Changes

==Roles in the Body==

==Roles in the Body==

Isoleucine, leucine and valine are constituents of [[Protein Overview - Nutrition|protein]]. Leucine is also a key catabolic regulator of l branched-chain amino acids<ref name="Harris">Harris RA, et al. Regulation of branched-chain α-keto acid dehydrogenase kinase expression in rat liver. J Nutr 2001;131:841S-845S.</ref>. Leucine also influences protein synthesis and muscle deposition by increasing plasma insulin secretion<ref>Yang J, et al. Leucine metabolism in regulation of insulin secretion from pancreatic beta cells. Nutr Rev 2010;68:270-279.</ref>, sensitivity of insulin binding to muscle cells<ref>Prod’homme M, et al. Insulin and amino acids both strongly participate to the regulation of protein metabolism. Curr Opin Clin Nutr Met Car 2004;7:71-7.</ref><ref>Anthony JC, et al. Contribution of insulin to the translational control of protein synthesis in skeletal muscle by leucine. Am J Physiol Endo Metab 2002;282:E1092-E1101.</ref><ref>Liu H, et al. Leucine facilitates the insulin-stimulated glucose uptake and insulin signalling in skeletal muscle cells: involving mTORC1 and mTORC2. Amino Acids 2014;46:1971-1979.</ref>, and inhibiting muscle catabolism<ref>Nagasawa T, et al. Rapid suppression of protein degradation in skeletal muscle after oral feeding of leucine in rats. J Nutr Biochem 2002;13:121-127.</ref><ref>Kadowaki M and Kanazawa T. Amino Acids as Regulators of Proteolysis. J Nutr 2003;133:2052S-2056S.</ref>.

Isoleucine, leucine and valine are constituents of [[Protein Overview - Nutrition|protein]]. Leucine is also a key catabolic regulator of l branched-chain amino acids<ref name="Harris">Harris RA, et al. Regulation of branched-chain α-keto acid dehydrogenase kinase expression in rat liver. J Nutr 2001;131:841S-845S.</ref>. Leucine also influences protein synthesis and muscle deposition by increasing plasma [[insulin]] secretion<ref>Yang J, et al. Leucine metabolism in regulation of insulin secretion from pancreatic beta cells. Nutr Rev 2010;68:270-279.</ref>, sensitivity of insulin binding to muscle cells<ref>Prod’homme M, et al. Insulin and amino acids both strongly participate to the regulation of protein metabolism. Curr Opin Clin Nutr Met Car 2004;7:71-7.</ref><ref>Anthony JC, et al. Contribution of insulin to the translational control of protein synthesis in skeletal muscle by leucine. Am J Physiol Endo Metab 2002;282:E1092-E1101.</ref><ref>Liu H, et al. Leucine facilitates the insulin-stimulated glucose uptake and insulin signalling in skeletal muscle cells: involving mTORC1 and mTORC2. Amino Acids 2014;46:1971-1979.</ref>, and inhibiting muscle catabolism<ref>Nagasawa T, et al. Rapid suppression of protein degradation in skeletal muscle after oral feeding of leucine in rats. J Nutr Biochem 2002;13:121-127.</ref><ref>Kadowaki M and Kanazawa T. Amino Acids as Regulators of Proteolysis. J Nutr 2003;133:2052S-2056S.</ref>.

==Consequences of Branched-Chain Amino Acid Deficiency==

==Consequences of Branched-Chain Amino Acid Deficiency==

==Dietary Sources==

==Dietary Sources==

Sufficient leucine, isoleucine, and valine are found in plant and animal protein sources, such as muscle meat, eggs, dairy protein (i.e., casein), cereal grains, and pulses (i.e., legumes).

Sufficient leucine, isoleucine, and valine are found in plant and animal protein sources, such as muscle meat, eggs, dairy protein (i.e. casein), cereal grains, and pulses (i.e. legumes).

==Diagnosing Branched-Chain Amino Acid Deficiency==

==Diagnosing Branched-Chain Amino Acid Deficiency==

==References==

==References==

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<references/>

[[Category:Amino Acids]]

[[Category:Amino Acids]]