Protein Carbonyl Content Assay Kit

Supplementary info

This supplementary information is collated from multiple sources and compiled automatically.

Activity summary

Protein carbonyls also known as carbonylated proteins serve as key markers for oxidative stress. They possess a carbonyl group introduced through oxidative modification of susceptible amino acid residues like lysine threonine proline and arginine. Protein carbonyls have no specific mass due to their varied formation but are widely detected across many cellular proteins. Carbonylation prominently expresses itself in intracellular and extracellular proteins affecting many tissues and organs. Laboratories often use the DNPH (dinitrophenylhydrazine) assay and other protein carbonylation assays to detect and quantify these modifications.

Biological function summary

Protein carbonylation alters protein function and structure. This process disrupts protein-protein interactions and impairs enzyme activity leading to protein dysfunction. Carbonylated proteins fail to perform effectively within cellular systems and accumulate in cells. These accumulations can form large aggregates which cells often recognize as damaged. Protein degradation systems struggle to efficiently degrade these aggregates which can lead to further cellular dysfunction.

Pathways

Protein carbonylation integrates into the oxidative stress response pathways. In particular it affects the proteostasis network by challenging the protein quality control systems which include chaperones and proteasomes. This can influence pathways like the ubiquitin-proteasome pathway as proteins like ubiquitin tag damaged proteins for degradation. Additionally carbonylated proteins intertwined with inflammatory pathways interact with proteins such as nuclear factor kappa B (NF-kB) contributing to pro-inflammatory signaling.

Associated diseases and disorders

Protein carbonyls associate closely with neurodegenerative diseases like Alzheimer's disease and Parkinson's disease. The increase in oxidative stress in these conditions leads to the accumulation of carbonylated proteins which correlate with disease progression. In Alzheimer's disease oxidative damage results in the carbonylation of the amyloid precursor protein enhancing amyloid-beta accumulation. In Parkinson’s disease alpha-synuclein undergoes carbonylation promoting its aggregation into Lewy bodies. These protein associations highlight the significant role of protein carbonyls in disease pathology.