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. 2024 Jul 19;22(7):322.
doi: 10.3390/md22070322.

Systematical Investigation on Anti-Fatigue Function and Underlying Mechanism of High Fischer Ratio Oligopeptides from Antarctic Krill on Exercise-Induced Fatigue in Mice

Sha-Yi Mao  1 , Shi-Kun Suo  1 , Yu-Mei Wang  1 , Chang-Feng Chi  2 , Bin Wang  1
Affiliations

Systematical Investigation on Anti-Fatigue Function and Underlying Mechanism of High Fischer Ratio Oligopeptides from Antarctic Krill on Exercise-Induced Fatigue in Mice

Sha-Yi Mao et al. Mar Drugs. .

Abstract

High Fischer ratio oligopeptides (HFOs) have a variety of biological activities, but their mechanisms of action for anti-fatigue are less systematically studied at present. This study aimed to systematically evaluate the anti-fatigue efficacy of HFOs from Antarctic krill (HFOs-AK) and explore its mechanism of action through establishing the fatigue model of endurance swimming in mice. Therefore, according to the comparison with the endurance swimming model group, HFOs-AK were able to dose-dependently prolong the endurance swimming time, reduce the levels of the metabolites (lactic acid, blood urea nitrogen, and blood ammonia), increase the content of blood glucose, muscle glycogen, and liver glycogen, reduce lactate dehydrogenase and creatine kinase extravasation, and protect muscle tissue from damage in the endurance swimming mice. HFOs-AK were shown to enhance Na+-K+-ATPase and Ca2+-Mg2+-ATPase activities and increase ATP content in muscle tissue. Meanwhile, HFOs-AK also showed significantly antioxidant ability by increasing the activities of superoxide dismutase and glutathione peroxidase in the liver and decreasing the level of malondialdehyde. Further studies showed that HFOs-AK could regulate the body's energy metabolism and thus exert its anti-fatigue effects by activating the AMPK signaling pathway and up-regulating the expression of p-AMPK and PGC-α proteins. Therefore, HFOs-AK can be used as an auxiliary functional dietary molecules to exert its good anti-fatigue activity and be applied to anti-fatigue functional foods.

Keywords: Antarctic krill (Euphausia superba); anti-fatigue; high Fischer ratio oligopeptides (HFO); in vivo metabolites; oxidative stress.

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Conflict of interest statement

The authors declare no conflicts of interest.

Figures

Figure 1
Figure 1
H&E staining of mouse liver tissue samples. The fatigue model of mice was established by an endurance swimming method. Whey peptides (0.5 mg/g·bw/d) served as a positive control. (A) Blank; (B) Model; (C) Whey peptides (0.5 mg/g·bw/d); (D) Low-dose of HFOs-AK (0.1 mg/g·bw/d); (E) Mid-dose of HFOs-AK (0.3 mg/g·bw/d); (F) High-dose of HFOs-AK (0.5 mg/g·bw/d). The yellow arrow indicates the hepatic sinusoids, and the red arrow indicates the hepatic cord.
Figure 2
Figure 2
H&E staining of mouse muscle tissue samples. Whey peptides (0.5 g/g·bw/d) served as a positive control. (A) Blank; (B) Model; (C) Whey peptides (0.5 mg/g·bw/d); (D) Low-dose of HFOs-AK (0.1 mg/g·bw/d); (E) Mid-dose of HFOs-AK (0.3 mg/g·bw/d); (F) High-dose of HFOs-AK (0.5 mg/g·bw/d). The red arrows in the diagram indicate damage and irregular alignment of the gastrocnemius muscles of mice.
Figure 3
Figure 3
Effect of HFOs-AK on exercise capacity (A) and in vivo metabolites of BUN (B), LA (C), and BA (D) in fatigue model of mice. Whey peptides (0.5 g/g·bw/d) served as a positive control. *** p < 0.001 compared to blank control group. ### p < 0.001, ## p < 0.01 and # p < 0.05 compared to model group.
Figure 4
Figure 4
Effect of HFOs-AK on LDH (A) and CK (B) activity in fatigue model of mice. Whey peptides (0.5 g/g·bw/d) served as a positive control. *** p < 0.001 and ** p < 0.01 compared to blank control group. ## p < 0.01 and # p < 0.05 compared to model group.
Figure 5
Figure 5
Effect of HFOs-AK on the contents of BG (A), MG (B), and LG (C) in fatigue model of mice. Whey peptides (0.5 g/g·bw/d) served as a positive control. *** p < 0.001 and * p < 0.05 compared to blank control group. ### p < 0.001, ## p < 0.01 and # p < 0.05 compared to model group.
Figure 6
Figure 6
Effect of HFOs-AK on ATP content (A), Na+-K+-ATPase (B) and Ca2+-Mg2+-ATPase (C) activities in fatigue mice. Whey peptides (0.5 g/g·bw/d) served as a positive control. *** p < 0.001 and * p < 0.05 compared to blank control group. ### p < 0.001 and # p < 0.05 compared to model group.
Figure 7
Figure 7
Effect of HFOs-AK on MDA (A) content, and SOD (B) and GSH-Px (C) activities in fatigue model of mice. Whey peptides (0.5 g/g·bw/d) served as a positive control. *** p < 0.001 compared to blank control group. ### p < 0.001, ## p < 0.01 and # p < 0.05 compared to model group.
Figure 8
Figure 8
Protein map of HFOs-AK on anti-fatigue signaling pathway in mice (A). Effect of HFOs-AK on expression levels of p-AMPK (B), PGC-1α (C), and Nrf2 (D) protein in mice. Whey peptides (0.5 g/g·bw/d) served as a positive control. *** p < 0.001 compared to blank control group. ### p < 0.001 compared to model group.
Figure 9
Figure 9
Anti-fatigue mechanisms of HFOs-AK on fatigue model of mice. The blue arrows in the chart indicate that the data is trending downward. The green arrows in the chart indicate that the data is trending upwards. The red arrows in the diagram indicate damage and irregular alignment of the gastrocnemius muscles of mice.
See this image and copyright information in PMC

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