Related Experiment Video
Updated: Sep 19, 2025

Resin-Assisted Capture Coupled with Isobaric Tandem Mass Tag Labeling for Multiplexed Quantification of Protein Thiol Oxidation
Published on: June 21, 2021
Oxidative stress in branched-chain organic acidemias using thiol-disulfide homeostasis
Emine Göksoy1,2, Burcu Kumru Akın3, Mehmet Keskin4
1Pediatric Metabolism Department, Cengiz Gokcek Children Hospital, Gaziantep, Türkiye.
Objectives:
Branched-chain organic acidemias (OAs) are inherited metabolic disorders resulting from enzyme deficiencies in the catabolic pathway of branched-chain amino acids, which could lead to mitochondrial dysfunction and oxidative stress. This study aimed to evaluate oxidative stress in OA patients using thiol-disulfide homeostasis (TDH) parameters.
Methods:
21 OA patients [methylmalonic acidemia (MMA), propionic acidemia (PA), and isovaleric acidemia] and 12 healthy controls participated in this study. TDH parameters such as native thiol, total thiol, and disulfide levels, in addition to Oxidative Stress Index, Total Antioxidant Status, and Total Oxidant Status were analyzed using spectrophotometry.
Results:
The OA group had significantly lower native (p=0.004) and total thiol (p=0.006) levels compared to controls. When analyzing subgroups, native thiols were found to be lower in MMA (p=0.012) and in PA (p=0.008) with elevated disulfides in MMA (p=0.003) in comparison to both PA and controls. As compared to abnormal neurodevelopmental status, there was a statistically significant relationship with lower native thiols and a shift towards oxidative stress (p=0.004).
Conclusions:
The parameters of the TDH are altered in patients with OA, especially in those with MMA and PA, indicating a significant level of oxidative stress. The neurodevelopmental outcome in OA may be exacerbated by this oxidative imbalance. The utilization of TDH as a biomarker may be a potential provider of oxidative status in OA patients and facilitate informing therapeutic strategies.
More Related Videos
10:24Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry
Published on: June 7, 2018
03:35Author Spotlight: Innovating Thiol Quantification and Biomarker Detection for Oxidative Stress Research
Published on: June 28, 2024
Related Concept Videos
Sulfur Assimilation
Preparation and Reactions of Thiols
Phase II Reactions: Glutathione Conjugation and Mercapturic Acid Formation
Several distinctive characteristics distinguish glutathione conjugation from other phase II...
Electron Transport Chain: Complex III and IV
Radical Autoxidation
Protein Modifications in the RER
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal...