書籍詳細

序章 アミノ酸機能研究の新展開

P.8 掲載の参考文献

• 1) 清水誠ほか: 必須アミノ酸研究委員会50年の歩み. 必須アミノ酸研究委員会発行 2006.

• 2) Fulks R. M., Li J. B., Goldberg A.L.:Effects of insulin, glucose, and amino acids on protein turnover in rat diaphragm. J Biol Chem 1975;250;290-298.
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• 3) Tischler M. E., Desautels M., Goldberg A. L.:Does leucine, leucyl-tRNA, or some metabolite of leucine regulate protein synthesis and degradation in skeletal and cardiac muscle? J Biol Chem 1982;257;1613-1621.
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• 4) Gulve E. A., Dice J. F.:Regulation of protein synthesis and degradation in L8 myotubes. Effects of serum, insulin and insulin-like growth factors. Biochem J 1989;260;377-387.
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• 5) Yagasaki K., Kida Y., Miura Y., et al:Actions of branched-chain amino acids on protein degradation in cultured muscle cells. Animal Cell Technology:Basic & Applied Aspects 1994;6;279-285.

• 6) 矢ヶ崎一三: L-ロイシンの筋細胞タンパク質合成刺激作用におけるシグナル伝達. 必須アミノ酸研究 1990; 126; 1-5.

• 7) Yagasaki K., Morisaki-Tsuji N., Miura A., et al:Possible involvement of phospholipase C and protein kinase C in stimulatory actions of L-leucine and its keto acid, α-ketoisocaproic acid, on protein synthesis in RLC-16 hepatocytes. Cytotechnology 2002;40;151-154.

• 8) Yagasaki K., Morisaki N., Kitahara Y., et al:Involvement of protein kinase C activation in L-leucine-induced stimulation of protein synthesis in L6 myotubes. Cytotechnology 2003;43;97-103.

• 9) Miura Y., Nakazawa T., Yagasaki K.:Possible involvement of calcium signaling pathways in L-leucine-stimulated protein synthesis in L6 myotubes. Biosci Biotechnol Biochem 2006;70;1533-1536.

• 10) Yagasaki K., Hatano N., Fujii M., et al:Possible involvement of phospholipase A2 and cyclooxygenase in stimulatory action of L-histidine on protein synthesis in L6 myotubes. Cytotechnology 2002;40;155-160.
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• 11) Nishitani S., Matsumura T., Fujitani S., et al:Leucine promotes glucose uptake in skeletal muscles of rats. Biochem Biophys Res Commun 2002; 299;693-696.
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• 12) Doi M., Yamaoka I., Fukunaga T., et al:Isoleucine, a potent plasma glucose-lowering amino acid, stimulates glucose uptake in C2 C12 myotubes. Biochem Biophys Res Commun 2003;312;1111-1117.

• 13) Doi M, Yamaoka I., Nakayama M., et al:Isoleucine, a blood glucose-lowering amino acid, increases glucose uptake in rat skeletal muscle in the absence of increases in AMP-activated protein kinase activity. J Nutr 2005;135;2103-2108.
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• 14) Fujisawa K., Yagasaki K., Funabiki R.:Reduction of hyperlipidemia and proteinuria without growth retardation in nephritic rats by a methionine-supplemented, low-soy-protein diet. Am J Clin Nutr 1995; 61;603-606.
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• 15) Fujisawa K., Yagasaki K., Funabiki R., et al:Restoration of low casein feed-induced decrease in serum erythropoietin concentration by fortifying diet with methionine and threonine in normal and nephritic rats. Nutr Res 2000;20;685-693.

• 16) Yagasaki K.:Potent remedial actions of food factors and dietary manipulations against cancer and nephritis in in vitro and in vivo disease models. In:Recent Research Developments in Life Sciences, Vol. 3, Pandalai S. G.(ed), Research Signpost, 2005, p307-318.

• 17) McCully K. S. Ragsdale B. D.:Production of arteriosclerosis by homocysteinemia. Am J Pathol 1970;61;1-11.
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• 18) Wald D. S., Law M., Morris J. K.:Homocysteine and cardiovascular disease:evidence on causality from a meta-analysis. BMJ 2002;325;1202-1208.
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• 19) 吉田昭: 栄養とアミノ酸. アミノ酸セミナー, 岸恭一(監修), 日本必須アミノ酸協会(編), 工業調査会, 2003, p8-33.

• 20) Eagle H.:Nutrition needs of mammalian cells in tissue culture. Science 1955;122;501-514.
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• 21) Yamada M.:The historical story of Eagle's media for mammalian cell culture. In:Nutritional Requirements of Cultured Cells, Katsuta H.(ed), Japan Scientific Societies Press, Tokyo, 1978, p23-38.

• 22) Chatterjee S., Premachandran S., Bagewadikar R. S., et al:Arginine metabolic pathways determine its therapeutic benefit in experimental heatstroke:role of Th1/Th2 cytokine balance. Nitric Oxide 2006;15; 408-416.
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• 23) Komatsu W., Mawatari K., Miura Y., et al:Restoration by dietary glutamine of reduced tumor necrosis factor production in a low-protein-diet-fed rat model. Biosci Biotechnol Biochem 2007;71;352-357.

• 24) Nishimura N., Umeda C., Ona H., et al:The effect of taurine on plasma cholesterol concentration in genetic type 2 diabetic GK rats. J Nutr Sci Vitaminol 2002;48;483-490.
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• 25) Zhang G., Miura Y., Yagasaki K.:Inhibitory effects of theanine and sera from theanine-fed rats on receptor-mediated cancer cell invasion beneath mesothelial-cell monolayers. Cytotechnology 2001;36;195-200.
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• 26) Takahashi N., Kaji H., Yanagida M., et al:Proteomics:Advanced technology for the analysis of cellular function. J Nutr 2003;133;2090S-2096S.
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第1章 分岐鎖アミノ酸 (BCAA) の代謝調節とサプリメントとしての有用性

P.42 掲載の参考文献

• 1) Harper A.E., Miller R.H., Block K.P.:Branched-chain amino acid metabolism. Annu Rev Nutr 1984;4;409-454.
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• 2) Rennie MJ.:Influence of exercise on protein and amino acid metabolism. In:Handbook of Physiology, Rowell L.B., et al. (ed), Oxford University Press, 1996, p995-1035.

• 3) Ahlborg G., Felig P., Hagenfeldt L., et al:Substrate turnover during prolonged exercise in man. Splanchnic and leg metabolism of glucose, free fatty acids, and amino acids. J Clin Invest 1974;53;1080-1090.
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• 4) Takahashi A., Suzuki S., Takahashi H., et al:Effects of amino acid supplementation on endocrine responses and profile of mood states during intermittent exercise for 24 hours. 体力科学 2000;49;561-570.

• 5) Shimomura Y., Yamamoto Y., Bajotto G., et al:Nutraceutical effects of branched-chain amino acids on skeletal muscle. J Nutr 2006;136;529s-532s.
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• 6) Shimomura Y., Murakami T., Nagasaki M., et al:Regulation of branched-chain amino acid metabolism and pharmacological effects of branched-chain amino acids. Hepatol Res 2004;30S;3-8.
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• 7) Schadewaldt P.:Determination of branched-chain L-amino-acid amino-transferase activity. Methods Enzymol 2000;324;23-32.

• 8) Hutson S.M., Bledsoe R.K., Hall T.R., et al:Cloning and expression of the mammalian cytosolic branched chain aminotransferase isoenzyme. J Biol Chem 1995;270;30344-30352.
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• 9) Hutson S.M., Berkich D., Drown P., et al:Role of branched-chain amino-transferase isoenzymes and gabapentin in neurotransmitter metabolism. J Neurochem 1998;71;863-874.
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• 10) Reed L.J., Hackert M.L.:Structure-function relationships in dihydrolipo-amide acyltransferases. J Biol Chem 1990;265;8971-8974.

• 11) Shimomura Y., Nanaumi N., Suzuki M., et al:Purification and partial characterization of branched-chain α-ketoacid dehydrogenase kinase from rat liver and rat heart. Arch Biochem Biophys 1990;283;293-299.

• 12) Popov K.M., Zhao Y., Shimomura Y., et al:Branched-chain α-ketoacid dehydrogenase kinase. Molecular cloning, expression, and sequence similarity with histidine protein kinases. J Biol Chem 1992;267;13127-13130.

• 13) Obayashi M., Sato Y., Harris RA., et al:Regulation of the activity of branched-chain 2-oxo acid dehydrogenase (BCODH) complex by binding BCODH kinase. FEBS Lett 2001;491;50-54.
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• 14) Shimomura Y., Sato J., Honda T., et al:Branched-chain amino acid catabolism in exercise and liver disease. J Nutr 2006;136;250s-253s.
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• 15) Damuni Z., Reed L.J.:Purification and properties of the catalytic subunit of the branched-chain α-keto acid dehydrogenase phosphatase from bovine kidney mitochondria. J Biol Chem 1987;262;5129-5132.

• 16) Shimomura Y., Obayashi M., Murakami T., et al:Regulation of branched-chain amino acid catabolism:nutritional and hormonal regulation of activity and expression of the branched-chain α-keto acid dehydrogenase kinase. Curr Opin Clin Nutr Metab Care 2001;4;419-423.

• 17) Suryawan A., Hawes J.W., Shimomura Y., et al:A molecular model of human branched-chain amino acid metabolism. Am J Clin Nutr 1998;68;72-81.
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• 18) Poortmans J.R.:Protein metabolism. In:Principles of Exercise Biochemistry, Poortmans J. R. (ed), Karger, 1988, p164-193.

• 19) Xu M., Nagasaki M., Obayashi M., et al:Mechanism of activation of branched-chain α-keto acid dehydrogenase complex by exercise. Biochem Biophys Res Commun 2001;287;752-756.

• 20) Paul H. S., Adibi S. A.:Leucine oxidation and protein turnover in clofibrate-induced muscle protein degradation in rats. J Clin Invest 1980;65;1285-1293.
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• 21) Teravainen H., Larsen A., Hillbom M.:Clofibrate-induced myopathy in the rat. Acta Neuropathol 1977;39;135-138.
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• 22) 食品成分表, 大修館, 2000.

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• 24) Harris R.A., Hawes J.W., Popov K.M., et al:Studies on the regulation of the mitochondrial α-ketoacid dehydrogenase complexes and their kinases. Advan Enzyme Regul 1997;37;271-293.

• 25) Popov K.M., Zhao Y., Shimomura Y., et al:Dietary control and tissue specific expression of branched-chain α-ketoacid dehydrogenase kinase. Arch Biochem Biophys 1995;316;148-154.

• 26) Zhao Y., Popov K.M., Shimomura Y., et al:Effect of dietary protein on the liver content and subunit composition of the branched-chain α-ketoacid dehydrogenase complex. Arch Biochem Biophys 1994;308;446-453.

• 27) Nellis M.M., Doering C.B., Kasinski A., et al:Insulin increases branched-chain α-ketoacid dehydrogenase kinase expression in clone 9 rat cells. Am J Physiol Endocrinol Metab 2002;283;E853-E860.

• 28) Huang Y. S., Chuang D.T., et al:Down-regulation of rat mitochondrial branched-chain 2-oxoacid dehydrogenase kinase gene expression by glucocorticoids. Biochem J 1999;339;503-510.
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• 29) Kobayashi R., Shimomura Y., Otsuka M., et al:Experimental hyperthyroidism causes inactivation of the branched-chain α-ketoacid dehydrogenase complex in rat liver. Arch Biochem Biophys 2000;375; 55-61.

• 30) Kobayashi R., Shimomura Y., Murakami T., et al:Gender difference in regulation of branched-chain amino acid catabolism. Biochem J 1997;327;449-453.
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• 31) Obayashi M., Shimomura Y., Nakai N., et al:Estrogen controls branched-chain amino acid catabolism in female rats. J Nutr 2004;134;2628-2633.
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• 32) Shiraki M., Shimomura Y., Miwa Y., et al:Activation of hepatic branched-chain α-keto acid dehydrogenase complex by tumor necrosis factor-a in rats. Biochem Biophys Res Commun 2005;328;973-978.

• 33) Kobayashi R., Shimomura Y., Murakami T., et al:Hepatic branched-chain α-keto acid dehydrogenase complex in female rats:activation by exercise and starvation. J Nutr Sci Vitaminol 1999;45;303-309.

• 34) Shimomura Y., Fujii H., Suzuki M., et al:Branched-chain α-keto acid dehydrogenase complex in rat skeletal muscle:Regulation of the activity and gene expression by nutrition and physical exercise. J Nutr 1995;125;1762S-1765S.

• 35) Fujii H., Shimomura Y., Murakami T., et al:Branched-chain α-keto acid dehydrogenase kinase content in rat skeletal muscle is decreased by endurance training. Biochem Mol Biol Int 1998;44;1211-1216.

• 36) Patel M.S., Harris R.A.:Mammalian α-keto acid dehydrogenase complexes:gene regulation and genetic defects. FASEB J 1995;9;1164-1172.

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• 39) Wu P., Inskeep K., Bowker-Kinley M.M., et al:Mechanism responsible for inactivation of skeletal muscle pyruvate dehydrogenase complex in starvation and diabetes. Diabetes 1999;48;1593-1599.
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• 40) Yudkoff M., Daikhin Y., Nissim I., et al:Brain amino acid requirements and toxicity:the example of leucine. J Nutr 2005;135;1531S-1538S.
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• 41) Blomstrand E., Hassmen P., Ek S., et al:Influence of ingesting a solution of branched-chain amino acids on perceived exertion during exercise. Acta Physiol Scand 1997;159;41-49.
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• 43) Joshi M. A., Jeoung N. H., Obayashi M., et al;Impaired growth and neurological abnormalities in branched-chain α-keto acid dehydrogenase kinase-deficient mice. Biochem J 2006;400;153-162.

• 44) Gietzen D.W., Magrum LJ.:Molecular mechanisms in the brain involved in the anorexia of branched-chain amino acid deficiency. J Nutr 2001; 131;851S-855S.
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• 48) Holecek M.:Relation between glutamine, branched-chain amino acids, and protein metabolism. Nutrition 2002;18;130-133.
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第2章 分岐鎖アミノ酸とタンパク質合成制御

P.82 掲載の参考文献

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第3章 含硫アミノ酸の機能特性

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第4章 脳機能とセリン合成

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第7章 運動と分岐鎖アミノ酸

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第8章 オルニチンの生理機能

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第9章 肝硬変・肝臓癌とアミノ酸

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第10章 外科侵襲とアルギニン, グルタミン

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終章 今後の展開

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