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Valine

Valine is an essential amino acid, meaning the body cannot produce it and must, therefore be provided by the diet. Valine is also one of the three unique branched-chain amino acids (BCAA) in that the liver does not metabolize them.

Valine is present in several different proteins, especially in many globulins. Valine plays a crucial role in tissue repair and muscle growth. Moreover, valine is a source of energy in glucose remodeling; it is a so-called glycogenic amino acid. Adequate dietary valine intake promotes normal cognitive performance and muscle coordination and improves emotional balance.

Dietary valine intake is important for the normal regeneration of hematopoietic stem cells. In hereditary sickle cell anemia, one amino acid in the red cell hemoglobin beta-globin protein is changed from glutamic acid to valine, which alters the protein structure so it doesn’t fold normally. This means substituting one amino acid with another can impair hemopoiesis.

Valine helps supply the muscles with glucose for energy production during intense physical activity. It is also involved in nitrogen transport into the muscles, allowing more oxygen and nutrients to be delivered for extended performance. A good balance is required because too high levels of valine are known to increase the amount of ammonia in the body and disrupt liver and kidney function.

The best dietary sources of valine include parmesan cheese, spirulina, game, soy protein, lamb and beef, turkey and chicken, pork, pumpkin seeds, fish and legumes. Valine is abundant in combination with other branched-chain amino acids.

Biostarks reference ranges for valine

  • Valine (Val-S): 230-460 umol/L

Scientific references:

  • National Center for Biotechnology Information (2021). PubChem Compound Summary for CID 6287, Valine. <https:// pubchem.ncbi.nlm.nih.gov/compound/L-valine>
  • Taya, Y. et al. (2016). Depleting dietary valine permits nonmyeloablative mouse hematopoietic stem cell transplantation. Science 354 (6316): 1152–1155.
  • Marengo-Rowe, A. (2006). Structure-function relations of human hemoglobins. Proceedings 19 (3): 239–245.
  • Nishihira, T. et al. (1988). Anti-cancer therapy with valine-depleted amino acid imbalance solution. The Tohoku Journal of Experimental Medicine 156 (3): 259–270.
  • Tsuda, Y., Iwasawa, K., & Yamaguchi, M. (2018). Acute supplementation of valine reduces fatigue during swimming exercise in rats. Bioscience, Biotechnology, and Biochemistry, 82(5), 856-861.
  • Hutchison, S. N., Zarghami, N. S., Cusick, P. K., Longenecker, J. B., & Haskell, B. E. (1983). The effect of valine deficiency on neutral amino acid patterns in plasma and brain of the rat. The Journal of nutrition, 113(11), 2164-2170.
  • NutritionData (2018). Foods highest in valine. <https://nutritiondata.self.com/foods-000088000000000000000.html> [cited: 15.12.2021]