Degradation of ribosomal and chaperone proteins is attenuated during the differentiation of replicatively aged C2C12 myoblasts

Autor: Alexander D. Brown, Claire E. Stewart, Jatin G. Burniston
Jazyk: angličtina
Rok vydání: 2022
Předmět:
Zdroj: Journal of Cachexia, Sarcopenia and Muscle, Vol 13, Iss 5, Pp 2562-2575 (2022)
Druh dokumentu: article
ISSN: 2190-6009
2190-5991
DOI: 10.1002/jcsm.13034
Popis: Abstract Background Cell assays are important for investigating the mechanisms of ageing, including losses in protein homeostasis and ‘proteostasis collapse’. We used novel isotopic labelling and proteomic methods to investigate protein turnover in replicatively aged (>140 population doublings) murine C2C12 myoblasts that exhibit impaired differentiation and serve as a model for age‐related declines in muscle homeostasis. Methods The Absolute Dynamic Profiling Technique for Proteomics (Proteo‐ADPT) was used to investigate proteostasis in young (passage 6–10) and replicatively aged (passage 48–50) C2C12 myoblast cultures supplemented with deuterium oxide (D2O) during early (0–24 h) or late (72–96 h) periods of differentiation. Peptide mass spectrometry was used to quantify the absolute rates of abundance change, synthesis and degradation of individual proteins. Results Young cells exhibited a consistent ~25% rise in protein accretion over the 96‐h experimental period. In aged cells, protein accretion increased by 32% (P
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