Plasma proteins modified by tyrosine nitration in acute respiratory distress syndrome

Gole, Madhura; Souza, José Maria de; Choi, Irene; Hertkorn, Caryn; Malcolm, Stuart; Foust, Raymond; Finkel, Barbara; Lanken, Paul N.; Ischiropoulos, Harry

doi:10.1152/ajplung.2000.278.5.l961

Cited by 132 publications

(91 citation statements)

References 43 publications

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“…Protein nitration can have a significant impact on the structural and functional integrity of the proteome (Sohal et al 2000;Murray et al 2003;Greenacre and Ischiropoulos 2001;Adachi et al 2002;Castro et al 1994;Gole et al 2000;Ischiropoulos 2003). Specific brain regions are especially vulnerable to oxidative stress as a result of elevated free radical levels and insufficient antioxidant defenses (Coyle and Puttfarcken 1993;Sohal et al 1994).…”

Section: Discussionmentioning

confidence: 99%

Proteomic analysis of protein nitration in rat cerebellum: effect of biological aging

Gokulrangan

Zaidi

Michaelis

et al. 2006

Journal of Neurochemistry

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3-Nitrotyrosine (3-NT) is a useful biomarker of increasing oxidative stress and protein nitration during biological aging. The proteomic analysis of cerebellar homogenate from Fisher 344/Brown Norway (BN/F1) rats shows an age-dependent increase in protein nitration, monitored by western-blot analysis after two-dimensional gel electrophoresis (2DE), mainly in the acidic region. Analysis of in-gel digests by nanoelectrospray (NSI)-MS/MS resulted in the identification of 16 putatively nitrated proteins. The selective isolation of nitrated proteins using immunoprecipitation, followed by SDS-PAGE and in-gel digest/NSI-MS/MS analysis led to the identification of 22 putatively nitrated proteins, of which 7 were identical to those detected after 2DE. When proteins were separated by solution isoelectrofocusing and analyzed by NSI MS/MS, we obtained MS/MS spectra of 3-NT containing peptides of four proteins -similar to ryanodine receptor 3, low density lipoprotein related receptor 2, similar to nebulin-related anchoring protein isoform C and 2,3 cyclic nucleotide 3-phosphodiesterase. Although the functional consequences of protein nitration for these targets are not yet known, our proteomic experiments serve as a first screen for the more targeted analysis of nitrated proteins from aging cerebellum for functional characterization. Oxidative stress and biological aging contribute to elevated levels of reactive oxygen species (ROS) and reactive nitrogen species (RNS), causing reversible as well as irreversible covalent protein modifications (Oliver et al.

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Section: Discussionmentioning

confidence: 99%

Proteomic analysis of protein nitration in rat cerebellum: effect of biological aging

Gokulrangan

Zaidi

Michaelis

et al. 2006

Journal of Neurochemistry

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“…The pathogenic mechanisms of this disease are not well understood, but the role of reactive oxygen species and ·NO has gained increasing attention. Previous studies show that NOS2 expression and ·NO end products are increased in lungs of patients with ARDS (25,32). Whether ·NO has a beneficial role or participates in the mechanisms of injury is still debated (24).…”

Section: Discussionmentioning

confidence: 99%

Effects of Acute Hypoxia and Lipopolysaccharide on Nitric Oxide Synthase-2 Expression in Acute Lung Injury

Agorreta

Garayoa²,

Montuenga³

et al. 2003

Am J Respir Crit Care Med

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The potential role of nitric oxide synthase-2 (NOS2) in acute lung injury (ALI) has gained increasing attention. This study evaluates the effects of hypoxia, an important feature of ALI, on NOS2 expression in a rat model of ALI caused by exposure to hypoxia and LPS. Exposure to hypoxia alone had no effect on the expression of NOS2 in rat lungs. LPS treatment resulted in a significant increase in NOS2 in the lungs, which was further enhanced by concomitant exposure to hypoxia. Immunohistochemical analysis and in situ hybridization showed no changes in the expression of NOS2 in lung resident cells under any conditions. The increase in NOS2 levels is mainly due to the influx of NOS2-expressing inflammatory cells. By morphologic analysis, these inflammatory cells were identified as neutrophils, lymphocytes, and monocytes. In vitro experiments of lung epithelial and endothelial cell lines showed no detectable expression of NOS2 with any of the treatments. In a macrophage cell line, LPS-induced NOS2 expression was not affected by the concomitant exposure to hypoxia. In conclusion, LPS increases NOS2 expression in rat lungs through the recruitment of NOS2-producing leukocytes. Simultaneous exposure to LPS and hypoxia results in a greater influx of inflammatory cells that further enhances NOS2 expression.Keywords: acute respiratory distress syndrome; endotoxin; leukocytes; sepsis Nitric oxide (·NO) is a multifunctional, short-lived gas that may contribute to toxic free radical production and potentiate lung injury. ·NO is synthesized by a family of enzymes called nitric oxide synthases (NOS). There are three NOS isoforms, namely, NOS1 (neuronal NOS), NOS2 (inducible NOS), and NOS3 (endothelial NOS). These isoenzymes were first purified from rat brain (1), murine macrophages (2), and bovine aortic endothelial cells (3), respectively. NOS enzymes are classically classified as either constitutive (NOS1 and NOS3) or inducible (NOS2), although it is now known that the expression of NOS1 and NOS3 can be induced (4), and that NOS2 is constitutively expressed in numerous cell types (5). The so-called constitutive isoforms (NOS1 and NOS3) release low amounts of ·NO and their activity is dependent on calcium and calmodulin (6). On the other hand, NOS2 produces large amounts of ·NO after induction by stimuli such as endotoxin and inflammatory cytokines (7-9). All three isoenzymes have been found in the lung (10-12) and mediate a wide variety of biological events in the respiratory system, (Received in original form September 11, 2002; accepted in final form May 16, 2003) Supported by the Spanish Ministry of Health (FIS 00/0698 and RTIC C03/10) and the Fundació n Echébano.Correspondence and requests for reprints should be addressed to Javier J. Zulueta, M.D., Pulmonary Medicine Service, Clínica Universitaria de Navarra, University of Navarra, Avenida Pío XII, 36, 31008 Pamplona, Spain. E-mail: jzulueta@unav.es This article has an online supplement, which is accessible from this issue's table of contents online at www.atsjournals...

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“…Nitric oxide production, nitrosative stress and protein nitration increases in both human ARDS and animal models of ARDS [29,[38][39][40][41][42]. Although the BAL levels of nitrite and nitrate did not predict ARDS development in critically ill humans at risk for ARDS, high BAL levels in ARDS patients were associated with worse outcomes and increased mortality [29].…”

Section: Discussionmentioning

confidence: 99%

Exhaled Breath Condensate Nitrate Levels are Inversely Associated with the Body Mass Index of Patients without Respiratory Disease

Fern

ezBustamante²,

Seres³

et al. 2015

J Pulm Respir Med

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Plasma proteins modified by tyrosine nitration in acute respiratory distress syndrome

Cited by 132 publications

References 43 publications

Proteomic analysis of protein nitration in rat cerebellum: effect of biological aging

Proteomic analysis of protein nitration in rat cerebellum: effect of biological aging

Effects of Acute Hypoxia and Lipopolysaccharide on Nitric Oxide Synthase-2 Expression in Acute Lung Injury

Exhaled Breath Condensate Nitrate Levels are Inversely Associated with the Body Mass Index of Patients without Respiratory Disease

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