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Volumn 128, Issue 12, 1998, Pages 2427-2434

Mitochondrial lysine uptake limits hepatic lysine oxidation in rats fed diets containing 5, 20 or 60% casein

Author keywords

Lysine; Metabolism; Mitochondria; Rats; Transport

Indexed keywords

AMINO ACID; CARBON 14; CASEIN; LYSINE; MITOCHONDRIAL ENZYME; OXIDOREDUCTASE; SACCHAROPINE DEHYDROGENASE;

EID: 0032411663     PISSN: 00223166     EISSN: None     Source Type: Journal    
DOI: 10.1093/jn/128.12.2427     Document Type: Article
Times cited : (34)

References (51)
  • 1
    • 0014286958 scopus 로고
    • Associations among food and protein intake, serine dehydratase, and plasma amino acids
    • Anderson, H. L., Benevenga, N. J. & Harper, A. E. (1968) Associations among food and protein intake, serine dehydratase, and plasma amino acids. Am. J. Physiol. 214: 1008-1013.
    • (1968) Am. J. Physiol. , vol.214 , pp. 1008-1013
    • Anderson, H.L.1    Benevenga, N.J.2    Harper, A.E.3
  • 2
    • 0000570730 scopus 로고
    • Systematic oscillations of amino acid transport in liver from rats adapted to controlled feeding schedules
    • Baril, E. F. & Potter, V. R. (1968) Systematic oscillations of amino acid transport in liver from rats adapted to controlled feeding schedules. J. Nutr. 95: 228-237.
    • (1968) J. Nutr. , vol.95 , pp. 228-237
    • Baril, E.F.1    Potter, V.R.2
  • 3
    • 0016220406 scopus 로고
    • Intracellular free amino acid concentration in human muscle tissue
    • Bergstrom, J., Furst, P., Noree, L. O. & Vinnars, E. (1974) Intracellular free amino acid concentration in human muscle tissue. J. Appl. Physiol. 36: 693-697.
    • (1974) J. Appl. Physiol. , vol.36 , pp. 693-697
    • Bergstrom, J.1    Furst, P.2    Noree, L.O.3    Vinnars, E.4
  • 4
    • 85088713290 scopus 로고
    • 14C-]L-lysine oxidation in liver homogenates from rats adapted to 5% or 60% casein diets
    • 14C-]L-lysine oxidation in liver homogenates from rats adapted to 5% or 60% casein diets. FASEB J. 6: A1943.
    • (1992) FASEB J. , vol.6
    • Blemings, K.P.1    Crenshaw, T.D.2    Benevenga, N.J.3
  • 5
    • 25544470211 scopus 로고
    • Response of rat hepatic mitochondrial lysine oxidation (Lys. ox.), lysine α-ketoglutarate reductase (LαKGR) and saccharopine dehydrogenase (SacD) to 5%, 18%, and 60% casein diets
    • Blemings, K. P., Crenshaw, T. D., Swick, R. W. & Benevenga, N. J. (1990) Response of rat hepatic mitochondrial lysine oxidation (Lys. ox.), lysine α-ketoglutarate reductase (LαKGR) and saccharopine dehydrogenase (SacD) to 5%, 18%, and 60% casein diets. FASEB J. 4: A919.
    • (1990) FASEB J. , vol.4
    • Blemings, K.P.1    Crenshaw, T.D.2    Swick, R.W.3    Benevenga, N.J.4
  • 6
    • 0028170488 scopus 로고
    • Lysine α-ketoglutarate reductase and saccharopine dehydrogenase are found exclusively in the mitochondrial matrix in rat liver
    • Blemings, K. P., Crenshaw, T. D., Swick, R. W. & Benevenga, N. J. (1994) Lysine α-ketoglutarate reductase and saccharopine dehydrogenase are found exclusively in the mitochondrial matrix in rat liver. J. Nutr. 124: 1215-1221.
    • (1994) J. Nutr. , vol.124 , pp. 1215-1221
    • Blemings, K.P.1    Crenshaw, T.D.2    Swick, R.W.3    Benevenga, N.J.4
  • 8
    • 0017861910 scopus 로고
    • Lysine metabolism in the rat brain: Blood-brain barrier transport, formation of pipecolic acid and human hyperpipecolatemia
    • Chang, Y. F. (1978a) Lysine metabolism in the rat brain: Blood-brain barrier transport, formation of pipecolic acid and human hyperpipecolatemia. J. Neurochem. 30: 355-360.
    • (1978) J. Neurochem. , vol.30 , pp. 355-360
    • Chang, Y.F.1
  • 9
    • 0017834164 scopus 로고
    • Lysine metabolism in the rat brain: The pipecolic acid-forming pathway
    • Chang, Y. F. (1978b) Lysine metabolism in the rat brain: The pipecolic acid-forming pathway. J. Neurochem. 30: 347-354.
    • (1978) J. Neurochem. , vol.30 , pp. 347-354
    • Chang, Y.F.1
  • 10
    • 0017071934 scopus 로고
    • Adaptive responses of lysine and threonine degrading enzymes in adult rats
    • Chu, S. & Hegsted, D. M. (1976) Adaptive responses of lysine and threonine degrading enzymes in adult rats. J. Nutr. 106: 1089-1096.
    • (1976) J. Nutr. , vol.106 , pp. 1089-1096
    • Chu, S.1    Hegsted, D.M.2
  • 11
    • 0023140949 scopus 로고
    • Channeling of extramitochondrial ornithine to matrix omithine transcarbamylase
    • Cohen, N. S., Cheung, C. W. & Rajiman, L. (1987) Channeling of extramitochondrial ornithine to matrix omithine transcarbamylase. J. Biol. Chem. 262: 203-208.
    • (1987) J. Biol. Chem. , vol.262 , pp. 203-208
    • Cohen, N.S.1    Cheung, C.W.2    Rajiman, L.3
  • 12
    • 0017724131 scopus 로고
    • Mitochondrial neutral amino acid transport: Evidence for a carrier mediated mechanism
    • Cybulski, R. L. & Fisher, R. R. (1977) Mitochondrial neutral amino acid transport: evidence for a carrier mediated mechanism. Biochem. 16: 5116-5120.
    • (1977) Biochem. , vol.16 , pp. 5116-5120
    • Cybulski, R.L.1    Fisher, R.R.2
  • 13
    • 0014559754 scopus 로고
    • Familial hyperlysinemia with lysine-ketoglutarate reductase insufficiency
    • Dancis, J., Hutzler, J., Cox, R. P. & Woody, N. C. (1969) Familial hyperlysinemia with lysine-ketoglutarate reductase insufficiency. J. Clin. Invest. 48: 1447-1452.
    • (1969) J. Clin. Invest. , vol.48 , pp. 1447-1452
    • Dancis, J.1    Hutzler, J.2    Cox, R.P.3    Woody, N.C.4
  • 14
    • 0023261660 scopus 로고
    • Failure of excess dietary lysine to antagonize arginine in young pigs
    • Edmonds, M. S. & Baker, D. H. (1987) Failure of excess dietary lysine to antagonize arginine in young pigs. J. Nutr: 117: 1396-1401.
    • (1987) J. Nutr , vol.117 , pp. 1396-1401
    • Edmonds, M.S.1    Baker, D.H.2
  • 15
    • 0015785637 scopus 로고
    • Amino acid production in isolated rat liver mitochondria
    • Ferdinand, W., Bartley, W. & Broomhead, V. (1973) Amino acid production in isolated rat liver mitochondria. Biochem. J. 134: 431-436.
    • (1973) Biochem. J. , vol.134 , pp. 431-436
    • Ferdinand, W.1    Bartley, W.2    Broomhead, V.3
  • 16
    • 0016823877 scopus 로고
    • Properties of partially purified saccharopine dehydrogenase from human placenta
    • Fjellstedt, T. A. & Robinson, J. C. (1975) Properties of partially purified saccharopine dehydrogenase from human placenta. Arch. Biochem. Biophys. 171: 191-196.
    • (1975) Arch. Biochem. Biophys. , vol.171 , pp. 191-196
    • Fjellstedt, T.A.1    Robinson, J.C.2
  • 17
    • 85040846424 scopus 로고
    • Energy and Protein Requirements
    • WHO, Geneva
    • Food and Agriculture Organization, World Health Organization, & United Nations University (1985) Energy and Protein Requirements. WHO Technical Report Series 724, WHO, Geneva.
    • (1985) WHO Technical Report Series , vol.724
  • 18
    • 0022503179 scopus 로고
    • Effect of dietary and extracellular potassium on lysine metabolism in the rat
    • Forsberg, N. E. & Austic, R. E. (1986) Effect of dietary and extracellular potassium on lysine metabolism in the rat. Nutr. Res. 6: 191-202.
    • (1986) Nutr. Res. , vol.6 , pp. 191-202
    • Forsberg, N.E.1    Austic, R.E.2
  • 19
    • 0006099412 scopus 로고
    • Feeding schedule alteration of daily rhythm in tyrosine alpha-ketoglutarate transaminase of rat liver
    • Fuller, R. W. & Snoddy, H. D. (1968) Feeding schedule alteration of daily rhythm in tyrosine alpha-ketoglutarate transaminase of rat liver. Science 159: 738.
    • (1968) Science , vol.159 , pp. 738
    • Fuller, R.W.1    Snoddy, H.D.2
  • 20
    • 0031658297 scopus 로고    scopus 로고
    • Concurrent measurement of protein synthesis and lysine catabolism in adult female rats induced to grow at different rates
    • Gahl, M. J., Benevenga, N. J. & Crenshaw, T. D. (1998) Concurrent measurement of protein synthesis and lysine catabolism in adult female rats induced to grow at different rates. J. Nutr. 128: 1503-1511.
    • (1998) J. Nutr. , vol.128 , pp. 1503-1511
    • Gahl, M.J.1    Benevenga, N.J.2    Crenshaw, T.D.3
  • 21
    • 0015935031 scopus 로고
    • Transport of omithine and citrulline across the mitochondrial membrane
    • Gamble, J. G. & Lehninger, A. L. (1973) Transport of omithine and citrulline across the mitochondrial membrane. J. Biol. Chem. 248: 610-618.
    • (1973) J. Biol. Chem. , vol.248 , pp. 610-618
    • Gamble, J.G.1    Lehninger, A.L.2
  • 23
    • 0016376551 scopus 로고
    • The isolation of outer and inner mitochondrial membranes
    • Fleischer, S. and Packer, L. (eds.) Academic Press, NY
    • Greenawalt, J. W. (1974) The isolation of outer and inner mitochondrial membranes. In Methods in Enzymology Fleischer, S. and Packer, L. (eds.) vol. 31, pp. 310-323. Academic Press, NY.
    • (1974) Methods in Enzymology , vol.31 , pp. 310-323
    • Greenawalt, J.W.1
  • 24
    • 0013798453 scopus 로고
    • Effect of variations in protein intake on enzymes of amino acid metabolism
    • Harper, A. E. (1965) Effect of variations in protein intake on enzymes of amino acid metabolism. Can. J. Biochem. 43: 1589-1603.
    • (1965) Can. J. Biochem. , vol.43 , pp. 1589-1603
    • Harper, A.E.1
  • 25
  • 26
    • 0021017952 scopus 로고
    • The uptake of omithine and lysine by rat liver mitochondria
    • Hommes, F. A., Kitchings, L. & Eller, A. G. (1983) The uptake of omithine and lysine by rat liver mitochondria. Biochem. Med. 30: 313-321.
    • (1983) Biochem. Med. , vol.30 , pp. 313-321
    • Hommes, F.A.1    Kitchings, L.2    Eller, A.G.3
  • 27
    • 0016430019 scopus 로고
    • Lysine-ketoglutarate reductase in human tissues
    • Hutzler, J. & Dancis, J. (1975) Lysine-ketoglutarate reductase in human tissues. Biochim. Biophys. Acta 377: 42-51.
    • (1975) Biochim. Biophys. Acta , vol.377 , pp. 42-51
    • Hutzler, J.1    Dancis, J.2
  • 29
    • 0018247903 scopus 로고
    • Circadian rhythms of urea formation and argininosuccinate synthetase activity in rat liver
    • Kato, H., Mizutani-Funahashi, M., Shiosaka, S. & Nakagawa, H. (1978) Circadian rhythms of urea formation and argininosuccinate synthetase activity in rat liver. J. Nutr. 108: 1071-1077.
    • (1978) J. Nutr. , vol.108 , pp. 1071-1077
    • Kato, H.1    Mizutani-Funahashi, M.2    Shiosaka, S.3    Nakagawa, H.4
  • 30
    • 0015902094 scopus 로고
    • Permeability of rat liver mitochondria to leucine, tyrosine, α-aminoisobutyric acid, and lysine
    • King, M. J. & Diwan, J. J. (1973) Permeability of rat liver mitochondria to leucine, tyrosine, α-aminoisobutyric acid, and lysine. Arch. Biochem. Biophys. 59: 166-173.
    • (1973) Arch. Biochem. Biophys. , vol.59 , pp. 166-173
    • King, M.J.1    Diwan, J.J.2
  • 31
  • 32
    • 0001326903 scopus 로고
    • Biuret Method
    • Colowick, S. D. and Kaplan, N. O., eds. Academic Press, NY
    • Layne, E. (1957) Biuret Method. In: Methods in Enzymology (Colowick, S. D. and Kaplan, N. O., eds.) vol. 3, pp. 450-451. Academic Press, NY.
    • (1957) Methods in Enzymology , vol.3 , pp. 450-451
    • Layne, E.1
  • 33
    • 0017359275 scopus 로고
    • Factors influencing the activity of omithine aminotransferase in isolated rat liver mitochondria
    • McGivan, J. D., Bradford, N. M. & Beavis, A. D. (1977) Factors influencing the activity of omithine aminotransferase in isolated rat liver mitochondria. Biochem. J. 162: 147-156.
    • (1977) Biochem. J. , vol.162 , pp. 147-156
    • McGivan, J.D.1    Bradford, N.M.2    Beavis, A.D.3
  • 34
    • 0002466016 scopus 로고
    • The role of liver and the non-hepatic tissues in the regulation of free amino acid levels in the blood
    • Holden, J.T., ed. Elsevier, NY
    • Miller, L. L. (1962) The role of liver and the non-hepatic tissues in the regulation of free amino acid levels in the blood. In: Amino Acid Pools-Distribution, Formation, and Function of Free Amino Acids (Holden, J.T., ed.) pp. 708-721. Elsevier, NY.
    • (1962) Amino Acid Pools-Distribution, Formation, and Function of Free Amino Acids , pp. 708-721
    • Miller, L.L.1
  • 35
    • 1642617484 scopus 로고
    • Adaptive response of liver and kidney lysine α-ketoglutarate reductase and lysine oxidation in rats fed graded levels of dietary lysine and casein
    • Muramatsu, K., Takada, R. & Uwa, K. (1984) Adaptive response of liver and kidney lysine α-ketoglutarate reductase and lysine oxidation in rats fed graded levels of dietary lysine and casein. Agric. Biol. Chem. 48: 703-711.
    • (1984) Agric. Biol. Chem. , vol.48 , pp. 703-711
    • Muramatsu, K.1    Takada, R.2    Uwa, K.3
  • 36
    • 0003633755 scopus 로고
    • Publication no. 85-23 (rev), National Institutes of Health, Bethesda, MD
    • National Research Council (1985) Guide for the care and use of laboratory animals, Publication no. 85-23 (rev), National Institutes of Health, Bethesda, MD.
    • (1985) Guide for the Care and Use of Laboratory Animals
  • 37
    • 0003498656 scopus 로고
    • National Academy Press, Washington, D.C.
    • National Research Council (1988) Nutrient requirements of swine, p. 48, National Academy Press, Washington, D.C.
    • (1988) Nutrient Requirements of Swine , pp. 48
  • 38
    • 26444440558 scopus 로고
    • National Academy Press. Washington, D.C.
    • National Research Council (1989) Recommended Dietary Allowances, 10th ed, pp. 70-71, National Academy Press. Washington, D.C.
    • (1989) Recommended Dietary Allowances, 10th Ed , pp. 70-71
  • 39
    • 0017653669 scopus 로고
    • Turnover of carbamyl-phosphate synthase, of outer mitochondrial enzymes, and of rat tissues
    • Nicolletti, M., Guerri, C. & Grisolia, S. (1977) Turnover of carbamyl-phosphate synthase, of outer mitochondrial enzymes, and of rat tissues. Eur. J. Biochem. 75: 583-592.
    • (1977) Eur. J. Biochem. , vol.75 , pp. 583-592
    • Nicolletti, M.1    Guerri, C.2    Grisolia, S.3
  • 40
    • 0017059461 scopus 로고
    • Control of ketogenesis from amino acids IV. Tissue specificity in oxidation of leucine, tyrosine, and lysine
    • Noda, C. & Ichihara, A. (1976) Control of ketogenesis from amino acids IV. Tissue specificity in oxidation of leucine, tyrosine, and lysine. J. Biochem. (Tokyo) 80: 1159-1164.
    • (1976) J. Biochem. (Tokyo) , vol.80 , pp. 1159-1164
    • Noda, C.1    Ichihara, A.2
  • 42
    • 0018337987 scopus 로고
    • Direct methods for measuring metabolite transport and distribution in mitochondria
    • Fleischer, S. & Packer, L., eds. Academic Press, NY
    • Palmieri, F. & Klingenberg, M. (1979) Direct methods for measuring metabolite transport and distribution in mitochondria. In: Methods in Enzymology LVI (Fleischer, S. & Packer, L., eds.) pp. 279-301. Academic Press, NY.
    • (1979) Methods in Enzymology LVI , pp. 279-301
    • Palmieri, F.1    Klingenberg, M.2
  • 43
    • 0019794734 scopus 로고
    • Plasma glucagon and insulin concentrations and hepatic phosphoenolpyruvate carboxykinase and pyruvate kinase activities during and upon adaptation of rats to a high protein diet
    • Peret, J., Foustock, S., Chanez, M., Bois-Joyeux, B. & Assan, R. (1981) Plasma glucagon and insulin concentrations and hepatic phosphoenolpyruvate carboxykinase and pyruvate kinase activities during and upon adaptation of rats to a high protein diet. J. Nutr. 111: 1173-1184.
    • (1981) J. Nutr. , vol.111 , pp. 1173-1184
    • Peret, J.1    Foustock, S.2    Chanez, M.3    Bois-Joyeux, B.4    Assan, R.5
  • 44
    • 0021950369 scopus 로고
    • Adaptation of rats to diets containing different levels of protein: Effects on food intake, plasma and brain amino acid concentrations and brain neurotransmitter metabolism
    • Peters, J. C. & Harper, A. E. (1985) Adaptation of rats to diets containing different levels of protein: effects on food intake, plasma and brain amino acid concentrations and brain neurotransmitter metabolism. J. Nutr. 115: 382-398.
    • (1985) J. Nutr. , vol.115 , pp. 382-398
    • Peters, J.C.1    Harper, A.E.2
  • 45
    • 0014335206 scopus 로고
    • Systematic oscillations in metabolic functions in liver from rats adapted to controlled feeding schedules
    • Potter, V. R., Baril, E. F., Watanabe, M. & Whittle, E. D. (1968) Systematic oscillations in metabolic functions in liver from rats adapted to controlled feeding schedules. Fed. Proc. 27: 1238-1245.
    • (1968) Fed. Proc. , vol.27 , pp. 1238-1245
    • Potter, V.R.1    Baril, E.F.2    Watanabe, M.3    Whittle, E.D.4
  • 46
    • 0001544643 scopus 로고
    • Animal behavior and internal drives
    • Richter, C. P. (1927) Animal behavior and internal drives. Qt. Rev. Biol. 2: 307-343.
    • (1927) Qt. Rev. Biol. , vol.2 , pp. 307-343
    • Richter, C.P.1
  • 47
    • 84961050939 scopus 로고
    • Adaptive characteristics of urea cycle enzymes in the rat
    • Schimke, R. T. (1962) Adaptive characteristics of urea cycle enzymes in the rat. J. Biol. Chem. 237: 459-468.
    • (1962) J. Biol. Chem. , vol.237 , pp. 459-468
    • Schimke, R.T.1
  • 48
    • 0028351969 scopus 로고
    • Regulation of oxidative degradation of L-lysine in rat liver mitochondria
    • Scislowski, P. W. D., Foster, A. R. & Fuller, M. F. (1994) Regulation of oxidative degradation of L-lysine in rat liver mitochondria. Biochem. J. 300: 887-891.
    • (1994) Biochem. J. , vol.300 , pp. 887-891
    • Scislowski, P.W.D.1    Foster, A.R.2    Fuller, M.F.3
  • 49
    • 0015233793 scopus 로고
    • Effect of protein content of diet on lysine oxidation by the rat
    • Soliman, A. & Harper, A. E. (1971) Effect of protein content of diet on lysine oxidation by the rat. Biochim. Biophys. Acta 244: 146-154.
    • (1971) Biochim. Biophys. Acta , vol.244 , pp. 146-154
    • Soliman, A.1    Harper, A.E.2
  • 50
    • 0027142823 scopus 로고
    • Metabolism of valine in rat skeletal muscle mitochondria
    • Torres, N., Tovar, A. R. & Harper, A. E. (1993) Metabolism of valine in rat skeletal muscle mitochondria. J. Nutr. Biochem. 4: 681-689.
    • (1993) J. Nutr. Biochem. , vol.4 , pp. 681-689
    • Torres, N.1    Tovar, A.R.2    Harper, A.E.3
  • 51
    • 0021148181 scopus 로고
    • Omithine uptake by isolated hepatocytes and distribution within the cell
    • Zollner, H. (1984) Omithine uptake by isolated hepatocytes and distribution within the cell. Int. J. Biochem. 16: 681-685.
    • (1984) Int. J. Biochem. , vol.16 , pp. 681-685
    • Zollner, H.1


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