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Volumn 33, Issue 2, 2008, Pages 279-284

Metabolic and regulatory roles of leucine in neural cells

Author keywords

Brain enzymes; Energy metabolism; Glutamate glutamine cycle; Ketone bodies; Leucine catabolism

Indexed keywords

2 OXOACID DEHYDROGENASE; AMINOTRANSFERASE; BETA METHYLCROTONOYL COENZYME A HYDRATASE; ESSENTIAL AMINO ACID; GLUTAMIC ACID; GLUTAMINE; HYDROXYMETHYLGLUTARYL COENZYME A LYASE; ISOVALERYL COENZYME A DEHYDROGENASE; LEUCINE; LIGASE; METHYLCROTONOYL COENZYME A CARBOXYLASE; UNCLASSIFIED DRUG;

EID: 38349135662     PISSN: 03643190     EISSN: None     Source Type: Journal    
DOI: 10.1007/s11064-007-9444-4     Document Type: Article
Times cited : (34)

References (67)
  • 1
    • 0015186836 scopus 로고
    • Brain uptake of radiolabeled amino acids, amines, and hexoses after arterial injection
    • Oldendorf WH (1971) Brain uptake of radiolabeled amino acids, amines, and hexoses after arterial injection. Am J Physiol 221:1629-1639
    • (1971) Am J Physiol , vol.221 , pp. 1629-1639
    • Oldendorf, W.H.1
  • 2
    • 0023634699 scopus 로고
    • Kinetics of neutral amino acid transport across the blood-brain barrier
    • Smith QR, Momma S, Aoyagi M et al (1987) Kinetics of neutral amino acid transport across the blood-brain barrier. J Neurochem 49:1651-1658
    • (1987) J Neurochem , vol.49 , pp. 1651-1658
    • Smith, Q.R.1    Momma, S.2    Aoyagi, M.3
  • 3
    • 0034098766 scopus 로고    scopus 로고
    • Transport of glutamate and other amino acids at the blood-brain barrier
    • Smith QR (2000) Transport of glutamate and other amino acids at the blood-brain barrier. J Nutr 130:1016S-1022S
    • (2000) J Nutr , vol.130
    • Smith, Q.R.1
  • 4
    • 19444376784 scopus 로고    scopus 로고
    • Cerebral ketone body metabolism
    • Morris AA (2005) Cerebral ketone body metabolism. J Inherit Metab Dis 28:109-121
    • (2005) J Inherit Metab Dis , vol.28 , pp. 109-121
    • Morris, A.A.1
  • 6
    • 2442728373 scopus 로고
    • Purification and characterization of branched chain alpha-keto acid dehydrogenase complex of bovine kidney
    • Pettit FH, Yeaman SJ, Reed LJ (1978) Purification and characterization of branched chain alpha-keto acid dehydrogenase complex of bovine kidney. Proc Natl Acad Sci USA 75:4881-4885
    • (1978) Proc Natl Acad Sci USA , vol.75 , pp. 4881-4885
    • Pettit, F.H.1    Yeaman, S.J.2    Reed, L.J.3
  • 7
    • 0021336721 scopus 로고
    • The relative carbon flux through the alpha- and the beta-keto pathways of leucine metabolism
    • Poston JM (1984) The relative carbon flux through the alpha- and the beta-keto pathways of leucine metabolism. J Biol Chem 259:2059-2061
    • (1984) J Biol Chem , vol.259 , pp. 2059-2061
    • Poston, J.M.1
  • 8
    • 0004226122 scopus 로고
    • The brain barrier system-II. Uptake and transport of amino acids by the brain
    • Lajtha A, Toth J (1961) The brain barrier system-II. Uptake and transport of amino acids by the brain. J Neurochem 8:216-225
    • (1961) J Neurochem , vol.8 , pp. 216-225
    • Lajtha, A.1    Toth, J.2
  • 9
    • 0015791380 scopus 로고
    • Effect of pentobarbital on amino acid and urea flux in the isolated dog brain
    • Betz AL, Gilboe DD (1973) Effect of pentobarbital on amino acid and urea flux in the isolated dog brain. Am J Physiol 224:580-587
    • (1973) Am J Physiol , vol.224 , pp. 580-587
    • Betz, A.L.1    Gilboe, D.D.2
  • 10
    • 0025095302 scopus 로고
    • Role of amino acid transport and counter transport in nutrition and metabolism
    • Christensen HN (1990) Role of amino acid transport and counter transport in nutrition and metabolism. Physiol Rev 70:43-77
    • (1990) Physiol Rev , vol.70 , pp. 43-77
    • Christensen, H.N.1
  • 11
    • 31544481841 scopus 로고    scopus 로고
    • Structure of the blood-brain barrier and its role in the transport of amino acids
    • 1 Suppl
    • Hawkins RA, O'Kane RL, Simpson IA et al (2006) Structure of the blood-brain barrier and its role in the transport of amino acids. J Nutr 136(1 Suppl):218S-226S
    • (2006) J Nutr , vol.136
    • Hawkins, R.A.1    O'Kane, R.L.2    Simpson, I.A.3
  • 12
    • 0024230927 scopus 로고
    • Neutral amino acid transport at the human blood-brain barrier
    • Hargreaves KM, Pardridge WM (1988) Neutral amino acid transport at the human blood-brain barrier. J Biol Chem 263:19392-19397
    • (1988) J Biol Chem , vol.263 , pp. 19392-19397
    • Hargreaves, K.M.1    Pardridge, W.M.2
  • 13
    • 0344896637 scopus 로고    scopus 로고
    • +-dependent transport of large neutral amino acids occurs at the abluminal membrane of the blood-brain barrier
    • +-dependent transport of large neutral amino acids occurs at the abluminal membrane of the blood-brain barrier. Am J Physiol Endocrinol Metab 285:E1167-E1173
    • (2003) Am J Physiol Endocrinol Metab , vol.285
    • O'Kane, R.L.1    Hawkins, R.A.2
  • 14
    • 0021020420 scopus 로고
    • Brain metabolism: A perspective from the blood-brain barrier
    • Pardridge WM (1983) Brain metabolism: a perspective from the blood-brain barrier. Physiol Rev 63:1481-1535
    • (1983) Physiol Rev , vol.63 , pp. 1481-1535
    • Pardridge, W.M.1
  • 15
    • 0017600519 scopus 로고
    • Transport of metabolic substances through the blood-brain barrier
    • Pardridge WM, Oldendorf WH (1977) Transport of metabolic substances through the blood-brain barrier. J Neurochem 28:5-12
    • (1977) J Neurochem , vol.28 , pp. 5-12
    • Pardridge, W.M.1    Oldendorf, W.H.2
  • 16
    • 0022504397 scopus 로고
    • Blood-brain barrier transport of the alpha-keto acid analogs of amino acids
    • Steele RD (1986) Blood-brain barrier transport of the alpha-keto acid analogs of amino acids. Fed Proc 45:2060-2064
    • (1986) Fed Proc , vol.45 , pp. 2060-2064
    • Steele, R.D.1
  • 17
    • 9644281565 scopus 로고    scopus 로고
    • System L-amino acid transporters are differently expressed in rat astrocyte and C6 glioma cells
    • Kim DK, Kim IJ, Hwang S et al (2004) System L-amino acid transporters are differently expressed in rat astrocyte and C6 glioma cells. Neurosci Res 50:437-446
    • (2004) Neurosci Res , vol.50 , pp. 437-446
    • Kim, D.K.1    Kim, I.J.2    Hwang, S.3
  • 18
    • 26844517064 scopus 로고    scopus 로고
    • Characterization of a branched-chain amino-acid transporter SBAT1 (SLC6A15) that is expressed in human brain
    • Takanaga H, Mackenzie B, Peng JB et al (2005) Characterization of a branched-chain amino-acid transporter SBAT1 (SLC6A15) that is expressed in human brain. Biochem Biophys Res Commun 337:892-900
    • (2005) Biochem Biophys Res Commun , vol.337 , pp. 892-900
    • Takanaga, H.1    MacKenzie, B.2    Peng, J.B.3
  • 19
    • 30044436322 scopus 로고    scopus 로고
    • +-dependent neutral amino acid transporter (B0AT2)
    • +-dependent neutral amino acid transporter (B0AT2). Biochem J 393:421-430
    • (2006) Biochem J , vol.393 , pp. 421-430
    • Broer, A.1    Tietze, N.2    Kowalczuk, S.3
  • 20
    • 0031007633 scopus 로고    scopus 로고
    • Cellular distribution of branched-chain amino acid aminotransferase isoenzymes among rat brain glial cells in culture
    • Bixel MG, Hutson SM, Hamprecht B (1997) Cellular distribution of branched-chain amino acid aminotransferase isoenzymes among rat brain glial cells in culture. J Histochem Cytochem 45:685-694
    • (1997) J Histochem Cytochem , vol.45 , pp. 685-694
    • Bixel, M.G.1    Hutson, S.M.2    Hamprecht, B.3
  • 21
    • 0030774069 scopus 로고    scopus 로고
    • Comparison of lactate transport in astroglial cells and monocarboxylate transporter 1 (MCT 1) expressing Xenopus laevis oocytes
    • Broer S, Rahman B, Pellegri G et al (1997) Comparison of lactate transport in astroglial cells and monocarboxylate transporter 1 (MCT 1) expressing Xenopus laevis oocytes. J Biol Chem 272: 30096-30102
    • (1997) J Biol Chem , vol.272 , pp. 30096-30102
    • Broer, S.1    Rahman, B.2    Pellegri, G.3
  • 22
    • 21344444566 scopus 로고    scopus 로고
    • Monocarboxylate transporters in the central nervous system: Distribution, regulation and function
    • Pierre K, Pellerin L (2005) Monocarboxylate transporters in the central nervous system: distribution, regulation and function. J Neurochem 94:1-14
    • (2005) J Neurochem , vol.94 , pp. 1-14
    • Pierre, K.1    Pellerin, L.2
  • 23
    • 0027408857 scopus 로고
    • Branched chain aminotransferase isoenzymes. Purification and characterization of the rat brain isoenzyme
    • Hall TR, Wallin R, Reinhart GD et al (1993) Branched chain aminotransferase isoenzymes. Purification and characterization of the rat brain isoenzyme. J Biol Chem 268:3092-3098
    • (1993) J Biol Chem , vol.268 , pp. 3092-3098
    • Hall, T.R.1    Wallin, R.2    Reinhart, G.D.3
  • 24
    • 0031750339 scopus 로고    scopus 로고
    • A molecular model of human branched-chain amino acid metabolism
    • Suryawan A, Hawes JW, Harris RA et al (1998) A molecular model of human branched-chain amino acid metabolism. Am J Clin Nutr 68:72-81
    • (1998) Am J Clin Nutr , vol.68 , pp. 72-81
    • Suryawan, A.1    Hawes, J.W.2    Harris, R.A.3
  • 25
    • 0025231999 scopus 로고
    • Purification of branched chain aminotransferase from rat heart mitochondria
    • Wallin R, Hall TR, Hutson SM (1990) Purification of branched chain aminotransferase from rat heart mitochondria. J Biol Chem 265:6019-6024
    • (1990) J Biol Chem , vol.265 , pp. 6019-6024
    • Wallin, R.1    Hall, T.R.2    Hutson, S.M.3
  • 26
    • 33846032696 scopus 로고    scopus 로고
    • Human mitochondrial branched chain aminotransferase isozyme: Structural role of the CXXC center in catalysis
    • Yennawar NH, Islam MM, Conway M et al (2006) Human mitochondrial branched chain aminotransferase isozyme: structural role of the CXXC center in catalysis. J Biol Chem 281:39660-39671
    • (2006) J Biol Chem , vol.281 , pp. 39660-39671
    • Yennawar, N.H.1    Islam, M.M.2    Conway, M.3
  • 27
    • 0035116897 scopus 로고    scopus 로고
    • Distribution of key enzymes of branched-chain amino acid metabolism in glial and neuronal cells in culture
    • Bixel M, Shimomura Y, Hutson S et al (2001) Distribution of key enzymes of branched-chain amino acid metabolism in glial and neuronal cells in culture. J Histochem Cytochem 49:407-418
    • (2001) J Histochem Cytochem , vol.49 , pp. 407-418
    • Bixel, M.1    Shimomura, Y.2    Hutson, S.3
  • 28
    • 0031783654 scopus 로고    scopus 로고
    • Role of branched-chain aminotransferase isoenzymes and gabapentin in neurotransmitter metabolism
    • Hutson SM, Berkich D, Drown P et al (1998) Role of branched-chain aminotransferase isoenzymes and gabapentin in neurotransmitter metabolism. J Neurochem 71:863-874
    • (1998) J Neurochem , vol.71 , pp. 863-874
    • Hutson, S.M.1    Berkich, D.2    Drown, P.3
  • 29
    • 4444293612 scopus 로고    scopus 로고
    • Branched-chain amino acids and neurotransmitter metabolism: Expression of cytosolic branched-chain aminotransferase (BCATc) in the cerebellum and hippocampus
    • Sweatt AJ, Garcia-Espinosa MA, Wallin R et al (2004) Branched-chain amino acids and neurotransmitter metabolism: expression of cytosolic branched-chain aminotransferase (BCATc) in the cerebellum and hippocampus. J Comp Neurol 477:360-370
    • (2004) J Comp Neurol , vol.477 , pp. 360-370
    • Sweatt, A.J.1    Garcia-Espinosa, M.A.2    Wallin, R.3
  • 30
    • 33847709986 scopus 로고    scopus 로고
    • Widespread neuronal expression of branched-chain aminotransferase in the CNS: Implication for leucine/glutamate metabolism and for signaling by amino acids
    • Garcia-Espinosa MA, Sweatt AJ, Hutson SM et al (2007) Widespread neuronal expression of branched-chain aminotransferase in the CNS: implication for leucine/glutamate metabolism and for signaling by amino acids. J Neurochem 100:1458-1468
    • (2007) J Neurochem , vol.100 , pp. 1458-1468
    • Garcia-Espinosa, M.A.1    Sweatt, A.J.2    Hutson, S.M.3
  • 31
    • 0035095315 scopus 로고    scopus 로고
    • Function of leucine in excitatory neurotransmitter metabolism in the central nervous system
    • Hutson SM, Lieth E, LaNoue KF (2001) Function of leucine in excitatory neurotransmitter metabolism in the central nervous system. J Nutr 131:846S-850S
    • (2001) J Nutr , vol.131
    • Hutson, S.M.1    Lieth, E.2    Lanoue, K.F.3
  • 32
    • 0026772495 scopus 로고
    • Branched-chain alpha-ketoacid dehydrogenase kinase. Molecular cloning, expression, and sequence similarity with histidine protein kinases
    • Popov KM, Zhao Y, Shimomura Y et al (1992) Branched-chain alpha-ketoacid dehydrogenase kinase. Molecular cloning, expression, and sequence similarity with histidine protein kinases. J Biol Chem 267:13127-13130
    • (1992) J Biol Chem , vol.267 , pp. 13127-13130
    • Popov, K.M.1    Zhao, Y.2    Shimomura, Y.3
  • 33
    • 34249699637 scopus 로고    scopus 로고
    • A novel branched-chain amino acid metabolon: Protein-protein interactions in a supramolecular complex
    • Islam MM, Wallin R, Wynn RM et al (2007) A novel branched-chain amino acid metabolon: Protein-protein interactions in a supramolecular complex. J Biol Chem 282:11893-11903
    • (2007) J Biol Chem , vol.282 , pp. 11893-11903
    • Islam, M.M.1    Wallin, R.2    Wynn, R.M.3
  • 34
    • 33646195697 scopus 로고    scopus 로고
    • Production and characterization of murine models of classic and intermediate maple syrup urine disease
    • Homanics GE, Skvorak K, Ferguson C et al (2006) Production and characterization of murine models of classic and intermediate maple syrup urine disease. BMC Med Genet 7:33
    • (2006) BMC Med Genet , vol.7 , pp. 33
    • Homanics, G.E.1    Skvorak, K.2    Ferguson, C.3
  • 35
    • 33751071072 scopus 로고    scopus 로고
    • Impaired growth and neurological abnormalities in branched-chain alpha-keto acid dehydrogenase kinase-deficient mice
    • Joshi MA, Jeoung NH, Obayashi M et al (2006) Impaired growth and neurological abnormalities in branched-chain alpha-keto acid dehydrogenase kinase-deficient mice. Biochem J 400:153-162
    • (2006) Biochem J , vol.400 , pp. 153-162
    • Joshi, M.A.1    Jeoung, N.H.2    Obayashi, M.3
  • 37
    • 0024467463 scopus 로고
    • Molecular cloning and nucleotide sequence of cDNAs encoding the precursors of rat long chain acyl-coenzyme A, short chain acyl-coenzyme A, and isovaleryl-coenzyme a dehydrogenases. Sequence homology of four enzymes of the acyl-CoA dehydrogenase family
    • Matsubara Y, Indo Y, Naito E et al (1989) Molecular cloning and nucleotide sequence of cDNAs encoding the precursors of rat long chain acyl-coenzyme A, short chain acyl-coenzyme A, and isovaleryl-coenzyme A dehydrogenases. Sequence homology of four enzymes of the acyl-CoA dehydrogenase family. J Biol Chem 264:16321-16331
    • (1989) J Biol Chem , vol.264 , pp. 16321-16331
    • Matsubara, Y.1    Indo, Y.2    Naito, E.3
  • 38
    • 0029064585 scopus 로고
    • Isolation of a cDNA encoding human holocarboxylase synthetase by functional complementation of a biotin auxotroph of Escherichia coli
    • Leon-del-Rio A, LeClerc D, Ackerman B et al (1995) Isolation of a cDNA encoding human holocarboxylase synthetase by functional complementation of a biotin auxotroph of Escherichia coli. Proc Natl Acad Sci USA 92:4626-4630
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 4626-4630
    • Leon-Del-Rio, A.1    Leclerc, D.2    Ackerman, B.3
  • 39
    • 0034937313 scopus 로고    scopus 로고
    • Biotin regulates the genetic expression of holocarboxylase synthetase and mitochondrial carboxylases in rats
    • Rodriguez-Melendez R, Cano S, Mendez ST et al (2001) Biotin regulates the genetic expression of holocarboxylase synthetase and mitochondrial carboxylases in rats. J Nutr 131:1909-1913
    • (2001) J Nutr , vol.131 , pp. 1909-1913
    • Rodriguez-Melendez, R.1    Cano, S.2    Mendez, S.T.3
  • 40
    • 33646584833 scopus 로고    scopus 로고
    • Immunocytochemical localization of 3-methylcrotonyl-CoA carboxylase in cultured ependymal, microglial and oligodendroglial cells
    • Murin R, Verleysdonk S, Rapp M et al (2006) Immunocytochemical localization of 3-methylcrotonyl-CoA carboxylase in cultured ependymal, microglial and oligodendroglial cells. J Neurochem 97:1393-1402
    • (2006) J Neurochem , vol.97 , pp. 1393-1402
    • Murin, R.1    Verleysdonk, S.2    Rapp, M.3
  • 41
    • 0033981702 scopus 로고    scopus 로고
    • Immunocytochemical localization of β-methylcrotonyl-CoA carboxylase in astroglial cells and neurons in culture
    • Bixel MG, Hamprecht B (2000) Immunocytochemical localization of β-methylcrotonyl-CoA carboxylase in astroglial cells and neurons in culture. J Neurochem 74:1059-1067
    • (2000) J Neurochem , vol.74 , pp. 1059-1067
    • Bixel, M.G.1    Hamprecht, B.2
  • 42
    • 38349098959 scopus 로고    scopus 로고
    • Distribution of 3-methylcrotonyl-CoA carboxylase in rat brain
    • Suppl. 2
    • Murin R, Hamprecht B (2005) Distribution of 3-methylcrotonyl-CoA carboxylase in rat brain. J Neurochem 94(Suppl. 2):242
    • (2005) J Neurochem , vol.94 , pp. 242
    • Murin, R.1    Hamprecht, B.2
  • 43
    • 0028901746 scopus 로고
    • AUH, a gene encoding an AU-specific RNA binding protein with intrinsic enoyl-CoA hydratase activity
    • Nakagawa J, Waldner H, Meyer-Monard S et al (1995) AUH, a gene encoding an AU-specific RNA binding protein with intrinsic enoyl-CoA hydratase activity. Proc Natl Acad Sci USA 92:2051-2055
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 2051-2055
    • Nakagawa, J.1    Waldner, H.2    Meyer-Monard, S.3
  • 44
    • 0036908780 scopus 로고    scopus 로고
    • 3-Methylglutaconic aciduria type I is caused by mutations in AUH
    • Ijlst L, Loupatty FJ, Ruiter JP et al (2002) 3-Methylglutaconic aciduria type I is caused by mutations in AUH. Am J Hum Genet 71:1463-1466
    • (2002) Am J Hum Genet , vol.71 , pp. 1463-1466
    • Ijlst, L.1    Loupatty, F.J.2    Ruiter, J.P.3
  • 45
    • 0037240025 scopus 로고    scopus 로고
    • Mutations in the AUH gene cause 3-methylglutaconic aciduria type I
    • Ly TB, Peters V, Gibson KM et al (2003) Mutations in the AUH gene cause 3-methylglutaconic aciduria type I. Hum Mutat 21:401-407
    • (2003) Hum Mutat , vol.21 , pp. 401-407
    • Ly, T.B.1    Peters, V.2    Gibson, K.M.3
  • 46
    • 0028892038 scopus 로고
    • Generation of ketone bodies from leucine by cultured astroglial cells
    • Bixel MG, Hamprecht B (1995) Generation of ketone bodies from leucine by cultured astroglial cells. J Neurochem 65:2450-2461
    • (1995) J Neurochem , vol.65 , pp. 2450-2461
    • Bixel, M.G.1    Hamprecht, B.2
  • 47
    • 0032518858 scopus 로고    scopus 로고
    • Molecular cloning of rat mitochondrial 3-hydroxy-3-methylglutaryl-CoA lyase and detection of the corresponding mRNA and of those encoding the remaining enzymes comprising the ketogenic 3-hydroxy-3-methylglutaryl-CoA cycle in central nervous system of suckling rat
    • Cullingford TE, Dolphin CT, Bhakoo KK et al (1998) Molecular cloning of rat mitochondrial 3-hydroxy-3-methylglutaryl-CoA lyase and detection of the corresponding mRNA and of those encoding the remaining enzymes comprising the ketogenic 3-hydroxy-3-methylglutaryl-CoA cycle in central nervous system of suckling rat. Biochem J 329:373-381
    • (1998) Biochem J , vol.329 , pp. 373-381
    • Cullingford, T.E.1    Dolphin, C.T.2    Bhakoo, K.K.3
  • 48
    • 0012182267 scopus 로고
    • Der chemische Mechanismus der Acetessigsäurebildung in der Leber
    • Lynen F, Henning U, Bublitz C et al (1958) Der chemische Mechanismus der Acetessigsäurebildung in der Leber. Biochem Z 330:269-295
    • (1958) Biochem Z , vol.330 , pp. 269-295
    • Lynen, F.1    Henning, U.2    Bublitz, C.3
  • 49
    • 33646597523 scopus 로고
    • Regulation of cerebral metabolism of amino acids. I. Influence of phenylalanine deficiency on oxidative utilization in vitro
    • Roberts S, Seto K, Hanking BM (1962) Regulation of cerebral metabolism of amino acids. I. Influence of phenylalanine deficiency on oxidative utilization in vitro. J Neurochem 9:493-501
    • (1962) J Neurochem , vol.9 , pp. 493-501
    • Roberts, S.1    Seto, K.2    Hanking, B.M.3
  • 50
    • 0013840986 scopus 로고
    • Oxidation of leucine, isoleucine and related ketoacids in developing rabbit brain
    • Swaiman KF, Milstein JM (1965) Oxidation of leucine, isoleucine and related ketoacids in developing rabbit brain. J Neurochem 12:981-986
    • (1965) J Neurochem , vol.12 , pp. 981-986
    • Swaiman, K.F.1    Milstein, J.M.2
  • 51
    • 0014336644 scopus 로고
    • 14C]acetate in sensorimotor cortex, thalamus, caudate nucleus and cerebellum of the cat
    • 14C]acetate in sensorimotor cortex, thalamus, caudate nucleus and cerebellum of the cat. J Neurochem 15:965-970
    • (1968) J Neurochem , vol.15 , pp. 965-970
    • Berl, S.1    Frigyesi, T.L.2
  • 52
    • 0003529304 scopus 로고
    • Regulation of cerebral metabolism of amino acids IV. Influence of amino acid levels on leucine uptake, utilization and incorporation into protein in vivo
    • Roberts S, Morelos BS (1965) Regulation of cerebral metabolism of amino acids IV. Influence of amino acid levels on leucine uptake, utilization and incorporation into protein in vivo. J Neurochem 12:373-387
    • (1965) J Neurochem , vol.12 , pp. 373-387
    • Roberts, S.1    Morelos, B.S.2
  • 53
    • 33646589407 scopus 로고
    • Brain cholesterol: Biosynthesis with selected precursors in vivo
    • Kabara JJ, Okita G (1961) Brain cholesterol: biosynthesis with selected precursors in vivo. J Neurochem 7:298-304
    • (1961) J Neurochem , vol.7 , pp. 298-304
    • Kabara, J.J.1    Okita, G.2
  • 54
    • 0018184242 scopus 로고
    • The metabolism of leucine by developing rat brain: Effect of leucine and 2-oxo-4-methylvalerate on lipid synthesis from glucose and ketone bodies
    • Patel MS, Owen OE (1978) The metabolism of leucine by developing rat brain: effect of leucine and 2-oxo-4-methylvalerate on lipid synthesis from glucose and ketone bodies. J Neurochem 30:775-782
    • (1978) J Neurochem , vol.30 , pp. 775-782
    • Patel, M.S.1    Owen, O.E.2
  • 55
    • 0018397254 scopus 로고
    • Lipogenesis in the developing brain: Utilization of radioactive leucine, isoleucine, octanoic acid and beta-hydroxybutyric acid
    • Dhopeshwarkar GA, Subramanian C (1979) Lipogenesis in the developing brain: utilization of radioactive leucine, isoleucine, octanoic acid and beta-hydroxybutyric acid. Lipids 14:47-51
    • (1979) Lipids , vol.14 , pp. 47-51
    • Dhopeshwarkar, G.A.1    Subramanian, C.2
  • 56
    • 0028006431 scopus 로고
    • Interrelationships of leucine and glutamate metabolism in cultured astrocytes
    • Yudkoff M, Daikhin Y, Lin ZP et al (1994) Interrelationships of leucine and glutamate metabolism in cultured astrocytes. J Neurochem 62:1192-1202
    • (1994) J Neurochem , vol.62 , pp. 1192-1202
    • Yudkoff, M.1    Daikhin, Y.2    Lin, Z.P.3
  • 57
    • 0036312611 scopus 로고    scopus 로고
    • Alteration of amino acid metabolism in neuronal aggregate cultures exposed to hypoglycaemic conditions
    • Honegger P, Braissant O, Henry H et al (2002) Alteration of amino acid metabolism in neuronal aggregate cultures exposed to hypoglycaemic conditions. J Neurochem 81:1141-1151
    • (2002) J Neurochem , vol.81 , pp. 1141-1151
    • Honegger, P.1    Braissant, O.2    Henry, H.3
  • 59
    • 0030033642 scopus 로고    scopus 로고
    • Astrocyte leucine metabolism: Significance of branched-chain amino acid transamination
    • Yudkoff M, Daikhin Y, Grunstein L et al (1996) Astrocyte leucine metabolism: significance of branched-chain amino acid transamination. J Neurochem 66:378-385
    • (1996) J Neurochem , vol.66 , pp. 378-385
    • Yudkoff, M.1    Daikhin, Y.2    Grunstein, L.3
  • 60
    • 0025326250 scopus 로고
    • Activation of glutamate dehydrogenase by leucine and its nonmetabolizable analogue in rat brain synaptosomes
    • Erecinska M, Nelson D (1990) Activation of glutamate dehydrogenase by leucine and its nonmetabolizable analogue in rat brain synaptosomes. J Neurochem 54:1335-1343
    • (1990) J Neurochem , vol.54 , pp. 1335-1343
    • Erecinska, M.1    Nelson, D.2
  • 61
    • 0033788590 scopus 로고    scopus 로고
    • Nerve tissue-specific (GLUD2) and housekeeping [GLUD1) human glutamate dehydrogenases are regulated by distinct allosteric mechanisms: Implications for biologic function
    • Plaitakis A, Metaxari M, Shashidharan P (2000) Nerve tissue-specific (GLUD2) and housekeeping [GLUD1) human glutamate dehydrogenases are regulated by distinct allosteric mechanisms: implications for biologic function. J Neurochem 75:1862-1869
    • (2000) J Neurochem , vol.75 , pp. 1862-1869
    • Plaitakis, A.1    Metaxari, M.2    Shashidharan, P.3
  • 62
    • 12244298900 scopus 로고    scopus 로고
    • Molecular basis of human glutamate dehydrogenase regulation under changing energy demands
    • Mastorodemos V, Zaganas I, Spanaki C et al (2005) Molecular basis of human glutamate dehydrogenase regulation under changing energy demands. J Neurosci Res 79:65-73
    • (2005) J Neurosci Res , vol.79 , pp. 65-73
    • Mastorodemos, V.1    Zaganas, I.2    Spanaki, C.3
  • 63
    • 0037403502 scopus 로고    scopus 로고
    • Creatine kinase activity from rat brain is inhibited by branched-chain amino acids in vitro
    • Pilla C, Cardozo RF, Dutra-Filho CS et al (2003) Creatine kinase activity from rat brain is inhibited by branched-chain amino acids in vitro. Neurochem Res 28:675-679
    • (2003) Neurochem Res , vol.28 , pp. 675-679
    • Pilla, C.1    Cardozo, R.F.2    Dutra-Filho, C.S.3
  • 64
    • 0025801462 scopus 로고
    • Leucine: Effector of phosphate activated glutaminase in rat cerebral cortex
    • Lellos V, Tselentis V, Galanopoulos E et al (1991) Leucine: effector of phosphate activated glutaminase in rat cerebral cortex. Neurochem Res 16:67-71
    • (1991) Neurochem Res , vol.16 , pp. 67-71
    • Lellos, V.1    Tselentis, V.2    Galanopoulos, E.3
  • 65
    • 33748308712 scopus 로고    scopus 로고
    • Role of leucine in regulating food intake
    • Laviano A, Meguid MM, Inui A et al (2006) Role of leucine in regulating food intake. Science 313:1236-1238
    • (2006) Science , vol.313 , pp. 1236-1238
    • Laviano, A.1    Meguid, M.M.2    Inui, A.3
  • 66
    • 33646582664 scopus 로고    scopus 로고
    • Hypothalamic mTOR signaling regulates food intake
    • Cota D, Proulx K, Smith KA et al (2006) Hypothalamic mTOR signaling regulates food intake. Science 312:927-930
    • (2006) Science , vol.312 , pp. 927-930
    • Cota, D.1    Proulx, K.2    Smith, K.A.3
  • 67
    • 20144374658 scopus 로고    scopus 로고
    • Uncharged tRNA and sensing of amino acid deficiency in mammalian piriform cortex
    • Hao S, Sharp JW, Ross-Inta CM et al (2005) Uncharged tRNA and sensing of amino acid deficiency in mammalian piriform cortex. Science 307:1776-1778
    • (2005) Science , vol.307 , pp. 1776-1778
    • Hao, S.1    Sharp, J.W.2    Ross-Inta, C.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.