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Article: Biochemistry of protein tyrosine nitration in cardiovascular pathology.

Peluffo, Gonzalo / Radi, Rafael

2007 Volume 75, Issue 2, Page(s) 291–302

Abstract: Several pathologies of the cardiovascular system are associated with an augmented production of nitric oxide and/or superoxide-derived oxidants and/or alteration in the antioxidant detoxification pathways that lead to nitroxidative stress. One important ... ...

Abstract	Several pathologies of the cardiovascular system are associated with an augmented production of nitric oxide and/or superoxide-derived oxidants and/or alteration in the antioxidant detoxification pathways that lead to nitroxidative stress. One important consequence of these reactive intermediates at the biochemical level is the nitration of protein tyrosines, which is performed through either of two of the relevant nitration pathways that operate in vivo, namely peroxynitrite and heme peroxidase-dependent nitration. Proteins nitrated at tyrosine residues have been detected in several compartments of the cardiovascular system. In this review a selection of nitrated proteins in plasma (fibrinogen, plasmin, Apo-1), vessel wall (Apo-B, cyclooxygenase, prostaglandin synthase, Mn-superoxide dismutase) and myocardium (myofibrillar creatine kinase, alpha-actinin, sarcoplasmic reticulum Ca(2+) ATPase) are analyzed in the context of cardiovascular disease. Nitration of tyrosine can affect protein function, which could directly link nitroxidative stress to the molecular alterations found in disease. While some proteins are inactivated by nitration (e.g. Mn-SOD) others undergo a gain-of-function (e.g. fibrinogen) that can have an ample impact on the pathophysiology of the cardiovascular system. Nitrotyrosine is also emerging as a novel independent marker of cardiovascular disease. Pharmacological strategies directed towards inhibiting protein nitration will assist to shed light on the relevance of this post-translational modification to human cardiovascular pathology.
MeSH term(s)	Animals ; Cardiovascular Diseases/metabolism ; Cardiovascular System/metabolism ; Fibrinogen/metabolism ; Humans ; Nitric Oxide/metabolism ; Nitrosation ; Signal Transduction/physiology ; Superoxide Dismutase/metabolism ; Tyrosine/analogs & derivatives ; Tyrosine/metabolism
Chemical Substances	Nitric Oxide (31C4KY9ESH) ; 3-nitrotyrosine (3604-79-3) ; Tyrosine (42HK56048U) ; Fibrinogen (9001-32-5) ; Superoxide Dismutase (EC 1.15.1.1)
Language	English
Publishing date	2007-07-15
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	80340-6
ISSN	1755-3245 ; 0008-6363
ISSN (online)	1755-3245
ISSN	0008-6363
DOI	10.1016/j.cardiores.2007.04.024
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Article ; Online: Correction: Nitro-Arachidonic Acid Prevents Angiotensin II Induced Mitochondrial Dysfunction in Kidney Proximal Tubular Cells.

Sánchez-Calvo, Beatriz / Cassina, Adriana / Rios, Natalia / Peluffo, Gonzalo / Boggia, José / Radi, Rafael / Rubbo, Homero / Trostchansky, Andrés

PloS one

2016 Volume 11, Issue 4, Page(s) e0154651

Abstract: This corrects the article DOI: 10.1371/journal.pone.0150459.]. ...

Abstract	[This corrects the article DOI: 10.1371/journal.pone.0150459.].
Language	English
Publishing date	2016
Publishing country	United States
Document type	Published Erratum
ISSN	1932-6203
ISSN (online)	1932-6203
DOI	10.1371/journal.pone.0154651
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Article ; Online: Nitric oxide diffusion to red blood cells limits extracellular, but not intraphagosomal, peroxynitrite formation by macrophages.

Prolo, Carolina / Álvarez, María Noel / Ríos, Natalia / Peluffo, Gonzalo / Radi, Rafael / Romero, Natalia

Free radical biology & medicine

2015 Volume 87, Page(s) 346–355

Abstract: Macrophage-derived nitric oxide ((•)NO) participates in cytotoxic mechanisms against diverse microorganisms and tumor cells. These effects can be mediated by (•)NO itself or (•)NO-derived species such as peroxynitrite formed by its diffusion-controlled ... ...

Abstract	Macrophage-derived nitric oxide ((•)NO) participates in cytotoxic mechanisms against diverse microorganisms and tumor cells. These effects can be mediated by (•)NO itself or (•)NO-derived species such as peroxynitrite formed by its diffusion-controlled reaction with NADPH oxidase-derived superoxide radical anion (O(2)(•-)). In vivo, the facile extracellular diffusion of (•)NO as well as different competing consumption routes limit its bioavailability for the reaction with O(2)(•-) and, hence, peroxynitrite formation. In this work, we evaluated the extent by which (•)NO diffusion to red blood cells (RBC) can compete with activated macrophages-derived O(2)(•-) and affect peroxynitrite formation yields. Macrophage-dependent peroxynitrite production was determined by boron-based probes that react directly with peroxynitrite, namely, coumarin-7-boronic acid (CBA) and fluorescein-boronate (Fl-B). The influence of (•)NO diffusion to RBC on peroxynitrite formation was experimentally analyzed in co-incubations of (•)NO and O(2)(•-)-forming macrophages with erythrocytes. Additionally, we evaluated the permeation of (•)NO to RBC by measuring the intracellular oxidation of oxyhemoglobin to methemoglobin. Our results indicate that diluted RBC suspensions dose-dependently inhibit peroxynitrite formation, outcompeting the O(2)(•-) reaction. Computer-assisted kinetic studies evaluating peroxynitrite formation by its precursor radicals in the presence of RBC are in accordance with experimental results. Moreover, the presence of erythrocytes in the proximity of (•)NO and O(2)(•-)-forming macrophages prevented intracellular Fl-B oxidation pre-loaded in L1210 cells co-cultured with activated macrophages. On the other hand, Fl-B-coated latex beads incorporated in the macrophage phagocytic vacuole indicated that intraphagosomal probe oxidation by peroxynitrite was not affected by nearby RBC. Our data support that in the proximity of a blood vessel, (•)NO consumption by RBC will limit the extracellular formation (and subsequent cytotoxic effects) of peroxynitrite by activated macrophages, while the intraphagosomal yield of peroxynitrite will remain unaffected.
MeSH term(s)	Animals ; Diffusion ; Erythrocytes/metabolism ; Kinetics ; Macrophages/metabolism ; Mice ; Nitric Oxide/metabolism ; Oxidation-Reduction ; Peroxynitrous Acid/biosynthesis ; Peroxynitrous Acid/metabolism ; Phagosomes/metabolism ; Superoxides/metabolism
Chemical Substances	Superoxides (11062-77-4) ; Peroxynitrous Acid (14691-52-2) ; Nitric Oxide (31C4KY9ESH)
Language	English
Publishing date	2015-10
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	807032-5
ISSN	1873-4596 ; 0891-5849
ISSN (online)	1873-4596
ISSN	0891-5849
DOI	10.1016/j.freeradbiomed.2015.06.027
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Article ; Online: Nitro-Arachidonic Acid Prevents Angiotensin II-Induced Mitochondrial Dysfunction in a Cell Line of Kidney Proximal Tubular Cells.

Sánchez-Calvo, Beatriz / Cassina, Adriana / Rios, Natalia / Peluffo, Gonzalo / Boggia, José / Radi, Rafael / Rubbo, Homero / Trostchansky, Andres

PloS one

2016 Volume 11, Issue 3, Page(s) e0150459

Abstract: Nitro-arachidonic acid (NO2-AA) is a cell signaling nitroalkene that exerts anti-inflammatory activities during macrophage activation. While angiotensin II (ANG II) produces an increase in reactive oxygen species (ROS) production and mitochondrial ... ...

Abstract	Nitro-arachidonic acid (NO2-AA) is a cell signaling nitroalkene that exerts anti-inflammatory activities during macrophage activation. While angiotensin II (ANG II) produces an increase in reactive oxygen species (ROS) production and mitochondrial dysfunction in renal tubular cells, little is known regarding the potential protective effects of NO2-AA in ANG II-mediated kidney injury. As such, this study examines the impact of NO2-AA on ANG II-induced mitochondrial dysfunction in an immortalized renal proximal tubule cell line (HK-2 cells). Treatment of HK-2 cells with ANG II increases the production of superoxide (O2●-), nitric oxide (●NO), inducible nitric oxide synthase (NOS2) expression, peroxynitrite (ONOO-) and mitochondrial dysfunction. Using high-resolution respirometry, it was observed that the presence of NO2-AA prevented ANG II-mediated mitochondrial dysfunction. Attempting to address mechanism, we treated isolated rat kidney mitochondria with ONOO-, a key mediator of ANG II-induced mitochondrial damage, in the presence or absence of NO2-AA. Whereas the activity of succinate dehydrogenase (SDH) and ATP synthase (ATPase) were diminished upon exposure to ONOO-, they were restored by pre-incubating the mitochondria with NO2-AA. Moreover, NO2-AA prevents oxidation and nitration of mitochondrial proteins. Combined, these data demonstrate that ANG II-mediated oxidative damage and mitochondrial dysfunction is abrogated by NO2-AA, identifying this compound as a promising pharmacological tool to prevent ANG II-induced renal disease.
MeSH term(s)	Adenosine Triphosphatases/metabolism ; Angiotensin II/pharmacology ; Arachidonic Acid/pharmacology ; Cell Line ; Humans ; Kidney Tubules, Proximal/drug effects ; Kidney Tubules, Proximal/metabolism ; Mitochondria/drug effects ; Mitochondria/metabolism ; Models, Biological ; Nitric Oxide Synthase/metabolism ; Oxidation-Reduction ; Peroxynitrous Acid/metabolism ; Succinate Dehydrogenase/metabolism ; Superoxides/metabolism
Chemical Substances	Superoxides (11062-77-4) ; Angiotensin II (11128-99-7) ; Peroxynitrous Acid (14691-52-2) ; Arachidonic Acid (27YG812J1I) ; Nitric Oxide Synthase (EC 1.14.13.39) ; Succinate Dehydrogenase (EC 1.3.99.1) ; Adenosine Triphosphatases (EC 3.6.1.-)
Language	English
Publishing date	2016
Publishing country	United States
Document type	Journal Article
ISSN	1932-6203
ISSN (online)	1932-6203
DOI	10.1371/journal.pone.0150459
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Article ; Online: Correction

Beatriz Sánchez-Calvo / Adriana Cassina / Natalia Rios / Gonzalo Peluffo / José Boggia / Rafael Radi / Homero Rubbo / Andrés Trostchansky

PLoS ONE, Vol 11, Iss 4, p e

Nitro-Arachidonic Acid Prevents Angiotensin II Induced Mitochondrial Dysfunction in Kidney Proximal Tubular Cells.

2016 Volume 0154651

Abstract: This corrects the article DOI:10.1371/journal.pone.0150459.]. ...

Abstract	[This corrects the article DOI:10.1371/journal.pone.0150459.].
Keywords	Medicine ; R ; Science ; Q
Language	English
Publishing date	2016-01-01T00:00:00Z
Publisher	Public Library of Science (PLoS)
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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Article: Protein tyrosine nitration--functional alteration or just a biomarker?

Souza, José M / Peluffo, Gonzalo / Radi, Rafael

Free radical biology & medicine

2008 Volume 45, Issue 4, Page(s) 357–366

Abstract: Protein 3-nitrotyrosine is a posttranslational modification found in many pathological conditions from acute to chronic diseases. Could 3-nitrotyrosine formation participate on the basis of these diseases or is it just a marker connected with the ... ...

Abstract	Protein 3-nitrotyrosine is a posttranslational modification found in many pathological conditions from acute to chronic diseases. Could 3-nitrotyrosine formation participate on the basis of these diseases or is it just a marker connected with the associated nitroxidative stress? In vitro and in vivo data, including proteomic research, show that protein tyrosine nitration is a selective process where only a small amount of proteins is found nitrated and one or a few tyrosine residues are modified in each. Accumulating data suggest a strong link between protein 3-nitrotyrosine and the mechanism involved in disease development. In this review, we analyze the factors determining protein 3-nitrotyrosine formation, the functional and biological outcome associated with protein tyrosine nitration, and the fate of the nitrated proteins.
MeSH term(s)	Amino Acid Sequence ; Biomarkers/metabolism ; Molecular Sequence Data ; Nitrates/metabolism ; Proteins/chemistry ; Proteins/metabolism ; Tyrosine/metabolism
Chemical Substances	Biomarkers ; Nitrates ; Proteins ; Tyrosine (42HK56048U)
Language	English
Publishing date	2008-08-15
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	807032-5
ISSN	1873-4596 ; 0891-5849
ISSN (online)	1873-4596
ISSN	0891-5849
DOI	10.1016/j.freeradbiomed.2008.04.010
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Article ; Online: Intraphagosomal peroxynitrite as a macrophage-derived cytotoxin against internalized Trypanosoma cruzi: consequences for oxidative killing and role of microbial peroxiredoxins in infectivity.

Alvarez, María Noel / Peluffo, Gonzalo / Piacenza, Lucía / Radi, Rafael

The Journal of biological chemistry

2010 Volume 286, Issue 8, Page(s) 6627–6640

Abstract: Macrophage-derived radicals generated by the NADPH oxidase complex and inducible nitric-oxide synthase (iNOS) participate in cytotoxic mechanisms against microorganisms. Nitric oxide ((•)NO) plays a central role in the control of acute infection by ... ...

Abstract	Macrophage-derived radicals generated by the NADPH oxidase complex and inducible nitric-oxide synthase (iNOS) participate in cytotoxic mechanisms against microorganisms. Nitric oxide ((•)NO) plays a central role in the control of acute infection by Trypanosoma cruzi, the causative agent of Chagas disease, and we have proposed that much of its action relies on macrophage-derived peroxynitrite (ONOO(-) + ONOOH) formation, a strong oxidant arising from the reaction of (•)NO with superoxide radical (O(2)(-)). Herein, we have shown that internalization of T. cruzi trypomastigotes by macrophages triggers the assembly of the NADPH oxidase complex to yield O(2)(-) during a 60-90-min period. This does not interfere with IFN-γ-dependent iNOS induction and a sustained (•)NO production (∼24 h). The major mechanism for infection control via reactive species formation occurred when (•)NO and O(2)() were produced simultaneously, generating intraphagosomal peroxynitrite levels compatible with microbial killing. Moreover, biochemical and ultrastructural analysis confirmed cellular oxidative damage and morphological disruption in internalized parasites. Overexpression of cytosolic tryparedoxin peroxidase in T. cruzi neutralized macrophage-derived peroxynitrite-dependent cytotoxicity to parasites and favored the infection in an animal model. Collectively, the data provide, for the first time, direct support for the action of peroxynitrite as an intraphagosomal cytotoxin against pathogens and the premise that microbial peroxiredoxins facilitate infectivity via decomposition of macrophage-derived peroxynitrite.
MeSH term(s)	Animals ; Cell Line ; Chagas Disease/enzymology ; Cytotoxins/metabolism ; Macrophages/enzymology ; Macrophages/parasitology ; Macrophages/ultrastructure ; Mice ; Nitric Oxide/metabolism ; Nitric Oxide Synthase Type II/metabolism ; Oxidation-Reduction ; Peroxynitrous Acid/metabolism ; Protozoan Proteins/biosynthesis ; Superoxides/metabolism ; Thioredoxins/biosynthesis ; Trypanosoma cruzi/enzymology ; Trypanosoma cruzi/ultrastructure
Chemical Substances	Cytotoxins ; Protozoan Proteins ; tryparedoxin ; Superoxides (11062-77-4) ; Peroxynitrous Acid (14691-52-2) ; Nitric Oxide (31C4KY9ESH) ; Thioredoxins (52500-60-4) ; Nitric Oxide Synthase Type II (EC 1.14.13.39) ; Nos2 protein, mouse (EC 1.14.13.39)
Language	English
Publishing date	2010-11-23
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1074/jbc.M110.167247
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Article ; Online: Trypanosoma cruzi antioxidant enzymes as virulence factors in Chagas disease.

Piacenza, Lucía / Peluffo, Gonzalo / Alvarez, María Noel / Martínez, Alejandra / Radi, Rafael

Antioxidants & redox signaling

2012 Volume 19, Issue 7, Page(s) 723–734

Abstract: Significance: Chagas disease (CD) affects several million people in Latin America and is spreading beyond its classical boundaries due to the migration of infected host and insect vectors, HIV co-infection, and blood transfusion. The current therapy is ... ...

Abstract	Significance: Chagas disease (CD) affects several million people in Latin America and is spreading beyond its classical boundaries due to the migration of infected host and insect vectors, HIV co-infection, and blood transfusion. The current therapy is not adequate for treatment of the chronic phase of CD, and new drugs are warranted. Recent advances: Trypanosoma cruzi is equipped with a specialized and complex network of antioxidant enzymes that are located at different subcellular compartments which defend the parasite against host oxidative assaults. Recently, strong evidence has emerged which indicates that enzyme components of the T. cruzi antioxidant network (cytosolic and mitochondrial peroxiredoxins and trypanothione synthetase) in naturally occurring strains act as a virulence factor for CD. This precept is recapitulated with the observed increased resistance of T. cruzi peroxirredoxins overexpressers to in vivo or in vitro nitroxidative stress conditions. In addition, the modulation of mitochondrial superoxide radical levels by iron superoxide dismutase (FeSODA) influences parasite programmed cell death, underscoring the role of this enzyme in parasite survival. Critical issues: The unraveling of the biological significance of FeSODs in T. cruzi programmed cell death in the context of chronic infection in CD is still under examination. Future directions: The role of the antioxidant enzymes in the pathogenesis of CD, including parasite virulence and persistence, and their feasibility as pharmacological targets justifies further investigation.
MeSH term(s)	Animals ; Apoptosis ; Chagas Disease/parasitology ; Chagas Disease/pathology ; Host-Parasite Interactions ; Humans ; Nitric Oxide/metabolism ; Oxidative Stress ; Oxidoreductases/physiology ; Protozoan Proteins/physiology ; Reactive Nitrogen Species/metabolism ; Trypanosoma cruzi/pathogenicity ; Trypanosoma cruzi/physiology ; Virulence Factors/physiology
Chemical Substances	Protozoan Proteins ; Reactive Nitrogen Species ; Virulence Factors ; Nitric Oxide (31C4KY9ESH) ; Oxidoreductases (EC 1.-)
Language	English
Publishing date	2012-05-21
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	1483836-9
ISSN	1557-7716 ; 1523-0864
ISSN (online)	1557-7716
ISSN	1523-0864
DOI	10.1089/ars.2012.4618
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Article ; Online: Nitro-Arachidonic Acid Prevents Angiotensin II-Induced Mitochondrial Dysfunction in a Cell Line of Kidney Proximal Tubular Cells.

Beatriz Sánchez-Calvo / Adriana Cassina / Natalia Rios / Gonzalo Peluffo / José Boggia / Rafael Radi / Homero Rubbo / Andres Trostchansky

PLoS ONE, Vol 11, Iss 3, p e

2016 Volume 0150459

Abstract	Nitro-arachidonic acid (NO2-AA) is a cell signaling nitroalkene that exerts anti-inflammatory activities during macrophage activation. While angiotensin II (ANG II) produces an increase in reactive oxygen species (ROS) production and mitochondrial dysfunction in renal tubular cells, little is known regarding the potential protective effects of NO2-AA in ANG II-mediated kidney injury. As such, this study examines the impact of NO2-AA on ANG II-induced mitochondrial dysfunction in an immortalized renal proximal tubule cell line (HK-2 cells). Treatment of HK-2 cells with ANG II increases the production of superoxide (O2●-), nitric oxide (●NO), inducible nitric oxide synthase (NOS2) expression, peroxynitrite (ONOO-) and mitochondrial dysfunction. Using high-resolution respirometry, it was observed that the presence of NO2-AA prevented ANG II-mediated mitochondrial dysfunction. Attempting to address mechanism, we treated isolated rat kidney mitochondria with ONOO-, a key mediator of ANG II-induced mitochondrial damage, in the presence or absence of NO2-AA. Whereas the activity of succinate dehydrogenase (SDH) and ATP synthase (ATPase) were diminished upon exposure to ONOO-, they were restored by pre-incubating the mitochondria with NO2-AA. Moreover, NO2-AA prevents oxidation and nitration of mitochondrial proteins. Combined, these data demonstrate that ANG II-mediated oxidative damage and mitochondrial dysfunction is abrogated by NO2-AA, identifying this compound as a promising pharmacological tool to prevent ANG II-induced renal disease.
Keywords	Medicine ; R ; Science ; Q
Language	English
Publishing date	2016-01-01T00:00:00Z
Publisher	Public Library of Science (PLoS)
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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Article ; Online: Fighting the oxidative assault: the Trypanosoma cruzi journey to infection.

Piacenza, Lucía / Alvarez, María Noel / Peluffo, Gonzalo / Radi, Rafael

Current opinion in microbiology

2009 Volume 12, Issue 4, Page(s) 415–421

Abstract: Activation of professional phagocytes with the concomitant generation of oxidant species is a medullar innate immune process for the control of acute Trypanosoma cruzi infection. Recent data reinforce the hypothesis that parasites more prepared to deal ... ...

Abstract	Activation of professional phagocytes with the concomitant generation of oxidant species is a medullar innate immune process for the control of acute Trypanosoma cruzi infection. Recent data reinforce the hypothesis that parasites more prepared to deal with the host-oxidative assault are more efficient for the establishment of Chagas disease. For instance, parasites overexpressing peroxiredoxins are more resistant to macrophage-derived peroxynitrite, a key cytotoxic oxidant produced in the phagosome towards the internalized parasite. Differentiation to the infective metacyclic trypomastigote is accompanied by an increased expression of antioxidant enzymes. Moreover, augmented antioxidant enzyme expression and activities correlate with higher parasite virulence in experimental infections. The potency of the parasite antioxidant armamentarium influences the final fate of the Trypanosoma cruzi journey to macrophage invasion at the onset of infection.
MeSH term(s)	Animals ; Chagas Disease/parasitology ; Host-Parasite Interactions ; Humans ; Macrophages/immunology ; Macrophages/parasitology ; Oxidants/immunology ; Oxidants/metabolism ; Oxidative Stress ; Stress, Physiological ; Trypanosoma cruzi/immunology ; Trypanosoma cruzi/physiology
Chemical Substances	Oxidants
Language	English
Publishing date	2009-08
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	1418474-6
ISSN	1879-0364 ; 1369-5274
ISSN (online)	1879-0364
ISSN	1369-5274
DOI	10.1016/j.mib.2009.06.011
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