Impact of local heating and cooling on skeletal muscle transcriptional response related to myogenesis and proteolysis

Zak, Roksana; Hassenstab, B. M.; Zuehlke, L. K.; Heesch, Matthew; Shute, Robert; Laursen, Terence; LaSalle, David Taylor; Slivka, Dustin

doi:10.1007/s00421-017-3749-z

“…signalling proteins that regulate protein translation-initiation (i.e. This is in line with a recent study showing that prolonged muscle cooling around resistance exercise does not change the gene expression of these markers of muscle protein breakdown compared to muscle heating (Zak et al 2018). Therefore, these findings with respect to anabolic signalling could not explain the differences we found in myofibrillar protein synthesis between the CWI and CON leg.…”

Section: Discussionsupporting

confidence: 87%

Post-exercise Cooling Impairs Muscle Protein Synthesis Rates In Healthy Young Males

Fuchs

¹

,

Kouw

²

,

Churchward‐Venne

³

et al. 2019

Medicine &Amp; Science in Sports &Amp; Exercise

View full text Add to dashboard Cite

Key points Protein ingestion and cooling are strategies employed by athletes to improve postexercise recovery and, as such, to facilitate muscle conditioning. However, whether cooling affects postprandial protein handling and subsequent muscle protein synthesis rates during recovery from exercise has not been assessed. We investigated the effect of postexercise cooling on the incorporation of dietary protein‐derived amino acids into muscle protein and acute postprandial (hourly) as well as prolonged (daily) myofibrillar protein synthesis rates during recovery from resistance‐type exercise over 2 weeks. Cold‐water immersion during recovery from resistance‐type exercise lowers the capacity of the muscle to take up and/or direct dietary protein‐derived amino acids towards de novo myofibrillar protein accretion. In addition, cold‐water immersion during recovery from resistance‐type exercise lowers myofibrillar protein synthesis rates during prolonged resistance‐type exercise training. Individuals aiming to improve skeletal muscle conditioning should reconsider applying cooling as a part of their postexercise recovery strategy. Abstract We measured the impact of postexercise cooling on acute postprandial (hourly) as well as prolonged (daily) myofibrillar protein synthesis rates during adaptation to resistance‐type exercise over 2 weeks. Twelve healthy males (aged 21 ± 2 years) performed a single resistance‐type exercise session followed by water immersion of both legs for 20 min. One leg was immersed in cold water (8°C: CWI), whereas the other leg was immersed in thermoneutral water (30°C: CON). After water immersion, a beverage was ingested containing 20 g of intrinsically (l‐[1‐13C]‐phenylalanine and l‐[1‐13C]‐leucine) labelled milk protein with 45 g of carbohydrates. In addition, primed continuous l‐[ring‐2H5]‐phenylalanine and l‐[1‐13C]‐leucine infusions were applied, with frequent collection of blood and muscle samples to assess myofibrillar protein synthesis rates in vivo over a 5 h recovery period. In addition, deuterated water (2H2O) was applied with the collection of saliva, blood and muscle biopsies over 2 weeks to assess the effects of postexercise cooling with protein intake on myofibrillar protein synthesis rates during more prolonged resistance‐type exercise training (thereby reflecting short‐term training adaptation). Incorporation of dietary protein‐derived l‐[1‐13C]‐phenylalanine into myofibrillar protein was significantly lower in CWI compared to CON (0.016 ± 0.006 vs. 0.021 ± 0.007 MPE; P = 0.016). Postexercise myofibrillar protein synthesis rates were lower in CWI compared to CON based upon l‐[1‐13C]‐leucine (0.058 ± 0.011 vs. 0.072 ± 0.017% h−1, respectively; P = 0.024) and l‐[ring‐2H5]‐phenylalanine (0.042 ± 0.009 vs. 0.053 ± 0.013% h−1, respectively; P = 0.025). Daily myofibrillar protein synthesis rates assessed over 2 weeks were significantly lower in CWI compared to CON (1.48 ± 0.17 vs. 1.67 ± 0.36% day−1, respectively; P = 0.042). Cold‐water immersion during recovery from resistance‐type e...

show abstract

“…This is in line with a recent study showing that prolonged muscle cooling around resistance exercise does not change the gene expression of these markers of muscle protein breakdown compared to muscle heating (Zak et al . ). In addition, it was recently shown that there were no clear effects of postexercise CWI on markers of muscle protein breakdown both before and after 7 weeks of resistance‐type exercise training (Fyfe et al .…”

Section: Discussionmentioning

confidence: 97%

Postexercise cooling impairs muscle protein synthesis rates in recreational athletes

Fuchs

¹

,

Kouw

²

,

Churchward‐Venne

³

et al. 2019

The Journal of Physiology

View full text Add to dashboard Cite

Key points Protein ingestion and cooling are strategies employed by athletes to improve postexercise recovery and, as such, to facilitate muscle conditioning. However, whether cooling affects postprandial protein handling and subsequent muscle protein synthesis rates during recovery from exercise has not been assessed. We investigated the effect of postexercise cooling on the incorporation of dietary protein‐derived amino acids into muscle protein and acute postprandial (hourly) as well as prolonged (daily) myofibrillar protein synthesis rates during recovery from resistance‐type exercise over 2 weeks. Cold‐water immersion during recovery from resistance‐type exercise lowers the capacity of the muscle to take up and/or direct dietary protein‐derived amino acids towards de novo myofibrillar protein accretion. In addition, cold‐water immersion during recovery from resistance‐type exercise lowers myofibrillar protein synthesis rates during prolonged resistance‐type exercise training. Individuals aiming to improve skeletal muscle conditioning should reconsider applying cooling as a part of their postexercise recovery strategy. Abstract We measured the impact of postexercise cooling on acute postprandial (hourly) as well as prolonged (daily) myofibrillar protein synthesis rates during adaptation to resistance‐type exercise over 2 weeks. Twelve healthy males (aged 21 ± 2 years) performed a single resistance‐type exercise session followed by water immersion of both legs for 20 min. One leg was immersed in cold water (8°C: CWI), whereas the other leg was immersed in thermoneutral water (30°C: CON). After water immersion, a beverage was ingested containing 20 g of intrinsically (l‐[1‐13C]‐phenylalanine and l‐[1‐13C]‐leucine) labelled milk protein with 45 g of carbohydrates. In addition, primed continuous l‐[ring‐2H5]‐phenylalanine and l‐[1‐13C]‐leucine infusions were applied, with frequent collection of blood and muscle samples to assess myofibrillar protein synthesis rates in vivo over a 5 h recovery period. In addition, deuterated water (2H2O) was applied with the collection of saliva, blood and muscle biopsies over 2 weeks to assess the effects of postexercise cooling with protein intake on myofibrillar protein synthesis rates during more prolonged resistance‐type exercise training (thereby reflecting short‐term training adaptation). Incorporation of dietary protein‐derived l‐[1‐13C]‐phenylalanine into myofibrillar protein was significantly lower in CWI compared to CON (0.016 ± 0.006 vs. 0.021 ± 0.007 MPE; P = 0.016). Postexercise myofibrillar protein synthesis rates were lower in CWI compared to CON based upon l‐[1‐13C]‐leucine (0.058 ± 0.011 vs. 0.072 ± 0.017% h−1, respectively; P = 0.024) and l‐[ring‐2H5]‐phenylalanine (0.042 ± 0.009 vs. 0.053 ± 0.013% h−1, respectively; P = 0.025). Daily myofibrillar protein synthesis rates assessed over 2 weeks were significantly lower in CWI compared to CON (1.48 ± 0.17 vs. 1.67 ± 0.36% day−1, respectively; P = 0.042). Cold‐water immersion during recovery from resistance‐type e...

show abstract

“…The gene expression of the IGF-1 isoforms IGF-1Ea, IGF-1Eb, and IGF-1Ec (also known as mechano growth factor) and the IGF-1 receptor increases acutely in skeletal muscle after resistance exercise (Psilander et al, 2003;McKay et al, 2008;Wilborn et al, 2009;Heinemeier et al, 2013). Among the negative regulators of muscle growth, muscle-specific RING finger (MuRF)-1 mRNA increases acutely (Louis et al, 2007;Drummond et al, 2008;Mascher et al, 2008;Reitelseder et al, 2014;Stefanetti et al, 2014;Zak et al, 2018), as does the expression of genes encoding various proteins in the ubiquitin−proteasome pathway (Mahoney et al, 2008). By contrast, myostatin expression decreases (Louis et al, 2007;Deldicque et al, 2008;Drummond et al, 2008;Mascher et al, 2008;Wilborn et al, 2009;Zak et al, 2018).…”

Section: Introductionmentioning

confidence: 99%

“…Among the negative regulators of muscle growth, muscle-specific RING finger (MuRF)-1 mRNA increases acutely (Louis et al, 2007;Drummond et al, 2008;Mascher et al, 2008;Reitelseder et al, 2014;Stefanetti et al, 2014;Zak et al, 2018), as does the expression of genes encoding various proteins in the ubiquitin−proteasome pathway (Mahoney et al, 2008). By contrast, myostatin expression decreases (Louis et al, 2007;Deldicque et al, 2008;Drummond et al, 2008;Mascher et al, 2008;Wilborn et al, 2009;Zak et al, 2018). Acute changes in the expression of atrogin-1 (also known as muscle atrophy F-box or F-box protein 32) (Louis et al, 2007;Deldicque et al, 2008;Mascher et al, 2008;Manini et al, 2011;Nader et al, 2014;Reitelseder et al, 2014;Stefanetti et al, 2014;Zak et al, 2018) and FoxO (Louis et al, 2007;Manini et al, 2011;Reitelseder et al, 2014;Stefanetti et al, 2014;Zak et al, 2018;Fyfe et al, 2019;Fuchs et al, 2020) in skeletal muscle after resistance exercise are more variable and time-dependent.…”

Section: Introductionmentioning

confidence: 99%

“…By contrast, myostatin expression decreases (Louis et al, 2007;Deldicque et al, 2008;Drummond et al, 2008;Mascher et al, 2008;Wilborn et al, 2009;Zak et al, 2018). Acute changes in the expression of atrogin-1 (also known as muscle atrophy F-box or F-box protein 32) (Louis et al, 2007;Deldicque et al, 2008;Mascher et al, 2008;Manini et al, 2011;Nader et al, 2014;Reitelseder et al, 2014;Stefanetti et al, 2014;Zak et al, 2018) and FoxO (Louis et al, 2007;Manini et al, 2011;Reitelseder et al, 2014;Stefanetti et al, 2014;Zak et al, 2018;Fyfe et al, 2019;Fuchs et al, 2020) in skeletal muscle after resistance exercise are more variable and time-dependent. The gene expression of growth arrest and DNA damage-inducible protein (GADD45) also increases acutely in skeletal muscle after eccentric exercise (Chen et al, 2003;Mahoney et al, 2008) and endurance exercise (Romero et al, 2016).…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

The Effects of Cold Water Immersion and Active Recovery on Molecular Factors That Regulate Growth and Remodeling of Skeletal Muscle After Resistance Exercise

Peake

¹

,

Markworth

²

,

Cumming

³

et al. 2020

View full text Add to dashboard Cite

Regular postexercise cooling attenuates muscle hypertrophy, yet its effects on the key molecular factors that regulate muscle growth and remodeling are not well characterized. In the present study, nine men completed two sessions of single-leg resistance exercise on separate days. On 1 day, they sat in cold water (10 • C) up to their waist for 10 min after exercise. On the other day, they exercised at a low intensity for 10 min after exercise. Muscle biopsies were collected from the exercised leg before, 2, 24, and 48 h after exercise in both trials. These muscle samples were analyzed to evaluate changes in genes and proteins involved in muscle growth and remodeling. Muscle-specific RING finger 1 mRNA increased at 2 h after both trials (P < 0.05), while insulin-like growth factor (IGF)-1 Ec, IGF-1 receptor, growth arrest and DNA damage-inducible protein 45, collagen type I alpha chain A, collagen type III alpha chain 1, laminin and tissue inhibitor of metallopeptidase 1 mRNA increased 24−48 h after both trials (P < 0.05). By contrast, atrogin-1 mRNA decreased at all time points after both trials (P < 0.05). Protein expression of tenascin C increased 2 h after the active recovery trial (P < 0.05), whereas FoxO3a protein expression decreased after both trials (P < 0.05). Myostatin mRNA and ubiquitin protein expression did not change after either trial. These responses were not significantly different between the trials. The present findings suggest that regular cold water immersion attenuates muscle hypertrophy independently of changes in factors that regulate myogenesis, proteolysis and extracellular matrix remodeling in muscle after exercise.

show abstract

Impact of local heating and cooling on skeletal muscle transcriptional response related to myogenesis and proteolysis

Abstract: These results suggest an impaired muscle growth response with local cold application compared to local heat application.

Cited by 20 publications

References 49 publications

Post-exercise Cooling Impairs Muscle Protein Synthesis Rates In Healthy Young Males

Post-exercise Cooling Impairs Muscle Protein Synthesis Rates In Healthy Young Males

Postexercise cooling impairs muscle protein synthesis rates in recreational athletes

The Effects of Cold Water Immersion and Active Recovery on Molecular Factors That Regulate Growth and Remodeling of Skeletal Muscle After Resistance Exercise

Contact Info

Product

Resources

About