Differential hepatic protein tyrosine nitration of mouse due to aging – Effect on mitochondrial energy metabolism, quality control machinery of the endoplasmic reticulum and metabolism of drugs

Marshall, Adrienne M.; Lutfeali, Reshma; Raval, Alpan; Chakravarti, Deb N.; Chakravarti, Bulbul

doi:10.1016/j.bbrc.2012.10.142

Cited by 13 publications

(12 citation statements)

References 29 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…In other environments or under conditions of high fluxes of peroxynitrite, the oxidant promotes further PDI oxidation, inactivation, and oligomerization. Because PDI has been implicated in both signaling (4,30,63,65) and damaging events (14,16,17,19,(21)(22)(23)(24), its interaction with peroxynitrite may contribute to the pathogenic mechanism of several disease states.…”

Section: Pdi Oxidation By Peroxynitritementioning

confidence: 99%

“…These oxidants are likely responsible for the oxidative posttranslational modifications of PDI that have been detected under various conditions associated with oxidative stress, leading to the loss of PDI activity (14). For instance, PDI has been shown to be S-glutathionylated in cell cultures challenged with a nitric oxide donor (15), S-nitrosated during neurodegenerative diseases (16 -18), adducted with 4-hydroxynonenal in the livers of rats treated with high-fat diet and ethanol (19) and in the lipid-rich areas of advanced human atherosclerotic lesions (20), carbonylated (21) and nitrated in aging mice (22), and nitrated in muscle biopsies of patients with mitochondrial diseases (23) and in the spinal cords of a mouse model of amyotrophic lateral sclerosis (24). These findings argue for a better understanding of PDI oxidation by biological oxidants with regard to the kinetics and products of these reactions.…”

mentioning

confidence: 99%

See 1 more Smart Citation

Peroxynitrite preferentially oxidizes the dithiol redox motifs of protein-disulfide isomerase

Peixoto

Geyer

Iqbal

et al. 2018

Journal of Biological Chemistry

View full text Add to dashboard Cite

Protein-disulfide isomerase (PDI) is a ubiquitous dithiol-disulfide oxidoreductase that performs an array of cellular functions, such as cellular signaling and responses to cell-damaging events. PDI can become dysfunctional by post-translational modifications, including those promoted by biological oxidants, and its dysfunction has been associated with several diseases in which oxidative stress plays a role. Because the kinetics and products of the reaction of these oxidants with PDI remain incompletely characterized, we investigated the reaction of PDI with the biological oxidant peroxynitrite. First, by determining the rate constant of the oxidation of PDI's redox-active Cys residues (Cys and Cys) by hydrogen peroxide ( = 17.3 ± 1.3 m s at pH 7.4 and 25 °C), we established that the measured decay of the intrinsic PDI fluorescence is appropriate for kinetic studies. The reaction of these PDI residues with peroxynitrite was considerably faster ( = (6.9 ± 0.2) × 10 m s), and both Cys residues were kinetically indistinguishable. Limited proteolysis, kinetic simulations, and MS analyses confirmed that peroxynitrite preferentially oxidizes the redox-active Cys residues of PDI to the corresponding sulfenic acids, which reacted with the resolving thiols at the active sites to produce disulfides ( Cys-Cys and Cys-Cys). A fraction of peroxynitrite, however, decayed to radicals that hydroxylated and nitrated other active-site residues (Trp, Trp, and Tyr). Excess peroxynitrite promoted further PDI oxidation, nitration, inactivation, and covalent oligomerization. We conclude that these PDI modifications may contribute to the pathogenic mechanism of several diseases associated with dysfunctional PDI.

show abstract

Section: Pdi Oxidation By Peroxynitritementioning

confidence: 99%

mentioning

confidence: 99%

Peroxynitrite preferentially oxidizes the dithiol redox motifs of protein-disulfide isomerase

Peixoto

Geyer

Iqbal

et al. 2018

Journal of Biological Chemistry

View full text Add to dashboard Cite

show abstract

“…Similarly, elevated levels of nitration are observed in cardiomyopathy, cardiovascular disease, atherosclerosis (Leeuwenburgh et al 1997, Turko and Murad 2002, Ungvari et al 2005, Peluffo and Radi 2007, Upmacis 2008, Lee et al 2009a, Surmeli et al 2010, arthritis (Sandhu et al 2003 ), diabetes (Turko et al 2003 ), cancer (Azad et al 2008 ), and aging (Pacher et al 2007, Marshall et al 2013. It can be inferred from the range of disorders affected by this PTM that the immune system is a major target of RNS.…”

Section: Introductionmentioning

confidence: 97%

Proteomics quantification of protein nitration

Robinson

2013

Reviews in Analytical Chemistry

View full text Add to dashboard Cite

Protein tyrosine nitration is a post-translational modification (PTM) that can occur in biological systems under conditions of oxidative stress. This PTM can impact protein structure and function and has been linked to diseases such as Alzheimer ' s disease, cardiomyopathy, and arthritis. In order to understand the role that 3-nitrotyrosine (3NT) plays in disease states, a better understanding at the macromolecular level is necessary. Proteomics is a powerful approach that can simultaneously measure hundreds to thousands of proteins in normal or diseased states and thus can be helpful in the analysis of 3NT-modified proteins. Recently, some attention has been focused on the development of proteomic workflows that provide enrichment, characterization, and relative quantification of 3NT-modified proteins. These approaches rely on gel electrophoresis, liquid chromatography, and mass spectrometry (MS) techniques. This review provides an overview of current proteomics approaches for 3NT-modified proteins and highlights current MS-based methods for quantification of this PTM.

show abstract

“…O excesso de peroxinitrito sobre os tióis redox ativos da PDI decai principalmente através do processo catalisado por próton para radicais hidroxila e dióxido de nitrogênio, que por sua vez, promove novas modificações na PDI. (CASONI et al, 2005;VATTEMI et al, 2011;MARSHALL et al, 2013).…”

Section: Discussionunclassified

“…Uma vez que a PDI tem sido implicada tanto na sinalização FERNANDES, 2012;PESCATORE et al, 2012;TANAKA et al, 2016) quanto em eventos danosos (KIM et al, 2000;RABEK;BOYLSTON;PAPACONSTANTINOU, 2003;UEHARA et al, 2006;VATTEMI et al, 2011;MARSHALL et al, 2013), sua interação com peroxinitrito pode contribuir para o mecanismo patogênico de vários estados patológicos. A simulação cinética foi realizada com o software Gepasi (http://www.gepasi.org) usando as equações mostradas no texto (Equações 2-4).…”

Section: Conclusãounclassified

Oxidação da proteína dissulfeto isomerase por peroxinitrito: cinética, produtos e implicações biológicas

Peixoto¹

View full text Add to dashboard Cite

show abstract

Differential hepatic protein tyrosine nitration of mouse due to aging – Effect on mitochondrial energy metabolism, quality control machinery of the endoplasmic reticulum and metabolism of drugs

Cited by 13 publications

References 29 publications

Peroxynitrite preferentially oxidizes the dithiol redox motifs of protein-disulfide isomerase

Peroxynitrite preferentially oxidizes the dithiol redox motifs of protein-disulfide isomerase

Proteomics quantification of protein nitration

Oxidação da proteína dissulfeto isomerase por peroxinitrito: cinética, produtos e implicações biológicas

Contact Info

Product

Resources

About