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Endogenous skeletal muscle antioxidants

Chan, Kin M., Decker, Eric A., Feustman, Cameron·1994·Critical Reviews in Food Science and Nutrition
DOI 10.1080/10408399409527669
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Abstract

Skeletal muscle is susceptible to oxidative deterioration due to a combination of lipid oxidation catalysts and membrane lipid systems that are high in unsaturated fatty acids. To prevent or delay oxidation reactions, several endogenous antioxidant systems are found in muscle tissue. These include alpha-tocopherol, histidine-containing dipeptides, and antioxidant enzymes such as glutathione peroxidase, superoxide dismutase, and catalase. The contribution of alpha-tocopherol to the oxidative stability of skeletal muscle is largely influenced by diet. Dietary supplementation of tocopherol has been shown to increase muscle alpha-tocopherol concentrations and inhibit both lipid oxidation and color deterioration. Dietary selenium supplementation has also been shown to increase the oxidative stability of muscle presumably by increasing the activity of glutathione peroxidase. The oxidative stability of skeletal muscle is also influenced by the histidine-containing dipeptides, carnosine and anserine. Whereas carnosine and anserine are affected by diet less than alpha-tocopherol and glutathione peroxidase, their concentrations vary widely with species and muscle type. In pigs, beef, and turkey muscle, carnosine concentrations are greater than anserine, while the opposite is true in rabbit, salmon, and chicken muscle. Anserine and carnosine are found in greater concentrations in muscle high in white fibers, with chicken white muscle containing over fivefold more anserine and carnosine than red muscle. Anserine and carnosine are thought to inhibit lipid oxidation by a combination of free radical scavenging and metal chelation.

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Metadata

Authors
Chan, K. M., Decker, E. A., & Feustman, C.
Venue
Critical Reviews in Food Science and Nutrition
Publisher
Informa UK Limited
Published
1994-07
Volume
34
Issue
4
Pages
403-426
ISSN
  • 1040-8398 (ISSN-L)
  • 1549-7852
DOI
10.1080/10408399409527669
OpenAlex
W2085477560
Cited by
439
References
4
FWCI
9.54
Type
journal article
Language
en
Open access
closed

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