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Review
. 2023 Dec 31;14(1):28.
doi: 10.3390/metabo14010028.

The Role of Amino Acids in Non-Enzymatic Antioxidant Mechanisms in Cancer: A Review

Elena I Dyachenko  1 , Lyudmila V Bel'skaya  1
Affiliations
Review

The Role of Amino Acids in Non-Enzymatic Antioxidant Mechanisms in Cancer: A Review

Elena I Dyachenko et al. Metabolites. .

Abstract

Currently, the antioxidant properties of amino acids and their role in the physicochemical processes accompanying oxidative stress in cancer remain unclear. Cancer cells are known to extensively uptake amino acids, which are used as an energy source, antioxidant precursors that reduce oxidative stress in cancer, and as regulators of inhibiting or inducing tumor cell-associated gene expression. This review examines nine amino acids (Cys, His, Phe, Met, Trp, Tyr, Pro, Arg, Lys), which play a key role in the non-enzymatic oxidative process in various cancers. Conventionally, these amino acids can be divided into two groups, in one of which the activity increases (Cys, Phe, Met, Pro, Arg, Lys) in cancer, and in the other, it decreases (His, Trp, Tyr). The review examines changes in the metabolism of nine amino acids in eleven types of oncology. We have identified the main nonspecific mechanisms of changes in the metabolic activity of amino acids, and described direct and indirect effects on the redox homeostasis of cells. In the future, this will help to understand better the nature of life of a cancer cell and identify therapeutic targets more effectively.

Keywords: amino acids; cancer; non-enzymatic antioxidant system; oxidative stress.

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Conflict of interest statement

The authors declare no conflicts of interest.

Figures

Figure 1
Figure 1
Arg and its participation in redox regulation. NO—nitric oxide; VEGF—vascular endothelial growth factor. The plus sign indicates the induction force; the arrow indicates the magnification force.
Figure 2
Figure 2
Suppression of the content of certain radicals due to Trp. NAD—nicotinamide adenine dinucleotide. The plus sign indicates the induction force; crosses indicate suppression.
Figure 3
Figure 3
Activation of cell cytolysis due to the interaction of His and hydrogen peroxide.
Figure 4
Figure 4
The role of Tyr in the activation of cell apoptosis.
Figure 5
Figure 5
Participation of Met and His in the redox process. MetO—methyl sulfoxide; GSH—glutathione. The plus symbol indicates potentiation of the synthesis of glutathione and methylsulfoxide.
Figure 6
Figure 6
Participation of Pro in the redox process. ROS—Reactive oxygen species; NADPH—nicotinamide adenine dinucleotide phosphate; the plus symbol indicates an increase in the effect.
Figure 7
Figure 7
The role of Lys in redox homeostasis. DNA—deoxyribonucleic acid; NADPH—nicotinamide adenine dinucleotide phosphate; NOS—nitrogen–oxygen–sulfur bridge.
Figure 8
Figure 8
The effect of excess accumulation of Phe on the redox balance.
See this image and copyright information in PMC

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References

    1. Isenberg J.S., Martin-Manso G., Maxhimer J.B., Roberts D.D. Regulation of nitric oxide signalling by thrombospondin 1: Implications for anti-angiogenic therapies. Nat. Rev. Cancer. 2009;9:182–194. doi: 10.1038/nrc2561. - DOI - PMC - PubMed
    1. Fukumura D., Kashiwagi S., Jain R.K. The role of nitric oxide in tumour progression. Nat. Rev. Cancer. 2006;6:521–534. doi: 10.1038/nrc1910. - DOI - PubMed
    1. Wu G., Bazer F.W., Burghardt R.C., Johnson G.A., Kim S.W., Knabe D.A., Li P., Li X., McKnight J.R., Satterfield M.C., et al. Proline and hydroxyproline metabolism: Implications for animal and human nutrition. Amino Acids. 2011;40:1053–1063. doi: 10.1007/s00726-010-0715-z. - DOI - PMC - PubMed
    1. Wensien M., von Pappenheim F.R., Funk L.M., Kloskowski P., Curth U., Diederichsen U., Uranga J., Ye J., Fang P., Pan K.T., et al. A lysine-cysteine redox switch with an NOS bridge regulates enzyme function. Nature. 2021;593:460–464. doi: 10.1038/s41586-021-03513-3. - DOI - PubMed
    1. Coleman C.S., Stanley B.A., Pegg A.E. Effect of mutations at active site residues on the activity of ornithine decarboxylase and its inhibition by active site-directed irreversible inhibitors. J. Biol. Chem. 1993;268:24572–24579. doi: 10.1016/S0021-9258(19)74505-0. - DOI - PubMed

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