Amino acids are important substances that must be transported to tissues such as the brain and muscles. The process is considered insulin dependent. It is not known whether all the amino acids are almost equally dependent in their transportation to tissues. We want to know whether some important amino acids are transported differently from other amino acids. Especially tryptophan is important because it is converted to serotonin, melatonin or kynurenine. Results showed that Amino acids levels in the plasma were meas ured after the intakes of 50 grams of glucose or sucrose to young (18 - 22 years old) and old (≥50 years old ) men. Total amino acids in the plasma decreased after the intakes of glucose. Total amino acid s levels decreased more significantly in old men after the administration of sucrose. Total and non-essential amino acids in the plasma decreased significantly at 120 min after the intakes of glucose in young and old men, but only sucrose caused their decreases in both aged and young men. Both glucose and sucrose in takes decreased significantly the plasma levels of the total essential and branched amino acids in young and old men. Surprisingly, plasma levels of tryptophan did not decrease upon the administration of glucose but only slightly decreased upon the administration of sucrose in young men. In conclusion , not all the amino acids were transported well into tissues upon the administration of glucose or sucrose. Tryptophan seems to be relatively resistant for insulin to facilitate the transportation into tissues.
Evans, W.J. (1995) What Is Sarcopenia? Journals of Gerontology Series A: Biological Sciences and Medical Sciences, 50A, 5-8. https://doi.org/10.1093/gerona/50A.Special_Issue.5
Dutta, C. and Hadley, E.C. (1995) The Significance of Sarcopenia in Old Age. Journals of Gerontology Series A: Biological Sciences and Medical Sciences, 50A, 1-4. https://doi.org/10.1093/gerona/50A.Special_Issue.1
Volpi, E., Mittendorfer, B., Rasmussen, B.B. and Wolfe, R.R. (2000) The Response of Muscle Protein Anabolism to Combined Hyperaminoacidemia and Glucose-Induced Hyperinsulinemia Is Impaired in the Elderly. Journal of Clinical Endocrinology and Metabolism, 85, 4481-4490. https://doi.org/10.1210/jc.85.12.4481
Guillet, C., Prod’homme, M., Balage, M., Gachon, P., Giraudet, C., Morin. L., Grizard, J. and Boirie, Y. (2004) Impaired Anabolic Response of Muscle Protein Synthesis Is Associated with S6K1 Dysregulation in Elderly Humans. The FASEB Journal, 18, 1586-1587. https://doi.org/10.1096/fj.03-1341fje
Cuthbertson, D., Smith, K., Babraj, J., Leese, G., Waddell, T., Atherton, P., Wackerhage, H., Taylor, P.M. and Rennie, M.J. (2005) Anabolic Signaling Deficits Underlie Amino Acid Resistance of Wasting, Aging Muscle. The FASEB Journal, 19, 422-424. https://doi.org/10.1096/fj.04-2640fje
Rasmussen, B.B., Fujita, S., Wolfe, R.R., Mittendorfer, B., Roy, M., Rowe, V.L. and Volpi, E. (2006) Insulin Resistance of Muscle Protein Metabolism in Aging. The FASEB Journal, 20, 768-769. https://doi.org/10.1096/fj.05-4607fje
Dardevet, D., Sornet, C., Bayle, G., Prugnaud, J., Pouyet, C. and Grizard, J. (2002) Postprandial Stimulation of Muscle Protein Synthesis in Old Rats Can Be Restored by a Leucine-Supplemented Meal. The Journal of Nutrition, 132, 95-100. https://doi.org/10.1093/jn/132.1.95
Kimball, S.R., Jefferson, L.S., Fadden, P., Haystead, T.A. and Lawrence Jr, J.C. (1996) Insulin and Diabetes Cause Reciprocal Changes in the Association of eIF-4E and PHAS-I in Rat Skeletal Muscle. American Journal of Physiology-Cell Physiology, 270, C705-C709. https://doi.org/10.1152/ajpcell.1996.270.2.C705
Timmerman, K.L., Lee, J.L., Dreyer, H.C., Dhanani, S., Glynn, E.L., Fry, C.S., Drummond, M.J., Sheffield-Moore, M., Rasmussen, B.B. and Volpi, E. (2010) Insulin Stimulates Human Skeletal Muscle Protein Synthesis via an Indirect Mechanism Involving Endothelial-Dependent Vasodilation and Mammalian Target of Rapamycin Complex 1 Signaling. Journal of Clinical Endocrinology and Metabolism, 95, 3848-3857. https://doi.org/10.1210/jc.2009-2696
Fujita, S., Rasmussen, B.B., Cadenas, J.G., Grady, J.J. and Volpi, E. (2006) Effect of Insulin on Human Skeletal Muscle Protein Synthesis Is Modulated by Insulin-Induced Changes in Muscle Blood Flow and Amino Acid Availability. American Journal of Physiology-Endocrinology and Metabolism, 291, E745-E754. https://doi.org/10.1152/ajpendo.00271.2005
Boirie, Y., Short, K.R., Ahlman, B., Charlton, M. and Nair, K.S. (2001) Tissue-Specific Regulation of Mitochondrial and Cyto-Plasmic Protein Synthesis Rates by Insulin. Diabetes, 50, 2652-2658. https://doi.org/10.2337/diabetes.50.12.2652
Gelfand, R.A. and Barrett, E.J. (1987) Effect of Physiologic Hyperinsulinemia on Skeletal Muscle Protein Synthesis and Breakdown in Man. Journal of Clinical Investigation, 80, 1-6. https://doi.org/10.1172/JCI113033
Fernstrom, J.D. and Wurtman, R.J. (1971) Brain Serotonin Content: Increase Following Ingestion of Carbohydrate Diet. Science, 174, 1023-1025. https://doi.org/10.1126/science.174.4013.1023
Fernstrom, J.D. and Wurtman, R.J. (1972) Brain Serotonin Content: Physiological Regulation by Plasma Neutral Amino Acids. Science, 178, 414-416. https://doi.org/10.1126/science.178.4059.414
Lipsett, D., Madras, B.K., Wurtman, R.J. and Munro, H.N. (1873) Serum Tryptophan Level after Carbohydrate Ingestion: Selective Decline in Non-Albumin-Bound Tryptophan Coincident with Reduction in Serum Free Fatty Acids. Life Sciences, 12, 57-64. https://doi.org/10.1016/0024-3205(73)90027-1
Pan, R.M., Mauron, C., Glaeser, B. and Wurtman, R.J. (1982) Effect of Various Oral Glucose Doses on Plasma Neutral Amino Acid Levels. Metabolism, 31, 937-943. https://doi.org/10.1016/0026-0495(82)90185-8
Sancak, Y., Peterson, T.R., Shaul, Y.D., et al. (2008) The Rag GTPases Bind Raptor and Mediate Amino Acid Signaling to mTORC1. Science, 320, 1496-1501. https://doi.org/10.1126/science.1157535
Heublein, S., Kazi, S., Ogmundsdottir, M.H., et al. (2010) Proton-Assisted Amino-Acid Transporters Are Conserved Regulators of Proliferation and Amino-Acid-Dependent mTORC1 Activation. Oncogene, 29, 4068-4079. https://doi.org/10.1038/onc.2010.177
Baird, F.E., Bett, K.J., MacLean, C., et al. (2009) Tertiary Active Transport of Amino Acids Reconstituted by Coexpression of System A and L Transporters in Xenopus Oocytes. The American Journal of Physiology-Endocrinology and Metabolism, 297, E822-E829. https://doi.org/10.1152/ajpendo.00330.2009
Nicklin, P., Bergman, P., Zhang, B., et al. (2009) Bidirectional Transport of Amino Acids Regulates mTOR and Autophagy. Cells, 136, 521-534. https://doi.org/10.1016/j.cell.2008.11.044
Zoncu, R., Bar-Peled, L., Efeyan, A., et al. (2011) mTORC1 Senses Lysosomal Amino Acids through an Inside-Out Mechanism That Requires the Vacuolar H+-ATPase. Science, 334, 678-683. https://doi.org/10.1126/science.1207056
Sancak, Y., Bar-Peled, L., Zoncu, R., et al. (2010) Ragulator-Rag Complex Targets mTORC1 to the Lysosomal Surface and Is Necessary for Its Activation by Amino Acids. Cells, 141, 290-303. https://doi.org/10.1016/j.cell.2010.02.024
Saltin, B. and Gollnick, P.D. (2011) Skeletal Muscle Adaptability: Significance for Metabolism and Performance. In: Peachy, L.D., Eds., Handbook of Physiology, Skeletal Muscle, American Physiological Society, Bethesda, 555-630.
Greenhaff, P.L., Karagounis, L.G., Peirce, N., et al. (2008) Disassociation between the Effects of Amino Acids and Insulin on Signaling, Ubiquitin Ligases, and Protein Turnover in Human Muscle. The American Journal of Physiology-Endocrinology and Metabolism, 295, E595-E604. https://doi.org/10.1152/ajpendo.90411.2008
Wilkes, E.A., Selby, A.L., Atherton, P.J., et al. (2009) Blunting of Insulin Inhibition of Proteolysis in Legs of Older Subjects May Contribute to Age Related Sarcopenia. The American Journal of Clinical Nutrition, 90, 1343-1350. https://doi.org/10.3945/ajcn.2009.27543
Chow, L.S., Albright, R.C., Bigelow, M.L., Toffolo, G., Cobelli, C. and Nair, K.S. (2006) Mechanism of Insulin’s Anabolic Effect on Muscle: Measurements of Muscle Protein Synthesis and Breakdown Using Aminoacyl-tRNA and Other Surrogate Measures. The American Journal of Physiology-Endocrinology and Metabolism, 291, E729-E736. https://doi.org/10.1152/ajpendo.00003.2006
Nygren, J. and Nair, K.S. (2003) Differential Regulation of Protein Dynamics in Splanchnic and Skeletal Muscle Beds by Insulin and Amino Acids in Healthy Human Subjects. Diabetes, 52, 1377-1385. https://doi.org/10.2337/diabetes.52.6.1377
Barazzoni, R., Short, K.R., Asmann, Y., Coenen-Schimke, J.M., Robinson, M.M. and Nair, K.S. (2012) Insulin Fails to Enhance mTOR Phosphorylation, Mitochondrial Protein Synthesis, and ATP Production in Human Skeletal Muscle without Amino Acid Replacement. American Journal of Physiology Endocrinology and Metabolism, 303, E1117-E1125. https://doi.org/10.1152/ajpendo.00067.2012
Stump, C.S., Short, K.R., Bigelow, M.L., Schimke, J.M. and Nair, K.S. (2003) Effect of Insulin on Human Skeletal Muscle Mitochondrial ATP Production, Protein Synthesis, and mRNA Transcripts. Proceedings of the National Academy of Sciences of the United States of America, 100, 7996-8001. https://doi.org/10.1073/pnas.1332551100
Tatpati, L.L., Irving, B.A., Tom, A., et al. (2010) The Effect of Branched Chain Amino Acids on Skeletal Muscle Mitochondrial Function in Young and Elderly Adults. The Journal of Clinical Endocrinology and Metabolism, 95, 894-902. https://doi.org/10.1210/jc.2009-1822
Jacobs, B.L. and Fornal, C.A. (1991) Activity of Brain Serotonergic Neurons in the Behaving Animal. Pharmacological Reviews, 43, 563-578.
Delgado, P.L., Charney, D.S., Price, L.H., Aghajanian, G.K., Landis, H. and Heninger, G.R. (1990) Serotonin Function and the Mechanism of Antidepressant Action. Reversal of Antidepressant-Induced Remission by Rapid Depletion of Plasma Tryptophan. Archives of General Psychiatry, 47, 411-418. https://doi.org/10.1001/archpsyc.1990.01810170011002
Dickinson, J.M. and Rasmussen, B.B. (2011) Essential Amino Acid Sensing, Signaling, and Transport in the Regulation of Human Muscle Protein Metabolism. Current Opinion in Clinical Nutrition and Metabolic Care, 14, 83-88. https://doi.org/10.1097/MCO.0b013e3283406f3e