2004 Spring Meeting of the Wpsa Uk Branch Papers

Doherty, Mary K.; McClean, L; Edwards, Ian John; McCormack, Heather; McTeir, Lynn; Whitehead, C. C.; Gaskell, S J; Beynon, Robert J.

doi:10.1080/00071660410001698092

Cited by 9 publications

(1 citation statement)

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“…The relative isotope abundance of the amino acid precursor pool (RIA p ) is a critical parameter in any turnover study, and experimental acquisition of this parameter should be included in the experimental workflow. In whole animal models, the initial value of RIA p is zero, label is then introduced in the diet, and precursor incorporation into new protein during translation is monitored over time ( 16 , 23 ). Assessing the distribution of heavy label in peptides containing two possible instances of the stable isotope labeled residue, arising either from incompletely labeled precursors, by dilution of the precursor pool by endogenous degradation-derived amino acids, or arising from biosynthesis de novo , is an effective method to calculate the RIA of heavy label in the amino acid precursor pool ( 11 ).…”

Section: Methodsmentioning

confidence: 99%

Proteome Dynamics: Tissue Variation in the Kinetics of Proteostasis in Intact Animals

Hammond

Claydon

Simpson

et al. 2016

Molecular & Cellular Proteomics

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Understanding the role of protein turnover in the maintenance of proteostasis requires accurate measurements of the rates of replacement of proteins in complex systems, such as intact animals. Moreover, any investigation of allometric scaling of protein turnover is likely to include species for which fully annotated proteomes are not available. We have used dietary administration of stable isotope labeled lysine to assess protein turnover rates for proteins from four tissues in the bank vole, Myodes glareolus. The annotated genome for this species is not available, so protein identification was attained through cross-species matching to the mouse. For proteins for which confident identifications were derived, the pattern of lysine incorporation over 40 days was used to define the rate of synthesis of individual proteins in the four tissues. The data were heavily filtered to retain a very high quality dataset of turnover rates for 1088 proteins. Comparative analysis of the four tissues revealed different median rates of degradation (kidney: 0.099 days−1; liver 0.136 days−1; heart, 0.054 days−1, and skeletal muscle, 0.035 days−1). These data were compared with protein degradation rates from other studies on intact animals or from cells in culture and indicate that both cell type and analytical methodology may contribute to variance in turnover data between different studies. These differences were not only due to tissue-specific proteins but were reflected in gene products common to all tissues. All data are available via ProteomeXchange with identifier PXD002054.

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Section: Methodsmentioning

confidence: 99%