ArticleJournal of biochemical and pharmacological research2013
Serum Dihydrolipoamide Dehydrogenase Is a Labile Enzyme.
Article in Journal of biochemical and pharmacological research, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 25 citations in OpenAlex.
- A microRNA Catalogue for Red Abalone Larvae Reveals Developmental and Acidification-Associated Abundance Patterns.Marine biotechnology (New York, N.Y.) · 2026Article
- Role of branched chain amino acid metabolism on aging.Biogerontology · 2025Review
- Roles of Dihydrolipoamide Dehydrogenase in Health and Disease.Antioxidants & redox signaling · 2023Review
- Renal-Protective Roles of Lipoic Acid in Kidney Disease.Nutrients · 2023Review
- Dihydrolipoamide dehydrogenase, pyruvate oxidation, and acetylation-dependent mechanisms intersecting drug iatrogenesis.Cellular and molecular life sciences : CMLS · 2021Review
- 5-Methoxyindole-2-Carboylic Acid (MICA) Fails to Retard Development and Progression of Type II Diabetes in ZSF1 Diabetic Rats.Reactive oxygen species (Apex, N.C.) · 2020Article
- An Updated View on the Molecular Pathomechanisms of Human Dihydrolipoamide Dehydrogenase Deficiency in Light of Novel Crystallographic Evidence.Neurochemical research · 2019Review
- Recent Progress on Branched-Chain Amino Acids in Obesity, Diabetes, and Beyond.Endocrinology and metabolism (Seoul, Korea) · 2019Review
- Chronic Inhibition of Mitochondrial Dihydrolipoamide Dehydrogenase (DLDH) as an Approach to Managing Diabetic Oxidative Stress.Antioxidants (Basel, Switzerland) · 2019Article
- Reexploring 5-methoxyindole-2-carboxylic acid (MICA) as a potential antidiabetic agent.Diabetes, metabolic syndrome and obesity : targets and therapy · 2018Article
- Pancreatic mitochondrial complex I exhibits aberrant hyperactivity in diabetes.Biochemistry and biophysics reports · 2017Article
- Medium Optimization for Improved Production of Dihydrolipohyl Dehydrogenase from Bacillus sphaericus PAD-91 in Escherichia coli.Molecular biotechnology · 2017Article
- Recombinant expression, characterization and application of a dihydrolipoamide dehydrogenase with diaphorase activity from Bacillus sphaericus.3 Biotech · 2017Article
- Redox imbalance and mitochondrial abnormalities in the diabetic lung.Redox biology · 2017Article
- Sources and implications of NADH/NAD(+) redox imbalance in diabetes and its complications.Diabetes, metabolic syndrome and obesity : targets and therapy · 2016Review
- Formation of reactive oxygen species by human and bacterial pyruvate and 2-oxoglutarate dehydrogenase multienzyme complexes reconstituted from recombinant components.Free radical biology & medicine · 2015Article
- 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
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Dihydrolipoamide dehydrogenase (DLDH) is a multifunctional oxidoreductase and is well known as an essential component of four mammalian mitochondrial multienzyme complexes: pyruvate dehydrogenase, α-ketoglutarate dehydrogenase, branched chain α-keto acid dehydrogenase, and the glycine cleavage system. However, existence of extracellular DLDH in mammals, if any, has not been clearly defined. The present article reports identification and biochemical characterization of serum DLDH. Proteomic analysis of rat serum using blue native polyacrylamide gel electrophoresis (BN-PAGE) and mass spectrometry peptide sequencing led to generation of 6 tryptic peptides in one band that matched to mitochondrial DLDH, indicating the existence of DLDH in rat serum. Measurement of enzymatic activity also indicated the existence of DLDH in human and mouse serum. Further biochemical analysis of rat serum DLDH revealed that this enzyme lacked diaphorase activity and could not be detected on Western blots probed with antibodies that recognized mitochondrial DLDH. Moreover, both ammonium sulfate fractioning and gel filtration of serum samples rendered a great loss in DLDH activity, indicating that the enzyme activity of this serum protein, unlike that of mitochondrial DLDH, is very labile. When DTT was supplemented in the buffer used for gel filtration, DLDH activity was found to be largely preserved; indicating that serum DLDH is susceptible to air-implicated inactivation. Results of the present study indicate that serum DLDH differs from mitochondrial DLDH in that it is a very labile enzyme.
Indexed as
Identifiers
23646291PMC3641859W2135294344What 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.