Concurrent resistance and aerobic exercise stimulates both myofibrillar and mitochondrial protein synthesis in sedentary middle-aged men

Donges, CE; Burd, NA; Duffield, R; Smith, GC; West, DWD; Short, MJ; Mackenzie, R; Plank, LD; Shepherd, PR; Phillips, SM; Edge, JA

Concurrent resistance and aerobic exercise stimulates both myofibrillar and mitochondrial protein synthesis in sedentary middle-aged men

Donges, CE Burd, NA Duffield, R

Smith, GC West, DWD Short, MJ Mackenzie, R Plank, LD Shepherd, PR Phillips, SM Edge, JA

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Publication Type:: Journal Article
Citation:: Journal of Applied Physiology, 2012, 112 (12), pp. 1992 - 2001
Issue Date:: 2012-06-15

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Field	Value	Language
dc.contributor.author	Donges, CE	en_US
dc.contributor.author	Burd, NA	en_US
dc.contributor.author	Duffield, R https://orcid.org/0000-0002-5641-1314	en_US
dc.contributor.author	Smith, GC	en_US
dc.contributor.author	West, DWD	en_US
dc.contributor.author	Short, MJ	en_US
dc.contributor.author	Mackenzie, R	en_US
dc.contributor.author	Plank, LD	en_US
dc.contributor.author	Shepherd, PR	en_US
dc.contributor.author	Phillips, SM	en_US
dc.contributor.author	Edge, JA	en_US
dc.date.issued	2012-06-15	en_US
dc.identifier.citation	Journal of Applied Physiology, 2012, 112 (12), pp. 1992 - 2001	en_US
dc.identifier.issn	8750-7587	en_US
dc.identifier.uri	http://hdl.handle.net/10453/32188
dc.description.abstract	We determined myofibrillar and mitochondrial protein fractional synthesis rates (FSR), intramuscular signaling protein phosphorylation, and mRNA expression responses after isolated bouts of resistance exercise (RE), aerobic exercise (AE), or in combination [termed concurrent exercise (CE)] in sedentary middle-aged men. Eight subjects (age = 53.3 ± 1.8 yr; body mass index = 29.4 ± 1.4 kg·m2) randomly completed 8 × 8 leg extension repetitions at 70% of one repetition-maximum, 40 min of cycling at 55% peak aerobic power output (AE), or (consecutively) 50% of the RE and AE trials (CE). Biopsies were obtained (during a primed, constant infusion of L-[ring-13C6]phenylalanine) while fasted, and at 1 and 4 h following postexercise ingestion of 20 g of protein. All trials increased mitochondrial FSR above fasted rates (RE = 1.3-fold; AE = 1.5; CE = 1.4; P < 0.05), although only CE (2.2) and RE (1.8) increased myofibrillar FSR (P < 0.05). At 1 h postexercise, phosphorylation of Akt on Ser473 (CE = 7.7; RE = 4.6) and Thr308 (CE = 4.4; RE = 2.9), and PRAS40 on Thr246 (CE = 3.8; AE = 2.5) increased (P < 0.05), with CE greater than AE for Akt Ser473-Thr308 and greater than RE for PRAS40 (P < 0.05). Despite increased phosphorylation of Akt-PRAS40, phosphorylation of mammalian target of rapamycin (Ser2448) remained unchanged (P > 0.05), while rpS6 (Ser 235/236) increased only in RE (10.4) (P < 0.05). CE and AE both resulted in increased peroxisome proliferator receptor-γ coactivator 1-α (PGC1α) expression at 1 h (CE = 2.9; AE = 2.8; P < 0.05) and 4 h (CE = 2.6; AE = 2.4) and PGC1β expression at 4 h (CE = 2.1; AE = 2.6; P < 0.05). These data suggest that CE-induced acute stimulation of myofibrillar and mitochondrial FSR, protein signaling, and mRNA expression are equivalent to either isolate mode (RE or AE). These results occurred without an interference effect on muscle protein subfractional synthesis rates, protein signaling, or mRNA expression. Copyright © 2012 the American Physiological Society.	en_US
dc.relation.ispartof	Journal of Applied Physiology	en_US
dc.relation.isbasedon	10.1152/japplphysiol.00166.2012	en_US
dc.subject.classification	Physiology	en_US
dc.subject.mesh	Myofibrils	en_US
dc.subject.mesh	Muscle, Skeletal	en_US
dc.subject.mesh	Humans	en_US
dc.subject.mesh	Carrier Proteins	en_US
dc.subject.mesh	Muscle Proteins	en_US
dc.subject.mesh	Heat-Shock Proteins	en_US
dc.subject.mesh	Mitochondrial Proteins	en_US
dc.subject.mesh	Transcription Factors	en_US
dc.subject.mesh	RNA, Messenger	en_US
dc.subject.mesh	Exercise	en_US
dc.subject.mesh	Protein Biosynthesis	en_US
dc.subject.mesh	Phosphorylation	en_US
dc.subject.mesh	Middle Aged	en_US
dc.subject.mesh	Male	en_US
dc.subject.mesh	Peroxisome Proliferator-Activated Receptor Gamma Coactivator 1-alpha	en_US
dc.subject.mesh	RNA-Binding Proteins	en_US
dc.title	Concurrent resistance and aerobic exercise stimulates both myofibrillar and mitochondrial protein synthesis in sedentary middle-aged men	en_US
dc.type	Journal Article
utslib.citation.volume	12	en_US
utslib.citation.volume	112	en_US
utslib.for	1106 Human Movement and Sports Sciences	en_US
utslib.for	06 Biological Sciences	en_US
utslib.for	11 Medical and Health Sciences	en_US
pubs.embargo.period	Not known	en_US
pubs.organisational-group	/University of Technology Sydney
pubs.organisational-group	/University of Technology Sydney/Faculty of Health
pubs.organisational-group	/University of Technology Sydney/Faculty of Health/Sports and Exercise Science
pubs.organisational-group	/University of Technology Sydney/Strength - CHSP - Health Services and Practice
utslib.copyright.status	closed_access
pubs.issue	12	en_US
pubs.publication-status	Published	en_US
pubs.volume	112	en_US

Abstract:

We determined myofibrillar and mitochondrial protein fractional synthesis rates (FSR), intramuscular signaling protein phosphorylation, and mRNA expression responses after isolated bouts of resistance exercise (RE), aerobic exercise (AE), or in combination [termed concurrent exercise (CE)] in sedentary middle-aged men. Eight subjects (age = 53.3 ± 1.8 yr; body mass index = 29.4 ± 1.4 kg·m2) randomly completed 8 × 8 leg extension repetitions at 70% of one repetition-maximum, 40 min of cycling at 55% peak aerobic power output (AE), or (consecutively) 50% of the RE and AE trials (CE). Biopsies were obtained (during a primed, constant infusion of L-[ring-13C6]phenylalanine) while fasted, and at 1 and 4 h following postexercise ingestion of 20 g of protein. All trials increased mitochondrial FSR above fasted rates (RE = 1.3-fold; AE = 1.5; CE = 1.4; P < 0.05), although only CE (2.2) and RE (1.8) increased myofibrillar FSR (P < 0.05). At 1 h postexercise, phosphorylation of Akt on Ser473 (CE = 7.7; RE = 4.6) and Thr308 (CE = 4.4; RE = 2.9), and PRAS40 on Thr246 (CE = 3.8; AE = 2.5) increased (P < 0.05), with CE greater than AE for Akt Ser473-Thr308 and greater than RE for PRAS40 (P < 0.05). Despite increased phosphorylation of Akt-PRAS40, phosphorylation of mammalian target of rapamycin (Ser2448) remained unchanged (P > 0.05), while rpS6 (Ser 235/236) increased only in RE (10.4) (P < 0.05). CE and AE both resulted in increased peroxisome proliferator receptor-γ coactivator 1-α (PGC1α) expression at 1 h (CE = 2.9; AE = 2.8; P < 0.05) and 4 h (CE = 2.6; AE = 2.4) and PGC1β expression at 4 h (CE = 2.1; AE = 2.6; P < 0.05). These data suggest that CE-induced acute stimulation of myofibrillar and mitochondrial FSR, protein signaling, and mRNA expression are equivalent to either isolate mode (RE or AE). These results occurred without an interference effect on muscle protein subfractional synthesis rates, protein signaling, or mRNA expression. Copyright © 2012 the American Physiological Society.

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