Proteins undergo post-translational modifications (PTMs) such as phosphorylation, ubiquitination, acetylation, and methylation. These modifications play essential roles for numerous biological functions, including signalling, regulation, protein activity, and gene expression control. The pathological development of many neurological diseases is known to be influenced by PTM dysregulation. Accurate identification and characterisation of these modifications are critical for a comprehensive understanding of cellular biology and the mechanisms underlying these diseases. A recent study in Biomeditsinskaya Khimiya (Biomedical Chemistry) dives deeper into the involvements of PTMs in the pathogenesis of Temporal Lobe Epilepsy (TLE) in adults.
To achieve this, Miroshnichenko et al. harnessed the power of PEAKS Studio to conduct a comparative proteome analysis of hippocampal tissue from patients with sclerotic and non-sclerotic temporal lobe epilepsy, as well as nonepileptic controls, to uncover differences in protein PTM levels. Thanks to PEAKS advanced PTM algorithm, which takes advantage of de novo partial tags, researchers were able to specify physiological PTMs, such as methylation of KRH, acetylation of K, acetylation of Protein N-terminal peptide, and citrullination of N in addition to more common oxidation of M and STY phosphorylation, without a significant effect on the search space. This allowed them to uncover deeper biological insight into the mechanism of pathological change in TLE. Scientists identified 53 proteins with significant changes in the levels of post-translational modifications linked to neurological disease pathways and epileptogenesis. By identifying site-specific PTMs, this study highlights molecular alterations that could serve as potential biomarkers for disease progression.
Read the full article here: Miroshnichenko, Yu. V., Rybina, A. V., Skvortsov, V. S. (2025). Identification of proteins with variable levels of post-translational modifications in human temporal lobe epilepsy. Biomeditsinskaya Khimiya, 71(5), 351-363. doi:10.18097/PBMCR1612