ArticleSheng Wu Wu Li Hsueh Bao2012
Reversible inactivation of dihydrolipoamide dehydrogenase by Angeli's salt.
Article in Sheng Wu Wu Li Hsueh Bao, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
What it found
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The trial behind it
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Who cites it
17 citing papers in PubMed, 22 citations in OpenAlex.
- Insights into Active Site Cysteine Residues inInternational journal of molecular sciences · 2025Review
- Roles of Dihydrolipoamide Dehydrogenase in Health and Disease.Antioxidants & redox signaling · 2023Review
- Nitric oxide regulation of cellular metabolism: Adaptive tuning of cellular energy.Nitric oxide : biology and chemistry · 2023Review
- Dihydrolipoamide dehydrogenase, pyruvate oxidation, and acetylation-dependent mechanisms intersecting drug iatrogenesis.Cellular and molecular life sciences : CMLS · 2021Review
- More than just protein building blocks: how amino acids and related metabolic pathways fuel macrophage polarization.The FEBS journal · 2021Review
- TCA cycle metabolic compromise due to an aberrant S-nitrosoproteome in HIV-associated neurocognitive disorder with methamphetamine use.Journal of neurovirology · 2021Article
- Nitric Oxide in Macrophage Immunometabolism: Hiding in Plain Sight.Metabolites · 2020Review
- Nitric Oxide-Dependent Protein Post-Translational Modifications Impair Mitochondrial Function and Metabolism to Contribute to Neurodegenerative Diseases.Antioxidants & redox signaling · 2020Review
- Chronic Inhibition of Mitochondrial Dihydrolipoamide Dehydrogenase (DLDH) as an Approach to Managing Diabetic Oxidative Stress.Antioxidants (Basel, Switzerland) · 2019Article
- A Multiplex Enzymatic Machinery for Cellular Protein S-nitrosylation.Molecular cell · 2018Article
- Administration of 5-methoxyindole-2-carboxylic acid that potentially targets mitochondrial dihydrolipoamide dehydrogenase confers cerebral preconditioning against ischemic stroke injury.Free radical biology & medicine · 2017Article
- PTEN degradation after ischemic stroke: a double-edged sword.Neuroscience · 2014Article
- Positive oxidative stress in aging and aging-related disease tolerance.Redox biology · 2014Review
- Protein redox modification as a cellular defense mechanism against tissue ischemic injury.Oxidative medicine and cellular longevity · 2014Review
- Serum Dihydrolipoamide Dehydrogenase Is a Labile Enzyme.Journal of biochemical and pharmacological research · 2013Article
- Protein Oxidative Modifications: Beneficial Roles in Disease and Health.Journal of biochemical and pharmacological research · 2013Article
- Reversible inactivation of dihydrolipoamide dehydrogenase by mitochondrial hydrogen peroxide.Free radical research · 2013Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Dihydrolipoamide dehydrogenase (DLDH) is a key component of 3 mitochondrial α-keto acid dehydrogenase complexes including pyruvate dehydrogenase complex, α-ketoglutarate dehydrogenase complex, and branched chain amino acid dehydrogenase complex. It is a pyridine-dependent disulfide oxidoreductase that is very sensitive to oxidative modifications by reactive nitrogen species (RNS) and reactive oxygen species (ROS). The objective of this study was to investigate the mechanisms of DLDH modification by RNS derived from Angeli's salt. Studies were conducted using isolated rat brain mitochondria that were incubated with varying concentrations of Angeli's salt followed by spectrophotometric enzyme assays, blue native gel analysis, and 2-dimensional gel-based proteomic approaches. Results show that DLDH could be inactivated by Angeli's salt in a concentration dependent manner and the inactivation was a targeting rather than a random process as peroxynitrite did not show any detectable inhibitory effect on the enzyme's activity under the same experimental conditions. Since Angeli's salt can readily decompose at physiological pH to yield nitroxyl anion (HNO) and nitric oxide, further studies were conducted to determine the actual RNS that was responsible for DLDH inactivation. Results indicate that it was HNO that exerted the effect of Angeli's salt on DLDH. Finally, two-dimensional Western blot analysis indicates that DLDH inactivation by Angeli's salt was accompanied by formation of protein s-nitrosothiols, suggesting that s-nitrosylation is likely the cause of loss in enzyme's activity. Taken together, the present study provides insights into mechanisms of DLDH inactivation induced by HNO derived from Angeli's salt.
Identifiers
23139597PMC3490496W2418105944What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.