.fil
Fil: Mehl, Ryan A.. University of Oregon; Estados Unidos
dc.description.fil
Fil: Lowther, W. Todd. Wake Forest School of Medicine; Estados Unidos
dc.description.fil
Fil: Poole, Leslie B.. Wake Forest School of Medicine; Estados Unidos
dc.description.fil
Fil: Denicola, Ana. Universidad de la República; Uruguay
dc.journal.title
Free Radical Biology and Medicine
![Se ha confirmado la validez de este valor de autoridad por un usuario](/themes/CONICETDigital/images/authority_control/invisible.gif)
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://linkinghub.elsevier.com/retrieve/pii/S0891584919304629
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1016/j.freeradbiomed.2019.07.016
Archivos asociados