One of the most important irreversible oxidative modifications of proteins is carbonylation, the process of introducing a carbonyl group in reaction with reactive oxygen species. Notably, carbonylation increases with the age of cells and is associated with the formation of intracellular protein aggregates and the pathogenesis of age-related disorders such as neurodegenerative diseases and cance...

Elevated oxidative stress in Down syndrome due to elevated levels of superoxide dismutase 1 can be assessed by estimating the products of lipid peroxidation malondialdehyde and protein carbonylation .The present study included 31 clinically diagnosed and karyotypically confirmed Down syndrome children with equal number of age and sex matched controls. The levels of malondialdehyde (6.1 ± 2.5 μm...

Protein carbonylation is one of the most pervasive oxidative stress-induced post-translational modifications (PTMs), which plays a significant role in the etiology and progression of several human diseases. It has been regarded as a biomarker of oxidative stress due to its relatively early formation and stability compared with other oxidative PTMs. Only a subset of proteins is prone to carbonyl...

A recent proteomics analysis from our laboratory demonstrated that several oxidative stress response proteins showed significant changes in steady-state levels in olfactory bulbs (OBs) of 20- vs. 1.5-month-old mice. Oxidative stress may result in protein oxidation. In this study, we investigated two forms of protein oxidative modification in murine OBs: carbonylation and nitration. Redox proteo...

Oxidative modifications of enzymes and structural proteins play a significant role in the aetiology and/or progression of several human diseases. Protein carbonyl content is the most general and well-used biomarker of severe oxidative protein damage. Human diseases associated with protein carbonylation include Alzheimer's disease, chronic lung disease, chronic renal failure, diabetes and sepsis...

BACKGROUND Carbonyl derivatives are mainly formed by direct metal-catalysed oxidation (MCO) attacks on the amino-acid side chains of proline, arginine, lysine and threonine residues. For reasons unknown, only some proteins are prone to carbonylation. METHODOLOGY/PRINCIPAL FINDINGS we used mass spectrometry analysis to identify carbonylated sites in: BSA that had undergone in vitro MCO, and 23...

It has been observed protein carbonylation and glycation in the lens epithelial cell fractions of lenses in people with mature cataract. We used lenses of diabetic patients, weak and strong cigarette smokers and people who had senile cataract. The protein glycation is the highest in a diabetic senile cataract patients and the lowest in non-diabetic senile cataract patients. The protein carbonyl...