Protein oxidation and cellular homeostasis: Emphasis on metabolism

Cecarini, Valentina; Gee, Jillian; Fioretti, Evandro; Amici, Manila; Angeletti, Mauro; Eleuteri, Anna Maria; Keller, Jeffrey N.

doi:10.1016/j.bbamcr.2006.08.039

Cited by 212 publications

(175 citation statements)

References 122 publications

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“…This same result was not observed in the analysis of IDE-mediated regulation of the proteasome activity. The proteasome is affected by oxidation, and that was apparent with the addition of KFC, which is an oxidizing agent [37,38]. However, the slopes of the inhibition curves for SNP and KFC were different.…”

Section: Discussionmentioning

confidence: 99%

Nitric oxide inhibits insulin-degrading enzyme activity and function through S-nitrosylation

Cordes

Bennett

Siford

et al. 2009

Biochemical Pharmacology

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Section: Discussionmentioning

confidence: 99%

Nitric oxide inhibits insulin-degrading enzyme activity and function through S-nitrosylation

Cordes

Bennett

Siford

et al. 2009

Biochemical Pharmacology

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“…Previously, we have shown that levels of lipid peroxidation products, such as 4-HNE, were increased in lungs of patients with COPD (40). Post-translational modifications of various proteins by oxidative/ nitrosative stress have been shown to have influence on various cellular functions (25,41,42). To determine the CS-mediated reduction in SIRT1 levels and its post-translational modifications, SIRT1 modification was evaluated by measuring the SIRT1 adducts with 4-HNE (reactive aldehydes which form protein carbonyls), a highly reactive diffusible product of lipid peroxidation and a key mediator of oxidant-induced cell signaling and apoptosis (43).…”

Section: Discussionmentioning

confidence: 99%

SIRT1, an Antiinflammatory and Antiaging Protein, Is Decreased in Lungs of Patients with Chronic Obstructive Pulmonary Disease

Saravanan¹,

Yang²,

Kinnula³

et al. 2008

Am J Respir Crit Care Med

463

393

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Rationale: Abnormal inflammation and accelerated decline in lung function occur in patients with chronic obstructive pulmonary disease (COPD). Human sirtuin (SIRT1), an antiaging and antiinflammatory protein, is a metabolic NAD 1 -dependent protein/histone deacetylase that regulates proinflammatory mediators by deacetylating histone and nonhistone proteins. Objectives: To determine the expression of SIRT1 in lungs of smokers and patients with COPD, and to elucidate the regulation of SIRT1 in response to cigarette smoke in macrophages, and its impact on nuclear factor (NF)-kB regulation. Methods: SIRT1 and NF-kB levels were assessed in lung samples of nonsmokers, smokers, and patients with COPD. Human monocytemacrophage cells (MonoMac6) were treated with cigarette smoke extract (CSE) to determine the mechanism of CSE-mediated regulation of SIRT1 and its involvement in RelA/p65 regulation and IL-8 release.Measurements and Main Results: Peripheral lungs of smokers and patients with COPD showed decreased levels of nuclear SIRT1, as compared with nonsmokers, associated with its post-translational modifications (formation of nitrotyrosine and aldehyde carbonyl adducts). Treatment of MonoMac6 cells with CSE showed decreased levels of SIRT1 associated with increased acetylation of RelA/p65 NFkB. Mutation or knockdown of SIRT1 resulted in increased acetylation of nuclear RelA/p65 and IL-8 release, whereas overexpression of SIRT1 decreased IL-8 release in response to CSE treatment in MonoMac6 cells. Conclusions: SIRT1 levels were reduced in macrophages and lungs of smokers and patients with COPD due to its post-translational modifications by cigarette smoke-derived reactive components, leading to increased acetylation of RelA/p65. Thus, SIRT1 plays a pivotal role in regulation of NF-kB-dependent proinflammatory mediators in lungs of smokers and patients with COPD.

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“…In contact with the pulp cells, HP and the ROS resulting from its degradation produce a direct oxidative damage and may generate a secondary oxidative stress due to the imbalance between the amount of ROS and intracellular antioxidants (1). The present study evaluated the protective action of VE α-T isomer at different concentrations (1, 3, 5 and 10 mM) used for various pretreatment times (1, 4, 8 and 24 h) against the toxicity of HP applied on MDPC-23 odontoblast-like cells.…”

Section: Discussionmentioning

confidence: 99%

“…HP and other reactive oxygen species (ROS) resulting from its degradation are highly reactive and unstable, and have a rapid interaction with cellular macromolecules such as proteins, lipids and nucleic acids. Antioxidant enzymes act inactivating ROS in order to maintain balance and permit an adequate functioning of the cell (1).…”

Section: Introductionmentioning

confidence: 99%

Dose-Response and Time-Course of a-Tocoferol Mediating the Cytoprotection Of Dental Pulp Cells Against Hydrogen Peroxide

et al. 2014

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This in vitro study evaluated the potential protective effect of vitamin E alpha-tocopherol (α-T) isomer against the toxicity of hydrogen peroxide (HP) applied on dental pulp cells. Odontoblast-like MDPC-23 cells were seeded on 96-well plates for 72 h, treated with different concentrations of α-T (1, 3, 5, and 10 mM) for different times (1, 4, 8, and 24 h) and then exposed or not to a 0.018% HP solution for 30 min. In positive and negative control groups, cells were exposed to HP or culture medium (DMEM containing 5% DMSO), respectively. Cell viability was assessed by the MTT assay and the absorbance numeric data, expressed as percentage values, were subjected to the statistical analysis by KruskalWallis and Mann-Whitney tests (α =5%). Considering the cells in the negative control as having 100% of cell viability, all combinations of α-T concentrations and pretreatment times showed a protective effect against HP cytotoxicity. Significant reduction of cell viability (59%) was observed in the positive control compared with the negative control.The highest values of pulp cell viability were obtained after pretreatment with 1 and 3 mM α-T concentrations for 24 h followed by exposure to HP (126% and 97% of cell viability, respectively). Under the tested conditions, the most effective cell protection against the cytotoxic effects of HP was provided by the lowest concentrations of α-T (1 and 3 mM) applied for 24 h.

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Protein oxidation and cellular homeostasis: Emphasis on metabolism

Cited by 212 publications

References 122 publications

Nitric oxide inhibits insulin-degrading enzyme activity and function through S-nitrosylation

Nitric oxide inhibits insulin-degrading enzyme activity and function through S-nitrosylation

SIRT1, an Antiinflammatory and Antiaging Protein, Is Decreased in Lungs of Patients with Chronic Obstructive Pulmonary Disease

Dose-Response and Time-Course of a-Tocoferol Mediating the Cytoprotection Of Dental Pulp Cells Against Hydrogen Peroxide

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