The influence of carbohydrate-protein co-ingestion following endurance exercise on myofibrillar and mitochondrial protein synthesis.
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, VO2max 66.5 ± 5.1 ml kg(−1) min(−1)) completed two trials in a randomized order. Subjects cycled for 90 min at 77 ± 1% VO2max 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-(13)C6]phenylalanine began 1.5 h prior to exercise and continued until 4 h 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 4 h post-exercise (P < 0.05). p70S6K(Thr389) phosphorylation increased at 4 h post-exercise for C+P (P < 0.05), whilst eEF2(Thr56) phosphorylation increased by ∼40% at 4 h 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.
[show abstract] [hide abstract]
ABSTRACT: To determine whether relationships between skeletal muscle hybrid fiber composition and whole-body exercise patterns help to elucidate their transitional capacity or a fine-tuning response to functional demands. This study investigated hybrid fibers from vastus lateralis biopsies of runners (N= 13) and nonrunners (N = 9) and related hybrid fiber occurrence and distribution of myosin heavy-chain isoforms (MHC) within hybrid fibers to exercise patterns. MHC composition of single fibers was identified by SDS-PAGE. Runners had more fibers expressing only MHC I, fewer expressing MHC IIx, and fewer IIa/IIx hybrid fibers (P < 0.05). Hybrid IIa/IIx and I/IIa fibers were, respectively, negatively and positively related to training volume or average preferred racing distance (PRDA) in runners (P < 0.05). The relationship between IIa/IIx hybrid fibers and PRDA was more exponential (R(2) = 0.88) than linear (R(2) = 0.69). Only IIa/IIx hybrid fibers correlated negatively with exercise hours in nonrunners (P < 0.05). Their IIa/IIx hybrid fibers had MHC IIa content ranging from 1 to 99%, with most between 41 and 60%. Runners favoring longer distances (PRDA > 8 km or training > 70 km x wk(-1)) had no IIa/IIx hybrid fibers with MHC IIa proportion > 60%. In these runners, MHC I within hybrid I/IIa fibers was skewed toward higher proportions (> 60%), whereas MHC I proportions were skewed oppositely in runners favoring shorter training or racing distances. Training volume influences both IIa/IIx and I/IIa hybrid fiber proportions in runners, but only the former in nonrunners. Hybrid IIa/IIx fiber proportions were modulated by racing distance. Distinctly different distributions of MHC isoforms within the hybrid fibers were seen in runners favoring longer distances versus those favoring shorter distances.Medicine & Science in Sports & Exercise 11/2007; 39(11):1977-84. · 4.43 Impact Factor
Article: Differential stimulation of myofibrillar and sarcoplasmic protein synthesis with protein ingestion at rest and after resistance exercise.[show abstract] [hide abstract]
ABSTRACT: We aimed to determine whether there is a differential stimulation of the contractile myofibrillar and the cellular sarcoplasmic proteins after ingestion of protein and how this is affected by resistance exercise. Fasted (FAST) muscle protein synthesis was measured in seven healthy young men with a primed constant infusion of L-[ring-(13)C(6)]phenylalanine. Participants then performed an intense bout of unilateral resistance exercise followed by the consumption of 25 g of whey protein to maximally stimulate protein synthesis. In the rested (FED) leg myofibrillar (MYO) protein synthesis was elevated (P < 0.01) above FAST at 3 h (approximately 163%) but not at 1 and 5 h (P > 0.05). In contrast, MYO protein synthesis in the exercised (FED-EX) leg was stimulated above FAST at 1, 3 and 5 h (approximately 100, 216, and 229%, respectively; P < 0.01) with the increase at 5 h being greater than FED (P < 0.01). Thus, the synthesis of muscle contractile proteins is stimulated by both feeding and resistance exercise early (1 h) but has a greater duration and amplitude after resistance exercise. Sarcoplasmic (SARC) protein synthesis was similarly elevated (P < 0.01) above FAST by approximately 104% at 3 h in both FED and FED-EX suggesting SARC protein synthesis is stimulated by feeding but that this response is not augmented by resistance exercise. In conclusion, myofibrillar and sarcoplasmic protein synthesis are similarly, but transiently, stimulated with protein feeding. In contrast, resistance exercise rapidly stimulates and sustains the synthesis of only the myofibrillar protein fraction after protein ingestion. These data highlight the importance of measuring the synthetic response of specific muscle protein fractions when examining the effects of exercise and nutrition.The Journal of Physiology 01/2009; 587(Pt 4):897-904. · 4.72 Impact Factor
Article: Differential effects of resistance and endurance exercise in the fed state on signalling molecule phosphorylation and protein synthesis in human muscle.[show abstract] [hide abstract]
ABSTRACT: Resistance (RE) and endurance (EE) exercise stimulate mixed skeletal muscle protein synthesis. The phenotypes induced by RE (myofibrillar protein accretion) and EE (mitochondrial expansion) training must result from differential stimulation of myofibrillar and mitochondrial protein synthesis. We measured the synthetic rates of myofibrillar and mitochondrial proteins and the activation of signalling proteins (Akt-mTOR-p70S6K) at rest and after an acute bout of RE or EE in the untrained state and after 10 weeks of RE or EE training in young healthy men. While untrained, RE stimulated both myofibrillar and mitochondrial protein synthesis, 67% and 69% (P < 0.02), respectively. After training, only myofibrillar protein synthesis increased with RE (36%, P = 0.05). EE stimulated mitochondrial protein synthesis in both the untrained, 154%, and trained, 105% (both P < 0.05), but not myofibrillar protein synthesis. Acute RE and EE increased the phosphorylation of proteins in the Akt-mTOR-p70S6K pathway with comparatively minor differences between two exercise stimuli. Phosphorylation of Akt-mTOR-p70S6K proteins was increased after 10 weeks of RE training but not by EE training. Chronic RE or EE training modifies the protein synthetic response of functional protein fractions, with a shift toward exercise phenotype-specific responses, without an obvious explanatory change in the phosphorylation of regulatory signalling pathway proteins.The Journal of Physiology 06/2008; 586(Pt 15):3701-17. · 4.72 Impact Factor