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Proteomes 2016, 4(1), 12; doi:10.3390/proteomes4010012

On the Rate of Synthesis of Individual Proteins within and between Different Striated Muscles of the Rat

Research Institute for Sport and Exercise Sciences, Liverpool John Moores University, Liverpool, L3 3AF, UK
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Academic Editor: Jacek R. Wisniewski
Received: 16 February 2016 / Revised: 8 March 2016 / Accepted: 10 March 2016 / Published: 15 March 2016
(This article belongs to the Special Issue Striated Muscle Proteomics)
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Abstract

The turnover of muscle protein is responsive to different (patho)-physiological conditions but little is known about the rate of synthesis at the level of individual proteins or whether this varies between different muscles. We investigated the synthesis rate of eight proteins (actin, albumin, ATP synthase alpha, beta enolase, creatine kinase, myosin essential light chain, myosin regulatory light chain and tropomyosin) in the extensor digitorum longus, diaphragm, heart and soleus of male Wistar rats (352 ± 30 g body weight). Animals were assigned to four groups (n = 3, in each), including a control and groups that received deuterium oxide (2H2O) for 4 days, 7 days or 14 days. Deuterium labelling was initiated by an intraperitoneal injection of 10 μL/g body weight of 99.9% 2H2O-saline, and was maintained by administration of 5% (v/v) 2H2O in drinking water provided ad libitum. Homogenates of the isolated muscles were analysed by 2-dimensional gel electrophoresis and matrix-assisted laser desorption ionisation time of flight mass spectrometry. Proteins were identified against the SwissProt database using peptide mass fingerprinting. For each of the eight proteins investigated, the molar percent enrichment (MPE) of 2H and rate constant (k) of protein synthesis was calculated from the mass isotopomer distribution of peptides based on the amino acid sequence and predicted number of exchangeable C–H bonds. The average MPE (2.14% ± 0.2%) was as expected and was consistent across muscles harvested at different times (i.e., steady state enrichment was achieved). The synthesis rate of individual proteins differed markedly within each muscle and the rank-order of synthesis rates differed among the muscles studied. After 14 days the fraction of albumin synthesised (23% ± 5%) was significantly (p < 0.05) greater than for other muscle proteins. These data represent the first attempt to study the synthesis rates of individual proteins across a number of different striated muscles. View Full-Text
Keywords: deuterium oxide; stable isotope labelling; mass isotopomer distribution analysis; matrix-assisted laser desorption ionisation mass spectrometry; 2D gel electrophoresis; skeletal muscle; cardiac muscle; protein synthesis deuterium oxide; stable isotope labelling; mass isotopomer distribution analysis; matrix-assisted laser desorption ionisation mass spectrometry; 2D gel electrophoresis; skeletal muscle; cardiac muscle; protein synthesis
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

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MDPI and ACS Style

Hesketh, S.; Srisawat, K.; Sutherland, H.; Jarvis, J.; Burniston, J. On the Rate of Synthesis of Individual Proteins within and between Different Striated Muscles of the Rat. Proteomes 2016, 4, 12.

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