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==