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Exercise alters and β-alanine combined with exercise augments histidyl dipeptide levels and scavenges lipid peroxidation products in human skeletal muscle

(2018) JOURNAL OF APPLIED PHYSIOLOGY. 125(6). p.1767-1778
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Abstract
Carnosine and anserine are dipeptides synthesized from histidine and β-alanine by carnosine synthase (ATPGD1). These dipeptides, present in high concentration in the skeletal muscle, form conjugates with lipid peroxidation products such as 4-hydroxy trans-2-nonenal (HNE). Although skeletal muscle levels of these dipeptides could be elevated by feeding β-alanine, it is unclear how these dipeptides and their conjugates are affected by exercise training with or without β-alanine supplementation. We recruited twenty physically active men, who were allocated to either β-alanine or placebo-feeding group matched for VO2 peak, lactate threshold, and maximal power (Wmax). Participants completed 2 weeks of conditioning phase followed by 1 week of exercise testing (CPET) and a single session followed by 6 weeks of high intensity interval training (HIIT). Analysis of muscle biopsies showed that the levels of carnosine and ATPGD1 expression were increased after CPET and decreased following a single session and 6 weeks of HIIT. Expression of ATPGD1 and levels of carnosine were increased upon β-alanine-feeding after CPET, while ATPGD1 expression decreased following a single session of HIIT. The expression of fiber type markers myosin heavy chain (MHC) I and IIa remained unchanged after CPET. Levels of carnosine, anserine, carnosine-HNE, carnosine-propanal and carnosine-propanol were further increased after 9 weeks of β-alanine supplementation and exercise training, but remained unchanged in the placebo-fed group. These results suggest that carnosine levels and ATPGD1 expression fluctuates with different phases of training. Enhancing carnosine levels by β-alanine feeding could facilitate the detoxification of lipid peroxidation products in the human skeletal muscle.
Keywords
Exercise Physiology and Sport Nutrition, acrolein, carnosine, exercise, 4-hydroxy-trans-2-nonenal, CARNOSINE CONTENT, ANTIOXIDANT STATUS, ALDOSE REDUCTASE, VASTUS LATERALIS, SUPPLEMENTATION, METABOLISM, DAMAGE, ACROLEIN, IDENTIFICATION, ANSERINE

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Citation

Please use this url to cite or link to this publication:

Chicago
Hoetker, David, Weiliang Chung, Deqing Zhang, Jingjing Zhao, Virginia K Schmidtke, Daniel W Riggs, Wim Derave, Aruni Bhatnagar, David Bishop, and Shahid P Baba. 2018. “Exercise Alters and Β-alanine Combined with Exercise Augments Histidyl Dipeptide Levels and Scavenges Lipid Peroxidation Products in Human Skeletal Muscle.” Journal of Applied Physiology 125 (6): 1767–1778.
APA
Hoetker, D., Chung, W., Zhang, D., Zhao, J., Schmidtke, V. K., Riggs, D. W., Derave, W., et al. (2018). Exercise alters and β-alanine combined with exercise augments histidyl dipeptide levels and scavenges lipid peroxidation products in human skeletal muscle. JOURNAL OF APPLIED PHYSIOLOGY, 125(6), 1767–1778.
Vancouver
1.
Hoetker D, Chung W, Zhang D, Zhao J, Schmidtke VK, Riggs DW, et al. Exercise alters and β-alanine combined with exercise augments histidyl dipeptide levels and scavenges lipid peroxidation products in human skeletal muscle. JOURNAL OF APPLIED PHYSIOLOGY. 2018;125(6):1767–78.
MLA
Hoetker, David et al. “Exercise Alters and Β-alanine Combined with Exercise Augments Histidyl Dipeptide Levels and Scavenges Lipid Peroxidation Products in Human Skeletal Muscle.” JOURNAL OF APPLIED PHYSIOLOGY 125.6 (2018): 1767–1778. Print.
@article{8589559,
  abstract     = {Carnosine and anserine are dipeptides synthesized from histidine and β-alanine by carnosine synthase (ATPGD1). These dipeptides, present in high concentration in the skeletal muscle, form conjugates with lipid peroxidation products such as 4-hydroxy trans-2-nonenal (HNE). Although skeletal muscle levels of these dipeptides could be elevated by feeding β-alanine, it is unclear how these dipeptides and their conjugates are affected by exercise training with or without β-alanine supplementation. We recruited twenty physically active men, who were allocated to either β-alanine or placebo-feeding group matched for VO2 peak, lactate threshold, and maximal power (Wmax). Participants completed 2 weeks of conditioning phase followed by 1 week of exercise testing (CPET) and a single session followed by 6 weeks of high intensity interval training (HIIT). Analysis of muscle biopsies showed that the levels of carnosine and ATPGD1 expression were increased after CPET and decreased following a single session and 6 weeks of HIIT. Expression of ATPGD1 and levels of carnosine were increased upon β-alanine-feeding after CPET, while ATPGD1 expression decreased following a single session of HIIT. The expression of fiber type markers myosin heavy chain (MHC) I and IIa remained unchanged after CPET. Levels of carnosine, anserine, carnosine-HNE, carnosine-propanal and carnosine-propanol were further increased after 9 weeks of β-alanine supplementation and exercise training, but remained unchanged in the placebo-fed group. These results suggest that carnosine levels and ATPGD1 expression fluctuates with different phases of training. Enhancing carnosine levels by β-alanine feeding could facilitate the detoxification of lipid peroxidation products in the human skeletal muscle.},
  author       = {Hoetker, David and Chung, Weiliang and Zhang, Deqing and Zhao, Jingjing and Schmidtke, Virginia K and Riggs, Daniel W and Derave, Wim and Bhatnagar, Aruni and Bishop, David and Baba, Shahid P},
  issn         = {8750-7587},
  journal      = {JOURNAL OF APPLIED PHYSIOLOGY},
  keywords     = {Exercise Physiology and Sport Nutrition,acrolein,carnosine,exercise,4-hydroxy-trans-2-nonenal,CARNOSINE CONTENT,ANTIOXIDANT STATUS,ALDOSE REDUCTASE,VASTUS LATERALIS,SUPPLEMENTATION,METABOLISM,DAMAGE,ACROLEIN,IDENTIFICATION,ANSERINE},
  language     = {eng},
  number       = {6},
  pages        = {1767--1778},
  title        = {Exercise alters and β-alanine combined with exercise augments histidyl dipeptide levels and scavenges lipid peroxidation products in human skeletal muscle},
  url          = {http://dx.doi.org/10.1152/japplphysiol.00007.2018},
  volume       = {125},
  year         = {2018},
}

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