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

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

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Hammond, Dean E. Claydon, Amy J. Simpson, Deborah M. Edward, Dominic Stockley, Paula Hurst, Jane L. Beynon, Robert J.
Description	Author Affiliation: Hammond DE ( From the Centre for Proteome Research, Institute of Integrative Biology, University of Liverpool, Crown Street, L697ZB, UK); Claydon AJ ( From the Centre for Proteome Research, Institute of Integrative Biology, University of Liverpool, Crown Street, L697ZB, UK); Simpson DM ( From the Centre for Proteome Research, Institute of Integrative Biology, University of Liverpool, Crown Street, L697ZB, UK); Edward D ( §Mammalian Behaviour and Evolution Group, Institute of Integrative Biology, University of Liverpool, Leahurst Campus, Neston, CH64 7TE, UK.); Stockley P ( §Mammalian Behaviour and Evolution Group, Institute of Integrative Biology, University of Liverpool, Leahurst Campus, Neston, CH64 7TE, UK.); Hurst JL ( §Mammalian Behaviour and Evolution Group, Institute of Integrative Biology, University of Liverpool, Leahurst Campus, Neston, CH64 7TE, UK.); Beynon RJ ( From the Centre for Proteome Research, Institute of Integrative Biology, University of Liverpool, Crown Street, L697ZB, UK)
Abstract	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.
File Format	HTM / HTML
ISSN	15359476
e-ISSN	15359484
DOI	10.1074/mcp.M115.053488
Journal	Molecular & Cellular Proteomics
Issue Number	4
Volume Number	15
Language	English
Publisher	American Society for Biochemistry and Molecular Biology
Publisher Date	2016-04-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Discipline Proteomics
Content Type	Text
Resource Type	Article
Subject	Medicine Analytical Chemistry Molecular Biology Biochemistry

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

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

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