메뉴 건너뛰기




Volumn 39, Issue 3, 2014, Pages 500-515

Heterogeneous cellular distribution of glutamate dehydrogenase in brain and in non-neural tissues

Author keywords

Expression profile; Glutamate dehydrogenase; hGDH1; hGDH2; Immunohistochemistry; Localization

Indexed keywords

ANTIBODY; GLUTAMATE DEHYDROGENASE; GLUTAMIC ACID; GUANOSINE TRIPHOSPHATE; MESSENGER RNA;

EID: 84896718850     PISSN: 03643190     EISSN: 15736903     Source Type: Journal    
DOI: 10.1007/s11064-013-1235-5     Document Type: Review
Times cited : (30)

References (100)
  • 1
    • 0002277203 scopus 로고
    • The evolution of glutamate dehydrogenases and a hypothesis for the insertion or deletion of multiple residues in the interior of polypeptide chains
    • Smith E (1979) The evolution of glutamate dehydrogenases and a hypothesis for the insertion or deletion of multiple residues in the interior of polypeptide chains. Proc Am Philos Soc 123:73-84
    • (1979) Proc Am Philos Soc , vol.123 , pp. 73-84
    • Smith, E.1
  • 3
    • 6944242766 scopus 로고    scopus 로고
    • Birth and adaptive evolution of a hominoid gene that supports high neurotransmitter flux
    • DOI 10.1038/ng1431
    • Burki F, Kaessmann H (2004) Birth and adaptive evolution of a hominoid gene that supports high neurotransmitter flux. Nature Genet 36:1061-1063 (Pubitemid 41184466)
    • (2004) Nature Genetics , vol.36 , Issue.10 , pp. 1061-1063
    • Burki, F.1    Kaessmann, H.2
  • 4
    • 2942620629 scopus 로고    scopus 로고
    • Evolution of glutamate dehydrogenase genes: Evidence for lateral gene transfer within and between prokaryotes and eukaryotes
    • Andersson JO, Roger AJ (2003) Evolution of glutamate dehydrogenase genes: evidence for lateral gene transfer within and between prokaryotes and eukaryotes. BMC Evol Biol 3:14
    • (2003) BMC Evol Biol , vol.3 , pp. 14
    • Andersson, J.O.1    Roger, A.J.2
  • 7
    • 84865720909 scopus 로고    scopus 로고
    • siRNA knock down of glutamate dehydrogenase in astrocytes affects glutamate metabolism leading to extensive accumulation of the neuroactive amino acids glutamate and aspartate
    • Skytt DM, Klawonn AM, Stridh MH, Pajecka K, Patruss Y, Quintana-Cabrera R, Bolanos JP, Schousboe A, Waagepetersen HS (2012) siRNA knock down of glutamate dehydrogenase in astrocytes affects glutamate metabolism leading to extensive accumulation of the neuroactive amino acids glutamate and aspartate. Neurochem Int 61:490-497
    • (2012) Neurochem Int , vol.61 , pp. 490-497
    • Skytt, D.M.1    Klawonn, A.M.2    Stridh, M.H.3    Pajecka, K.4    Patruss, Y.5    Quintana-Cabrera, R.6    Bolanos, J.P.7    Schousboe, A.8    Waagepetersen, H.S.9
  • 8
    • 0019133275 scopus 로고
    • L-Leucine and a nonmetabolized analogue activate pancreatic islet glutamate dehydrogenase
    • DOI 10.1038/288187a0
    • Sener A, Malaisse WJ (1980) L-leucine and a nonmetabolized analogue activate pancreatic islet glutamate dehydrogenase. Nature 288:187-189 (Pubitemid 11212612)
    • (1980) Nature , vol.288 , Issue.5787 , pp. 187-189
    • Sener, A.1    Malaisse, W.J.2
  • 9
    • 84856303217 scopus 로고    scopus 로고
    • The role of glutamate dehydrogenase in mammalian ammonia metabolism
    • Spanaki C, Plaitakis A (2012) The role of glutamate dehydrogenase in mammalian ammonia metabolism. Neurotox Res 21:117-127
    • (2012) Neurotox Res , vol.21 , pp. 117-127
    • Spanaki, C.1    Plaitakis, A.2
  • 11
    • 77952778182 scopus 로고    scopus 로고
    • Human GLUD2 glutamate dehydrogenase is expressed in neural and testicular supporting cells
    • Spanaki C, Zaganas I, Kleopa KA, Plaitakis A (2010) Human GLUD2 glutamate dehydrogenase is expressed in neural and testicular supporting cells. J Biol Chem 285:16748-16756
    • (2010) J Biol Chem , vol.285 , pp. 16748-16756
    • Spanaki, C.1    Zaganas, I.2    Kleopa, K.A.3    Plaitakis, A.4
  • 12
    • 64949087113 scopus 로고
    • Distribution pattern of several enzymes in human liver and its variations during cell damage. III: On the methodology of enzyme determination in human organ extracts and serum
    • Schmidt E, Schmidt FW (1963) Distribution pattern of several enzymes in human liver and its variations during cell damage. III: on the methodology of enzyme determination in human organ extracts and serum. Enzymol Biol Clin 35:73-79
    • (1963) Enzymol Biol Clin , vol.35 , pp. 73-79
    • Schmidt, E.1    Schmidt, F.W.2
  • 13
    • 0018175180 scopus 로고
    • The tissue activities of some diagnostic enzymes in ten mammalian species
    • Clampitt RB, Hart RJ (1978) The tissue activities of some diagnostic enzymes in ten mammalian species. J Comp Pathol 88:607-621 (Pubitemid 9057759)
    • (1978) Journal of Comparative Pathology , vol.88 , Issue.4 , pp. 607-621
    • Clampitt, R.B.1    Hart, R.J.2
  • 14
    • 0020999476 scopus 로고
    • Postnatal changes in the activity of glutamate dehydrogenase and aspartate aminotransferase in the rat nervous system with special reference to the glutamate transmitter metabolism
    • DOI 10.1016/0165-3806(83)90202-X
    • Rothe F, Schmidt W, Wolf G (1983) Postnatal changes in the activity of glutamate dehydrogenase and aspartate aminotransferase in the rat nervous system with special reference to the glutamate transmitter metabolism. Brain Res 313:67-74 (Pubitemid 14211303)
    • (1983) Developmental Brain Research , vol.11 , Issue.1 , pp. 67-74
    • Rothe, F.1    Schmidt, W.2    Wolf, G.3
  • 15
    • 0033066343 scopus 로고    scopus 로고
    • Cellular and regional expression of glutamate dehydrogenase in the rat nervous system: Non-radioactive in situ hybridization and comparative immunocytochemistry
    • DOI 10.1016/S0306-4522(98)00740-4, PII S0306452298007404
    • Schmitt A, Kugler P (1999) Cellular and regional expression of glutamate dehydrogenase in the rat nervous system: non-radioactive in situ hybridization and comparative immunocytochemistry. Neuroscience 92:293-308 (Pubitemid 29249039)
    • (1999) Neuroscience , vol.92 , Issue.1 , pp. 293-308
    • Schmitt, A.1    Kugler, P.2
  • 16
    • 0015128939 scopus 로고
    • Amino acid metabolism and ammonia formation in brain slices
    • Weil-Malherbe H, Gordon J (1971) Amino acid metabolism and ammonia formation in brain slices. J Neurochem 18:1659-1672
    • (1971) J Neurochem , vol.18 , pp. 1659-1672
    • Weil-Malherbe, H.1    Gordon, J.2
  • 17
    • 9244219794 scopus 로고
    • Cerebral glutamate-glutamine interrelations in vivo and in vitro
    • Schoffeniels E, Franck G, Hertz L, Towers DB (eds) Pergamon Press, Oxford
    • Quastel JH (1978) Cerebral glutamate-glutamine interrelations in vivo and in vitro. In: Schoffeniels E, Franck G, Hertz L, Towers DB (eds) Dynamic properties of glia cells. Pergamon Press, Oxford, pp 153-162
    • (1978) Dynamic Properties of Glia Cells , pp. 153-162
    • Quastel, J.H.1
  • 18
    • 0020322662 scopus 로고
    • The activities in different neural cell types of certain enzymes associated with the metabolic compartmentation glutamate
    • DOI 10.1016/0165-3806(82)90091-8
    • Patel AJ, Hunt A, Gordon RD, Balazs R (1982) The activities in different neural cell types of certain enzymes associated with the metabolic compartmentation of glutamate. Brain Res 256:3-11 (Pubitemid 12062960)
    • (1982) Developmental Brain Research , vol.4 , Issue.1 , pp. 3-11
    • Patel, A.J.1    Hunt, A.2    Gordon, R.D.3    Balazs, R.4
  • 19
    • 0015932548 scopus 로고
    • Bovine thyroid cytosol glutamate dehydrogenase
    • Larson JD, Schulz AR (1973) Bovine thyroid cytosol glutamate dehydrogenase. Life sci 12:73-78
    • (1973) Life Sci , vol.12 , pp. 73-78
    • Larson, J.D.1    Schulz, A.R.2
  • 20
    • 0021958309 scopus 로고
    • Ontogenetic development of glutamate metabolizing enzymes in cultured cerebellar granule cells and in cerebellum in vivo
    • DOI 10.1007/BF00964771
    • Drejer J, Larsson OM, Kvamme E, Svenneby G, Hertz L, Schousboe A (1985) Ontogenetic development of glutamate metabolizing enzymes in cultured cerebellar granule cells and in cerebellum in vivo. Neurochem Res 10:49-62 (Pubitemid 15140709)
    • (1985) Neurochemical Research , vol.10 , Issue.1 , pp. 49-62
    • Drejer, J.1    Larsson, O.M.2    Kvamme, E.3
  • 21
    • 0035577775 scopus 로고    scopus 로고
    • Differential expression of glutamate dehydrogenase in cultured neurons and astrocytes from mouse cerebellum and cerebral cortex
    • DOI 10.1002/jnr.10058
    • Zaganas I, Waagepetersen HS, Georgopoulos P, Sonnewald U, Plaitakis A, Schousboe A (2001) Differential expression of glutamate dehydrogenase in cultured neurons and astrocytes from mouse cerebellum and cerebral cortex. J Neurosci Res 66:909-913 (Pubitemid 33126393)
    • (2001) Journal of Neuroscience Research , vol.66 , Issue.5 , pp. 909-913
    • Qu, H.1    Konradsen, J.R.2    Van Hengel, M.3    Wolt, S.4    Sonnewald, U.5
  • 22
    • 0021966194 scopus 로고
    • Isolation of astrocytes, neurons, and synaptosomes of rat brain cortex: Distribution of enzymes of glutamate metabolism
    • DOI 10.1007/BF00964570
    • Subbalakshmi GY, Murthy CR (1985) Isolation of astrocytes, neurons, and synaptosomes of rat brain cortex: distribution of enzymes of glutamate metabolism. Neurochem Res 10:239-250 (Pubitemid 15087740)
    • (1985) Neurochemical Research , vol.10 , Issue.2 , pp. 239-250
    • Subbalakshmi, G.Y.C.V.1    Murthy C.., R.K.2
  • 23
    • 0021249724 scopus 로고
    • Regional development of glutamate dehydrogenase in the rat brain
    • Leong SF, Clark JB (1984) Regional development of glutamate dehydrogenase in the rat brain. J Neurochem 43:106-111 (Pubitemid 14083322)
    • (1984) Journal of Neurochemistry , vol.43 , Issue.1 , pp. 106-111
    • Leong, S.F.1    Clark, J.B.2
  • 24
    • 0020345943 scopus 로고
    • Topographic and quantitative characteristics of glutamate dehydrogenase of the hippocampus formation during the postnatal development of the rat brain: Comparative studies on succinate and alpha-glycerophosphate dehydrogenase with special reference to putatively glutamatergic structures
    • Schunzel G, Wolf G (1982) Topographic and quantitative characteristics of glutamate dehydrogenase of the hippocampus formation during the postnatal development of the rat brain: comparative studies on succinate and alpha-glycerophosphate dehydrogenase with special reference to putatively glutamatergic structures. Acta Histochem 71:145-151
    • (1982) Acta Histochem , vol.71 , pp. 145-151
    • Schunzel, G.1    Wolf, G.2
  • 25
    • 0025696513 scopus 로고
    • Immunohistochemical demonstration of glutamate dehydrogenase in the postnatally developing rat hippocampal formation and cerebellar cortex: Comparison to activity staining
    • Rothe F, Wolf G, Schunzel G (1990) Immunohistochemical demonstration of glutamate dehydrogenase in the postnatally developing rat hippocampal formation and cerebellar cortex: comparison to activity staining. Neuroscience 39:419-429
    • (1990) Neuroscience , vol.39 , pp. 419-429
    • Rothe, F.1    Wolf, G.2    Schunzel, G.3
  • 26
    • 11344253878 scopus 로고    scopus 로고
    • Developmental expression of glutamate transporters and glutamate dehydrogenase in astrocytes of the postnatal rat hippocampus
    • DOI 10.1002/hipo.20015
    • Kugler P, Schleyer V (2004) Developmental expression of glutamate transporters and glutamate dehydrogenase in astrocytes of the postnatal rat hippocampus. Hippocampus 14:975-985 (Pubitemid 40073658)
    • (2004) Hippocampus , vol.14 , Issue.8 , pp. 975-985
    • Kugler, P.1    Schleyer, V.2
  • 27
    • 0022483611 scopus 로고
    • Histochemical demonstration of sodium-dependent glutamate uptake in brain tissues by glutamate dehydrogenase reaction
    • Wolf G, Schunzel G, Rothe F (1986) Histochemical demonstration of sodium-dependent glutamate uptake in brain tissues by glutamate dehydrogenase reaction. Exp Brain Res 62:659-662 (Pubitemid 16035949)
    • (1986) Experimental Brain Research , vol.62 , Issue.3 , pp. 659-662
    • Wolf, G.1    Schunzel, G.2    Rothe, F.3
  • 28
    • 0023192573 scopus 로고
    • Glutamate dehydrogenase in aminoacidergic structures of the postnatally developing rat cerebellum
    • DOI 10.1016/0304-3940(87)90552-0
    • Wolf G, Schunzel G (1987) Glutamate dehydrogenase in aminoacidergic structures of the postnatally developing rat cerebellum. Neurosci Lett 78:7-11 (Pubitemid 17086550)
    • (1987) Neuroscience Letters , vol.78 , Issue.1 , pp. 7-11
    • Wolf, G.1    Schunzel, G.2
  • 29
    • 0034058324 scopus 로고    scopus 로고
    • Glutamate transport and metabolism in dopaminergic neurons of substantia nigra: Implications for the pathogenesis of Parkinson's disease
    • Plaitakis A, Shashidharan P (2000) Glutamate transport and metabolism in dopaminergic neurons of substantia nigra: implications for the pathogenesis of Parkinson's disease. J Neurol 247(Suppl 2):Ii25-Ii35
    • (2000) J Neurol , vol.247 , Issue.SUPPL. 2
    • Plaitakis, A.1    Shashidharan, P.2
  • 30
    • 0023572285 scopus 로고
    • Glial glutamate dehydrogenase: Ultrastructural localization and regional distribution in relation to the mitochondrial enzyme, cytochrome oxidase
    • DOI 10.1002/jnr.490180207
    • Aoki C, Milner TA, Berger SB, Sheu KF, Blass JP, Pickel VM (1987) Glial glutamate dehydrogenase: ultrastructural localization and regional distribution in relation to the mitochondrial enzyme, cytochrome oxidase. J Neurosci Res 18:305-318 (Pubitemid 18016459)
    • (1987) Journal of Neuroscience Research , vol.18 , Issue.2 , pp. 305-318
    • Aoki, C.1    Milner, T.A.2    Berger, S.B.3    Sheu, K.-F.R.4    Blass, J.P.5    Pickel, V.M.6
  • 31
    • 0023372146 scopus 로고
    • Regional distribution of astrocytes with intense immunoreactivity for glutamate dehydrogenase in rat brain: Implications for neuron-glia interactions in glutamate transmission
    • Aoki C, Milner TA, Sheu KF, Blass JP, Pickel VM (1987) Regional distribution of astrocytes with intense immunoreactivity for glutamate dehydrogenase in rat brain: implications for neuron-glia interactions in glutamate transmission. J Neurosci 7:2214-2231
    • (1987) J Neurosci , vol.7 , pp. 2214-2231
    • Aoki, C.1    Milner, T.A.2    Sheu, K.F.3    Blass, J.P.4    Pickel, V.M.5
  • 32
    • 0023655015 scopus 로고
    • Immunohistochemical demonstration of glutamate dehydrogenase in astrocytes
    • Kaneko T, Akiyama H, Mizuno N (1987) Immunohistochemical demonstration of glutamate dehydrogenase in astrocytes. Neurosci Lett 77:171-175
    • (1987) Neurosci Lett , vol.77 , pp. 171-175
    • Kaneko, T.1    Akiyama, H.2    Mizuno, N.3
  • 33
    • 0023145046 scopus 로고
    • Immunocytochemical characterization of glutamate dehydrogenase in the cerebellum of the rat
    • DOI 10.1111/j.1471-4159.1987.tb04140.x
    • Wenthold RJ, Altschuler RA, Skaggs KK, Reeks KA (1987) Immunocytochemical characterization of glutamate dehydrogenase in the cerebellum of the rat. J Neurochem 48:636-643 (Pubitemid 17005179)
    • (1987) Journal of Neurochemistry , vol.48 , Issue.2 , pp. 636-643
    • Wenthold, R.J.1    Altschuler, R.A.2    Skaggs, K.K.3    Reeks, K.A.4
  • 34
    • 0028036505 scopus 로고
    • Quantitative ultrastructural localization of glutamate dehydrogenase in the rat cerebellar cortex
    • DOI 10.1016/0306-4522(94)90349-2
    • Rothe F, Brosz M, Storm-Mathisen J (1994) Quantitative ultrastructural localization of glutamate dehydrogenase in the rat cerebellar cortex. Neuroscience 62:1133-1146 (Pubitemid 24335607)
    • (1994) Neuroscience , vol.62 , Issue.4 , pp. 1133-1146
    • Rothe, F.1    Brosz, M.2    Storm-Mathisen, J.3
  • 36
    • 0023923289 scopus 로고
    • Immunocytochemical localization of glutamate dehydrogenase in mitochondria of the cerebellum: An ultrastructural study using a monoclonal antibody
    • Madl JE, Clements JR, Beitz AJ, Wenthold RJ, Larson AA (1988) Immunocytochemical localization of glutamate dehydrogenase in mitochondria of the cerebellum: an ultrastructural study using a monoclonal antibody. Brain Res 452:396-402
    • (1988) Brain Res , vol.452 , pp. 396-402
    • Madl, J.E.1    Clements, J.R.2    Beitz, A.J.3    Wenthold, R.J.4    Larson, A.A.5
  • 38
    • 21444445235 scopus 로고    scopus 로고
    • Interpreting expression profiles of cancers by genome-wide survey of breadth of expression in normal tissues
    • DOI 10.1016/j.ygeno.2005.04.008, PII S0888754305001114
    • Ge X, Yamamoto S, Tsutsumi S, Midorikawa Y, Ihara S, Wang SM, Aburatani H (2005) Interpreting expression profiles of cancers by genome-wide survey of breadth of expression in normal tissues. Genomics 86:127-141 (Pubitemid 40917220)
    • (2005) Genomics , vol.86 , Issue.2 , pp. 127-141
    • Ge, X.1    Yamamoto, S.2    Tsutsumi, S.3    Midorikawa, Y.4    Ihara, S.5    Wang, S.M.6    Aburatani, H.7
  • 39
    • 84865755077 scopus 로고    scopus 로고
    • Expression of human GLUD2 glutamate dehydrogenase in human tissues: Functional implications
    • Zaganas I, Spanaki C, Plaitakis A (2012) Expression of human GLUD2 glutamate dehydrogenase in human tissues: functional implications. Neurochem Int 61:455-462
    • (2012) Neurochem Int , vol.61 , pp. 455-462
    • Zaganas, I.1    Spanaki, C.2    Plaitakis, A.3
  • 40
    • 0034911054 scopus 로고    scopus 로고
    • Multiple sclerosis: Altered glutamate homeostasis in lesions correlates with oligodendrocyre and axonal damage
    • DOI 10.1002/ana.1077
    • Werner P, Pitt D, Raine CS (2001) Multiple sclerosis: altered glutamate homeostasis in lesions correlates with oligodendrocyte and axonal damage. Ann Neurol 50:169-180 (Pubitemid 32738141)
    • (2001) Annals of Neurology , vol.50 , Issue.2 , pp. 169-180
    • Werner, P.1    Pitt, D.2    Raine, C.S.3
  • 41
    • 50849144657 scopus 로고    scopus 로고
    • Mitochondrial targeting adaptation of the hominoid-specific glutamate dehydrogenase driven by positive Darwinian selection
    • Rosso L, Marques AC, Reichert AS, Kaessmann H (2008) Mitochondrial targeting adaptation of the hominoid-specific glutamate dehydrogenase driven by positive Darwinian selection. PLoS Genet 4:e1000150
    • (2008) PLoS Genet , vol.4
    • Rosso, L.1    Marques, A.C.2    Reichert, A.S.3    Kaessmann, H.4
  • 42
    • 0026515847 scopus 로고
    • Histochemical demonstration of glutamate dehydrogenase and phosphate-activated glutaminase activities in semithin sections of the rat retina
    • Gebhard R (1992) Histochemical demonstration of glutamate dehydrogenase and phosphate-activated glutaminase activities in semithin sections of the rat retina. Histochemistry 97:101-103
    • (1992) Histochemistry , vol.97 , pp. 101-103
    • Gebhard, R.1
  • 43
    • 84896714403 scopus 로고    scopus 로고
    • Changes of glutamate dehydrogenase (GDH) activity in the retina of rats with short-term itraoacular (IOP) elevation
    • E-Abstract 4092
    • Shen F, Danias J, Lee HK, Chen B, Lee KC, Su YL, Podos SM, Mittag T (2002) Changes of glutamate dehydrogenase (GDH) activity in the retina of rats with short-term itraoacular (IOP) elevation. Invest Ophthalmol Vis Sci 43:E-Abstract 4092
    • (2002) Invest Ophthalmol Vis Sci , vol.43
    • Shen, F.1    Danias, J.2    Lee, H.K.3    Chen, B.4    Lee, K.C.5    Su, Y.L.6    Podos, S.M.7    Mittag, T.8
  • 45
    • 0015338758 scopus 로고
    • Symposium on acid-base homeostasis: Control of renal production of ammonia
    • Pitts RF (1972) Symposium on acid-base homeostasis: control of renal production of ammonia. Kidney Int 1:297-305
    • (1972) Kidney Int , vol.1 , pp. 297-305
    • Pitts, R.F.1
  • 46
    • 0029785988 scopus 로고    scopus 로고
    • Ammonia and glutamine metabolism during liver insufficiency: The role of kidney and brain in interorgan nitrogen exchange
    • Dejong CH, Deutz NE, Soeters PB (1996) Ammonia and glutamine metabolism during liver insufficiency: the role of kidney and brain in interorgan nitrogen exchange. Scand J Gastroenterol 31(Suppl 218):61-77.
    • (1996) Scand J Gastroenterol , vol.31 , Issue.SUPPL. 218 , pp. 61-77
    • Dejong, C.H.1    Deutz, N.E.2    Soeters, P.B.3
  • 49
    • 0032698449 scopus 로고    scopus 로고
    • Newer aspects of glutamine/glutamate metabolism: The role of acute pH changes
    • Nissim I (1999) Newer aspects of glutamine/glutamate metabolism: the role of acute pH changes. Am J Physiol 277:F493-F497
    • (1999) Am J Physiol , vol.277
    • Nissim, I.1
  • 50
    • 40149094508 scopus 로고    scopus 로고
    • Genome-wide gene expression profiling reveals renal genes regulated during metabolic acidosis
    • DOI 10.1152/physiolgenomics.00160.2007
    • Nowik M, Lecca MR, Velic A, Rehrauer H, Brandli AW, Wagner CA (2008) Genome-wide gene expression profiling reveals renal genes regulated during metabolic acidosis. Physiol Genomics 32:322-334 (Pubitemid 351328555)
    • (2008) Physiological Genomics , vol.32 , Issue.3 , pp. 322-334
    • Nowik, M.1    Lecca, M.R.2    Velic, A.3    Rehrauer, H.4    Brandli, A.W.5    Wagner, C.A.6
  • 51
    • 80052265272 scopus 로고    scopus 로고
    • The human GLUD2 glutamate dehydrogenase and its regulation in health and disease
    • Plaitakis A, Latsoudis H, Spanaki C (2011) The human GLUD2 glutamate dehydrogenase and its regulation in health and disease. Neurochem Int 59:495-509
    • (2011) Neurochem Int , vol.59 , pp. 495-509
    • Plaitakis, A.1    Latsoudis, H.2    Spanaki, C.3
  • 53
    • 0027442441 scopus 로고
    • Experimental evidence that the physiological position of the liver within the circulation is not a major determinant of zonation of gene expression
    • DOI 10.1016/0270-9139(93)90471-X
    • Wagenaar GT, Chamuleau RA, de Haan JG, Maas MA, de Boer PA, Marx F, Moorman AF, Frederiks WM, Lamers WH (1993) Experimental evidence that the physiological position of the liver within the circulation is not a major determinant of zonation of gene expression. Hepatology 18:1144-1153 (Pubitemid 23320446)
    • (1993) Hepatology , vol.18 , Issue.5 , pp. 1144-1153
    • Wagenaar, G.T.M.1    Chamuleau, R.A.F.M.2    De Haan, J.G.3    Maas, M.A.W.4    De Boer, P.A.J.5    Marx, F.6    Moorman, A.F.M.7    Frederiks, W.M.8    Lamers, W.H.9
  • 54
    • 0025049516 scopus 로고
    • Expression patterns of mRNAs for ammonia-metabolizing enzymes in the developing rat: The ontogenesis of hepatocyte heterogeneity
    • Moorman AF, De Boer PA, Das AT, Labruyere WT, Charles R, Lamers WH (1990) Expression patterns of mRNAs for ammo-nia- metabolizing enzymes in the developing rat: the ontogenesis of hepatocyte heterogeneity. Histochem J 22:457-468 (Pubitemid 20327231)
    • (1990) Histochemical Journal , vol.22 , Issue.9 , pp. 457-468
    • Moorman, A.F.M.1    De Boer, P.A.J.2    Das, A.T.3    Labruyere, W.T.4    Charles, R.5    Lamers, W.H.6
  • 56
    • 0019522512 scopus 로고
    • Multihormonal control of enzyme clusters in rat liver ontogenesis. I. Effects of adrenalectomy and gonadectomy
    • DOI 10.1016/0047-6374(81)90009-9
    • Lamers WH, Mooren PG (1981) Multihormonal control of enzyme clusters in rat liver ontogenesis I: effects of adrenalectomy and gonadectomy. Mech Ageing Dev 15:77-92 (Pubitemid 11110078)
    • (1981) Mechanisms of Ageing and Development , vol.15 , Issue.1 , pp. 77-92
    • Lamers, W.H.1    Mooren, P.G.2
  • 57
    • 0019864114 scopus 로고
    • Multihormonal control of enzyme clusters in rat liver ontogenesis. II. Role of glucocorticosteroid and thyroid hormone and of glucagon and insulin
    • DOI 10.1016/0047-6374(81)90010-5
    • Lamers WH, Mooren PG (1981) Multihormonal control of enzyme clusters in rat liver ontogenesis II: role of glucocorticosteroid and thyroid hormone and of glucagon and insulin. Mech Ageing Dev 15:93-118 (Pubitemid 11110079)
    • (1981) Mechanisms of Ageing and Development , vol.15 , Issue.1 , pp. 93-118
    • Lamers, W.H.1    Mooren, P.G.2
  • 58
    • 0019448577 scopus 로고
    • Changes in the control of enzyme clusters in the liver of adult and senescent rats
    • DOI 10.1016/0047-6374(81)90011-7
    • Lamers WH, Mooren PG (1981) Changes in the control of enzyme clusters in the liver of adult and senescent rats. Mech Ageing Dev 15:119-128 (Pubitemid 11110080)
    • (1981) Mechanisms of Ageing and Development , vol.15 , Issue.1 , pp. 119-128
    • Lamers, W.H.1    Mooren, P.G.2
  • 62
    • 0000597418 scopus 로고
    • Cell heterogeneity within the hepatic lobule of the rat: Staining reactions
    • Novikoff AB (1959) Cell heterogeneity within the hepatic lobule of the rat: staining reactions. J Histochem Cytochem 7:240-244
    • (1959) J Histochem Cytochem , vol.7 , pp. 240-244
    • Novikoff, A.B.1
  • 63
    • 0018665854 scopus 로고
    • Microphotometric studies on intraacinar enzyme distribution in rat liver
    • Wimmer M, Pette D (1979) Microphotometric studies on intraacinar enzyme distribution in rat liver. Histochemistry 64:23-33 (Pubitemid 10210109)
    • (1979) Histochemistry , vol.64 , Issue.1 , pp. 23-33
    • Wimmer, M.1    Pette, D.2
  • 64
    • 0025799609 scopus 로고
    • Microquantitative analysis of the intraacina profiles of glutamate dehydrogenase in rat liver
    • Maly IP, Sasse D (1991) Microquantitative analysis of the intraacina profiles of glutamate dehydrogenase in rat liver. J Histochem Cytochem 39:1121-1124
    • (1991) J Histochem Cytochem , vol.39 , pp. 1121-1124
    • Maly, I.P.1    Sasse, D.2
  • 65
    • 0014082605 scopus 로고
    • The redox state of free nicotinamide-adenine dinucleotide in the cytoplasm and mitochondria of rat liver
    • Williamson DH, Lund P, Krebs HA (1967) The redox state of free nicotinamide-adenine dinucleotide in the cytoplasm and mitochondria of rat liver. Biochem J 103:514-527
    • (1967) Biochem J , vol.103 , pp. 514-527
    • Williamson, D.H.1    Lund, P.2    Krebs, H.A.3
  • 66
    • 77955533490 scopus 로고    scopus 로고
    • From metabolic cycles to compartmentation: Another first for Krebs
    • Halestrap APBJ (2008) From metabolic cycles to compartmentation: another first for Krebs. Biochemistry 30:24-28
    • (2008) Biochemistry , vol.30 , pp. 24-28
    • Halestrap, A.P.B.J.1
  • 67
    • 78449311212 scopus 로고    scopus 로고
    • The simultaneous determination of NAD(H) and NADP(H) utilization by glutamate dehydrogenase
    • Treberg JR, Brosnan ME, Brosnan JT (2010) The simultaneous determination of NAD(H) and NADP(H) utilization by glutamate dehydrogenase. Mol Cell Biochem 344:253-259
    • (2010) Mol Cell Biochem , vol.344 , pp. 253-259
    • Treberg, J.R.1    Brosnan, M.E.2    Brosnan, J.T.3
  • 68
    • 77952626170 scopus 로고    scopus 로고
    • Systemic activation of glutamate dehydrogenase increases renal ammoniagenesis: Implications for the hyperinsulinism/hyperammonemia syndrome
    • Treberg JR, Clow KA, Greene KA, Brosnan ME, Brosnan JT (2010) Systemic activation of glutamate dehydrogenase increases renal ammoniagenesis: implications for the hyperinsulinism/hyperammonemia syndrome. Am J Physiol Endocrinol Metab 298:E1219-E1225
    • (2010) Am J Physiol Endocrinol Metab , vol.298
    • Treberg, J.R.1    Clow, K.A.2    Greene, K.A.3    Brosnan, M.E.4    Brosnan, J.T.5
  • 70
    • 0030018440 scopus 로고    scopus 로고
    • 15N- labeled ammonia in the perfused rat liver
    • DOI 10.1074/jbc.271.27.16199
    • Brosnan JT, Brosnan ME, Charron R, Nissim I (1996) A mass isotopomer study of urea and glutamine synthesis from 15 N-labeled ammonia in the perfused rat liver. J Biol Chem 271:16199-16207 (Pubitemid 26236238)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.27 , pp. 16199-16207
    • Brosnan, J.T.1    Brosnan, M.E.2    Charron, R.3    Nissim, I.4
  • 71
    • 0032849897 scopus 로고    scopus 로고
    • Studies of hepatic glutamine metabolism in the perfused rat liver with (15)N-labeled glutamine
    • Nissim I, Brosnan ME, Yudkoff M, Brosnan JT (1999) Studies of hepatic glutamine metabolism in the perfused rat liver with (15)N-labeled glutamine. J Biol Chem 274:28958-28965
    • (1999) J Biol Chem , vol.274 , pp. 28958-28965
    • Nissim, I.1    Brosnan, M.E.2    Yudkoff, M.3    Brosnan, J.T.4
  • 72
    • 70349569257 scopus 로고    scopus 로고
    • Hepatic glutamate metabolism: A tale of 2 hepatocytes
    • Brosnan ME, Brosnan JT (2009) Hepatic glutamate metabolism: a tale of 2 hepatocytes. Am J Clin Nutr 90:857s-861s
    • (2009) Am J Clin Nutr , vol.90
    • Brosnan, M.E.1    Brosnan, J.T.2
  • 73
    • 0033005267 scopus 로고    scopus 로고
    • High protein diet induces pericentral glutamate dehydrogenase and ornithine aminotransferase to provide sufficient glutamate for pericentral detoxification of ammonia in rat liver lobules
    • DOI 10.1007/s004180050380
    • Boon L, Geerts WJ, Jonker A, Lamers WH, Van Noorden CJ (1999) High protein diet induces pericentral glutamate dehydrogenase and ornithine aminotransferase to provide sufficient glutamate for pericentral detoxification of ammonia in rat liver lobules. Histochem Cell Biol 111:445-452 (Pubitemid 29302024)
    • (1999) Histochemistry and Cell Biology , vol.111 , Issue.6 , pp. 445-452
    • Boon, L.1    Geerts, W.J.C.2    Jonker, A.3    Lamers, W.H.4    Van Noorden, C.J.F.5
  • 76
    • 0001766942 scopus 로고
    • Subcellular distribution of the enzymes of the glutamic acid glutamine and gamma-aminobutyric acid cycles in rat brain
    • Salganicoff L, De Robertis E (1965) Subcellular distribution of the enzymes of the glutamic acid glutamine and gamma-aminobutyric acid cycles in rat brain. J Neurochem 12:287-309
    • (1965) J Neurochem , vol.12 , pp. 287-309
    • Salganicoff, L.1    De Robertis, E.2
  • 77
    • 0017333787 scopus 로고
    • The interaction of phospholipid membranes and detergents with glutamate dehydrogenase
    • Nemat-Gorgani M, Dodd G (1977) The interaction of phospholipid membranes and detergents with glutamate dehydrogenase. Eur J Biochem 74:139-147
    • (1977) Eur J Biochem , vol.74 , pp. 139-147
    • Nemat-Gorgani, M.1    Dodd, G.2
  • 78
    • 0015932713 scopus 로고
    • Biosynthesis of glutamate dehydrogenase in rat liver: Demonstration of its microsomal localization and hypothetical mechanism of transfer to mitochondria
    • Godinot C, Lardy HA (1973) Biosynthesis of glutamate dehydrogenase in rat liver: demonstration of its microsomal localization and hypothetical mechanism of transfer to mitochondria. Biochemistry 12:2051-2060
    • (1973) Biochemistry , vol.12 , pp. 2051-2060
    • Godinot, C.1    Lardy, H.A.2
  • 79
    • 0034256931 scopus 로고    scopus 로고
    • Differential distribution of the enzymes glutamate dehydrogenase and aspartate aminotransferase in cortical synaptic mitochondria contributes to metabolic compartmentation in cortical synaptic terminals
    • DOI 10.1016/S0197-0186(00)00042-5, PII S0197018600000425
    • McKenna MC, Stevenson JH, Huang X, Hopkins IB (2000) Differential distribution of the enzymes glutamate dehydrogenase and aspartate aminotransferase in cortical synaptic mitochondria contributes to metabolic compartmentation in cortical synaptic terminals. Neurochem Int 37:229-241 (Pubitemid 30254155)
    • (2000) Neurochemistry International , vol.37 , Issue.2-3 , pp. 229-241
    • McKenna, M.C.1    Stevenson, J.H.2    Huang, X.3    Hopkins, I.B.4
  • 80
    • 0018338308 scopus 로고
    • Preparation of synaptic and nonsynaptic mitochondria from mammalian brain
    • Lai JC, Clark JB (1979) Preparation of synaptic and nonsynaptic mitochondria from mammalian brain.Methods Enzymol 55:51-60 81.
    • (1979) Methods Enzymol , vol.55 , pp. 51-6081
    • Lai, J.C.1    Clark, J.B.2
  • 82
    • 0016698172 scopus 로고
    • Detection of structural differences between nuclear and mitochondrial glutamate dehydrogenases by the use of immunoadsorbents
    • di Prisco G, Casola L (1975) Detection of structural differences between nuclear and mitochondrial glutamate dehydrogenases by the use of immunoadsorbents. Biochemistry 14:4679-4683
    • (1975) Biochemistry , vol.14 , pp. 4679-4683
    • Di Prisco, G.1    Casola, L.2
  • 83
    • 0016238889 scopus 로고
    • Purification and some properties of glutamate dehydrogenase from ox liver nuclei
    • di Prisco G, Garofano F (1974) Purification and some properties of glutamate dehydrogenase from ox liver nuclei. Biochem Biophys Res Commun 58:683-689
    • (1974) Biochem Biophys Res Commun , vol.58 , pp. 683-689
    • Di Prisco, G.1    Garofano, F.2
  • 84
    • 0022454117 scopus 로고
    • The subcellular localization of glutamate dehydrogenase (GDH): Is GDH a marker for mitochondria brain?
    • Lai JC, Sheu KF, Kim YT, Clarke DD, Blass JP (1986) The subcellular localization of glutamate dehydrogenase (GDH): is GDH a marker for mitochondria in brain? Neurochem Res 11:733-744 (Pubitemid 16077125)
    • (1986) Neurochemical Research , vol.11 , Issue.5 , pp. 733-744
    • Lai, J.C.K.1    Sheu, K.R.2    Kim, Y.T.3
  • 85
    • 0021340557 scopus 로고
    • Neurological disorders associated with deficiency of glutamate dehydrogenase
    • Plaitakis A, Berl S, Yahr MD (1984) Neurological disorders associated with deficiency of glutamate dehydrogenase. Ann Neurol 15:144-153 (Pubitemid 14188521)
    • (1984) Annals of Neurology , vol.15 , Issue.2 , pp. 144-153
    • Plaitakis, A.1    Berl, S.2    Yahr, M.D.3
  • 87
    • 0022646352 scopus 로고
    • Purification and characterization of a soluble and a particulate glutamate dehydrogenase from rat brain
    • Colon AD, Plaitakis A, Perakis A, Berl S, Clarke DD (1986) Purification and characterization of a soluble and a particulate glutamate dehydrogenase from rat brain. J Neurochem 46:1811-1819 (Pubitemid 16095488)
    • (1986) Journal of Neurochemistry , vol.46 , Issue.6 , pp. 1811-1819
    • Colon, A.D.1    Plaitakis, A.2    Perakis, A.3
  • 88
    • 0033427740 scopus 로고    scopus 로고
    • Purification and characterization of glutamate dehydrogenase as another isoprotein binding to the membrane of rough endoplasmic reticulum
    • DOI 10.1002/(SICI)1097-4644(20000201)76:2244::AID
    • Lee WK, Shin S, Cho SS, Park JS (1999) Purification and characterization of glutamate dehydrogenase as another isoprotein binding to the membrane of rough endoplasmic reticulum. J Cell Biochem 76:244-253 (Pubitemid 30030772)
    • (1999) Journal of Cellular Biochemistry , vol.76 , Issue.2 , pp. 244-253
    • Lee, W.-K.1    Shin, S.2    Cho, S.S.3    Park, J.-S.4
  • 89
    • 0028783544 scopus 로고
    • Two soluble forms of glutamate dehydrogenase isoproteins from bovine brain
    • Cho SW, Lee J, Choi SY (1995) Two soluble forms of glutamate dehydrogenase isoproteins from bovine brain. Euro J Biochem 233:340-346
    • (1995) Euro J Biochem , vol.233 , pp. 340-346
    • Cho, S.W.1    Lee, J.2    Choi, S.Y.3
  • 90
    • 0027524801 scopus 로고
    • A membrane-bound form of glutamate dehydrogenase possesses an ATP-dependent high-affinity microtubule-binding activity
    • Rajas F, Rousset B (1993) A membrane-bound form of glutamate dehydrogenase possesses an ATP-dependent high-affinity microtubule-binding activity. Biochem 295:447-455 (Pubitemid 23315183)
    • (1993) Biochemical Journal , vol.295 , Issue.2 , pp. 447-455
    • Rajas, F.1    Rousset, B.2
  • 91
    • 24044453711 scopus 로고    scopus 로고
    • Proteomic profiling of hepatic endoplasmic reticulum-associated proteins in an animal model of insulin resistance and metabolic dyslipidemia
    • DOI 10.1074/jbc.M413343200
    • Morand JP, Macri J, Adeli K (2005) Proteomic profiling of hepatic endoplasmic reticulum-associated proteins in an animal model of insulin resistance and metabolic dyslipidemia. J Biol Chem 280:17626-17633 (Pubitemid 41388997)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.18 , pp. 17626-17633
    • Morand, J.-P.F.1    Macri, J.2    Adeli, K.3
  • 93
    • 0029912850 scopus 로고    scopus 로고
    • Involvement of a membrane-bound form of glutamate dehydrogenase in the association of lysosomes to microtubules
    • DOI 10.1074/jbc.271.47.29882
    • Rajas F, Gire V, Rousset B (1996) Involvement of a membrane-bound form of glutamate dehydrogenase in the association of lysosomes to microtubules. J Biol Chem 271:29882-29890 (Pubitemid 26389622)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.47 , pp. 29882-29890
    • Rajas, F.1    Gire, V.2    Rousset, B.3
  • 94
    • 84885036973 scopus 로고    scopus 로고
    • Chicken liver glutamate dehydrogenase (GDH) demonstrates a histone H3 specific protease (H3ase) activity in vitro
    • Purohit JS, Tomar RS, Panigrahi AK, Pandey SM, Singh D, Chaturvedi MM (2013) Chicken liver glutamate dehydrogenase (GDH) demonstrates a histone H3 specific protease (H3ase) activity in vitro. Biochimie 95:1999-2009
    • (2013) Biochimie , vol.95 , pp. 1999-2009
    • Purohit, J.S.1    Tomar, R.S.2    Panigrahi, A.K.3    Pandey, S.M.4    Singh, D.5    Chaturvedi, M.M.6
  • 95
    • 12244298900 scopus 로고    scopus 로고
    • Molecular basis of human glutamate dehydrogenase regulation under changing energy demands
    • DOI 10.1002/jnr.20353, Brain Energy Metabolism: Transporters, Mitochondria and Neurodegeneration
    • Mastorodemos V, Zaganas I, Spanaki C, Bessa M, Plaitakis A (2005) Molecular basis of human glutamate dehydrogenase regulation under changing energy demands. J Neurosci Res 79:65-73 (Pubitemid 40116419)
    • (2005) Journal of Neuroscience Research , vol.79 , Issue.1-2 , pp. 65-73
    • Mastorodemos, V.1    Zaganas, I.2    Spanaki, C.3    Bessa, M.4    Plaitakis, A.5
  • 96
    • 0020478808 scopus 로고
    • Rat liver L-glutamate dehydrogenase, malate dehydrogenase, D-beta-hydroxybutyrate dehydrogenase, and sulfite oxidase are each synthesized as larger precursors by cytoplasmic free polysomes
    • Mihara K, Omura T, Harano T, Brenner S, Fleischer S, Rajagopalan KV, Blobel G (1982) Rat liver L-glutamate dehydrogenase, malate dehydrogenase, D-beta-hydroxybutyrate dehydrogenase, and sulfite oxidase are each synthesized as larger precursors by cytoplasmic free polysomes. J Biol Chem 257:3355-3358
    • (1982) J Biol Chem , vol.257 , pp. 3355-3358
    • Mihara, K.1    Omura, T.2    Harano, T.3    Brenner, S.4    Fleischer, S.5    Rajagopalan, K.V.6    Blobel, G.7
  • 97
    • 84865796233 scopus 로고    scopus 로고
    • Alpha helical structures in the leader sequence of human GLUD2 glutamate dehydrogenase responsible for mitochondrial import
    • Kotzamani D, Plaitakis A (2012) Alpha helical structures in the leader sequence of human GLUD2 glutamate dehydrogenase responsible for mitochondrial import. Neurochem Int 61:463-469
    • (2012) Neurochem Int , vol.61 , pp. 463-469
    • Kotzamani, D.1    Plaitakis, A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.