The influence of carbohydrate-protein co-ingestion following endurance exercise on myofibrillar and mitochondrial protein synthesis

Leigh Breen, Andrew Philp, Oliver C. Witard, Sarah R. Jackman, Anna Selby, Ken Smith, Keith Baar, Kevin D. Tipton

Research output: Contribution to journalArticlepeer-review

100 Scopus citations

Abstract

The aim of the present study was to determine mitochondrial and myofibrillar muscle protein synthesis (MPS) when carbohydrate (CHO) or carbohydrate plus protein (C+P) beverages were ingested following prolonged cycling exercise. The intracellular mechanisms thought to regulate MPS were also investigated. In a single-blind, cross-over study, 10 trained cyclists (age 29 ± 6 years, 66.5 ± 5.1 ml kg -1 min -1) completed two trials in a randomized order. Subjects cycled for 90 min at 77 ± 1% before ingesting a CHO (25 g of carbohydrate) or C+P (25 g carbohydrate + 10 g whey protein) beverage immediately and 30 min post-exercise. A primed constant infusion of l-[ring- 13C 6]phenylalanine began 1.5h prior to exercise and continued until 4h post-exercise. Muscle biopsy samples were obtained to determine myofibrillar and mitochondrial MPS and the phosphorylation of intracellular signalling proteins. Arterialized blood samples were obtained throughout the protocol. Plasma amino acid and urea concentrations increased following ingestion of C+P only. Serum insulin concentration increased more for C+P than CHO. Myofibrillar MPS was ∼35% greater for C+P compared with CHO (0.087 ± 0.007 and 0.057 ± 0.006%h -1, respectively; P= 0.025). Mitochondrial MPS rates were similar for C+P and CHO (0.082 ± 0.011 and 0.086 ± 0.018%h -1, respectively). mTOR Ser2448 phosphorylation was greater for C+P compared with CHO at 4h post-exercise (P < 0.05). p70S6K Thr389 phosphorylation increased at 4h post-exercise for C+P (P < 0.05), whilst eEF2 Thr56 phosphorylation increased by ∼40% at 4h post-exercise for CHO only (P < 0.01). The present study demonstrates that the ingestion of protein in addition to carbohydrate stimulates an increase in myofibrillar, but not mitochondrial, MPS following prolonged cycling. These data indicate that the increase in myofibrillar MPS for C+P could, potentially, be mediated through p70S6K, downstream of mTOR, which in turn may suppress the rise in eEF2 on translation elongation.

Original languageEnglish (US)
Pages (from-to)4011-4025
Number of pages15
JournalJournal of Physiology
Volume589
Issue number16
DOIs
StatePublished - Aug 2011

ASJC Scopus subject areas

  • Physiology

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