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| | ==What is Threonine?== | | ==What is Threonine?== |
| − | Threonine is an essential amino acid for dogs and cats. Threonine is characterised as a gluconeogenic amino acid and contains a hydroxyl side chain which is chemically reactive. Dietary threonine is absorbed by a neutral amino acid transporter in the small intestine (particularly the jejunum) and plasma threonine is actively reabsorbed in the proximal tubule of the kidney. | + | Threonine is an [[Amino Acids Overview - Nutrition|'''essential amino acid]] for dogs and cats'''. Threonine is characterised as a '''[[Nutrition Glossary#Glucogenic Amino Acids|gluconeogenic]]''' amino acid and contains a hydroxyl side chain which is chemically reactive. Dietary threonine is absorbed by a neutral amino acid transporter in the [[Small Intestine Overview - Anatomy & Physiology|small intestine]] (particularly the [[Jejunum - Anatomy & Physiology|jejunum]]) and plasma threonine is actively reabsorbed in the [[Nephron Microscopic Anatomy#Proximal Tubule|proximal tubule]] of the kidney. |
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| | ==Why is it Important?== | | ==Why is it Important?== |
| − | Threonine is a component of structural proteins. The hydroxyl group on the side chain of threonine often serves as the site for phosphorylation and de-phosphorylation reactions that control the activities of many proteins and enzymes<ref>National Research Council (NRC). Protein and Amino Acids. In Nutrient Requirements for Dogs and Cats. 2006 Washington, DC: National Academies Press p. 130-131.</ref>. | + | Threonine is a '''component of structural [[Protein Overview - Nutrition|proteins]]'''. The hydroxyl group on the side chain of threonine often serves as the site for phosphorylation and de-phosphorylation reactions that control the activities of many proteins and enzymes<ref>National Research Council (NRC). Protein and Amino Acids. In Nutrient Requirements for Dogs and Cats. 2006 Washington, DC: National Academies Press p. 130-131.</ref>. |
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| | ==Roles in the body== | | ==Roles in the body== |
| − | The phosphorylation/dephosphorylation of the threonine hydroxyl groups on proteins by either is serine/threonine kinase or serine/threonine phosphatase, respectively, controls activity of normal physiologic function, such as insulin release<ref>Ortsader H, et al. Protein phosphatase in pancreatic islets. J Endo 2014;221:R121-R144.</ref> or cellular apoptosis<ref>Depaoli-Roach AA, et al. Serine/threonine protein phosphatases in the control of cell function. Adv Enz Regul 1994;34:199-224. </ref>. | + | The phosphorylation/dephosphorylation of the threonine hydroxyl groups on proteins is by either serine/threonine kinase or serine/threonine phosphatase, respectively, and controls activity of normal physiologic function, such as [[insulin]] release<ref>Ortsader H, et al. Protein phosphatase in pancreatic islets. J Endo 2014;221:R121-R144.</ref> or cellular apoptosis<ref>Depaoli-Roach AA, et al. Serine/threonine protein phosphatases in the control of cell function. Adv Enz Regul 1994;34:199-224. </ref>. |
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| | ==Consequences of Threonine Deficiency== | | ==Consequences of Threonine Deficiency== |
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| | ==Dietary Sources== | | ==Dietary Sources== |
| − | Sufficient threonine is found in plant and animal protein sources, such as muscle meat, eggs, dairy protein (e.g., casein), cereal grains, and pulses (i.e., legumes). | + | Sufficient threonine is found in plant and animal protein sources, such as muscle meat, eggs, dairy protein (e.g. casein), cereal grains, and pulses (i.e. legumes). |
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| | ==Diagnosing Threonine Deficiency== | | ==Diagnosing Threonine Deficiency== |
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| | ==References== | | ==References== |
| | <references/> | | <references/> |
| | + | <br> |
| | + | {{Reviewed Nutrition 1 |
| | + | |date = 18 May 2015}} |
| | + | {{Waltham}} |
| | + | {{OpenPages}} |
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| | [[Category:Amino Acids]] | | [[Category:Amino Acids]] |
| − | [[Category:To Do - Nutrition]]
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| − | [[Category:To Do - Nutrition GGP]]
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