Threonine-deficient diets induced changes in hepatic bioenergetics
Autor: | Cecilia R Giulivi, Andrew Almendares, Catherine Ross-Inta, Yi Fan Zhang |
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Rok vydání: | 2009 |
Předmět: |
Male
Threonine medicine.medical_specialty Time Factors Bioenergetics Physiology Mitochondria Liver Oxidative phosphorylation Biology Mitochondrion Mitochondria Heart Oxidative Phosphorylation Rats Sprague-Dawley Eating Adenosine Triphosphate Protein Deficiency Physiology (medical) Internal medicine medicine Protein biosynthesis Animals chemistry.chemical_classification Hepatology Catabolism Myocardium Body Weight Gastroenterology NAD Rats Amino acid Liver and Biliary Tract Disease Models Animal Endocrinology Liver chemistry Biochemistry Flavin-Adenine Dinucleotide Animal Nutritional Physiological Phenomena Dietary Proteins Energy Metabolism Energy source |
Zdroj: | American Journal of Physiology-Gastrointestinal and Liver Physiology. 296:G1130-G1139 |
ISSN: | 1522-1547 0193-1857 |
Popis: | Diets deficient in an indispensable amino acid are known to suppress food intake in rats. Few studies were focused at understanding how amino acid-deficient diets may elicit biochemical changes at the mitochondrial level. The goal of this study was to evaluate mitochondrial function in rats fed diets with 0.00, 0.18, 0.36, and 0.88% threonine (Thr) (set at 0, 30, 60, and 140% of Thr requirement for growth). Here, it is described for the first time that Thr-deficient diets induce a specific uncoupling of mitochondria in liver, especially with NADH-linked substrates, not observed in heart (except for Thr-devoid diet). The advantage of this situation would be to provide ATP to support growth and maintenance when high-quality protein food (or wealth of high-quality food in general) is available, whereas Thr-deficient diets (or deficient-quality protein food) promote the opposite, increasing mitochondrial uncoupling in liver. The uncoupling with NADH substrates would favor the use of nutrients as energy sources with higher FADH-to-NADH ratios, such as fat, minimizing the first irreversible NADH-dependent catabolism of many amino acids, including Thr, thus enhancing the use of the limiting amino acid for protein synthesis when a low quality protein source is available. |
Databáze: | OpenAIRE |
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