Aging oxidation drives brain proteins into harmful condensates, study finds
An international research team that included Martín Hugo, a Serra Húnter lecturer in the Department of Biochemistry and Molecular Biology at the UAB, has described how two opposing chemical modifications of proteins, sulfenylation and persulfidation, regulate the behavior of key proteins in the brain during aging. The study was recently published in the journal Nature Structural & Molecular…
An international research team, including Martín Hugo from the University of Barcelona, has uncovered the role of protein oxidation in the aging brain's detrimental condensates. Published in Nature Structural & Molecular Biology, the study reveals that aging leads to an accumulation of protein oxidation, which drives the excessive condensation and aggregation of crucial brain proteins, such as synapsin 1 and G3BP2.
Persulfidation, a process controlled by hydrogen sulfide production, offers a counteracting effect by preserving protein fluidity and functionality. When the body's ability to produce hydrogen sulfide declines, proteins become trapped in an aberrant state, resulting in shorter lifespans and symptoms akin to neurodegeneration in mice.
Interestingly, compounds that boost hydrogen sulfide levels, like ergothioneine, can counteract this adverse effect, presenting a promising avenue for tackling age-related brain diseases. The research team has also created an interactive platform enabling users to explore the atlas of cysteine modifications across various ages and molecular pathways.
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