![]() ![]() C, labeling kinetics of human HSP90B1 (endoplasmin) shown as an example of protein-level determination of k deg values. Blue and red colors indicate unlabeled and isotopically labeled spectra/cells, respectively. Colors indicate distinct orders and suborders. A, phylogenetic tree and maximal life spans of species analyzed in this study. Proteome-wide quantitation of k deg in mammalian fibroblasts. Protein turnove aging protein degradation proteostasis quantitative proteomics.Ĭopyright © 2021 The Authors. We suggest that in lieu of a rapid constitutive turnover, long-lived species may have evolved more energetically efficient mechanisms for selective detection and clearance of damaged proteins. Despite having slower rates of protein turnover, naked mole rat cells tolerate protein misfolding stress more effectively than mouse cells. In comparison with mice, cells from long-lived naked mole rats have slower rates of protein turnover, lower levels of ATP production, and reduced reactive oxygen species levels. We show that organismal life span is negatively correlated with turnover rates of highly abundant proteins. Here, we used a proteomic approach to measure rates of protein turnover within primary fibroblasts isolated from a number of species with diverse life spans including the longest-lived mammal, the bowhead whale. Thus, the relationship between aging, protein turnover, and energetic demand remains unclear. ![]() ![]() However, the high energetic demand of protein turnover generates reactive oxygen species that compromise the long-term health of the proteome. Cells continually degrade and replace damaged proteins. ![]()
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