메뉴 건너뛰기




Volumn 415, Issue , 2015, Pages 1-11

Expression of human GLUD1 and GLUD2 glutamate dehydrogenases in steroid producing tissues

Author keywords

Enzyme kinetics; Glutamate dehydrogenase; Immunohistochemistry; Steroid hormone; Steroidogenesis

Indexed keywords

GLUTAMATE DEHYDROGENASE; GLUTAMATE DEHYDROGENASE 1; GLUTAMATE DEHYDROGENASE 2; UNCLASSIFIED DRUG; GLUD1 PROTEIN, HUMAN; GLUD2 PROTEIN, HUMAN; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; STEROID;

EID: 84942577114     PISSN: 03037207     EISSN: 18728057     Source Type: Journal    
DOI: 10.1016/j.mce.2015.07.020     Document Type: Article
Times cited : (17)

References (30)
  • 2
    • 84921024562 scopus 로고    scopus 로고
    • Determination of glutamate dehydrogenase activity and its kinetics in mouse tissues using metabolic mapping (quantitative enzyme histochemistry)
    • Botman D., Tigchelaar W., Van Noorden C.J. Determination of glutamate dehydrogenase activity and its kinetics in mouse tissues using metabolic mapping (quantitative enzyme histochemistry). J. Histochem. Cytochem. 2014, 62:802-812.
    • (2014) J. Histochem. Cytochem. , vol.62 , pp. 802-812
    • Botman, D.1    Tigchelaar, W.2    Van Noorden, C.J.3
  • 3
    • 6944242766 scopus 로고    scopus 로고
    • Birth and adaptive evolution of a hominoid gene that supports high neurotransmitter flux
    • Burki F., Kaessmann H. Birth and adaptive evolution of a hominoid gene that supports high neurotransmitter flux. Nat. Genet. 2004, 36:1061-1063.
    • (2004) Nat. Genet. , vol.36 , pp. 1061-1063
    • Burki, F.1    Kaessmann, H.2
  • 5
    • 34547093211 scopus 로고    scopus 로고
    • Amino acid changes within antenna helix are responsible for different regulatory preferences of human glutamate dehydrogenase isozymes
    • Choi M.M., Kim E.A., Yang S.J., Choi S.Y., Cho S.W., Huh J.W. Amino acid changes within antenna helix are responsible for different regulatory preferences of human glutamate dehydrogenase isozymes. J. Biol. Chem. 2007, 282:19510-19517.
    • (2007) J. Biol. Chem. , vol.282 , pp. 19510-19517
    • Choi, M.M.1    Kim, E.A.2    Yang, S.J.3    Choi, S.Y.4    Cho, S.W.5    Huh, J.W.6
  • 6
    • 84871412362 scopus 로고    scopus 로고
    • The role of glutamine synthetase and glutamate dehydrogenase in cerebral ammonia homeostasis
    • Cooper A.J. The role of glutamine synthetase and glutamate dehydrogenase in cerebral ammonia homeostasis. Neurochem. Res. 2012, 37:2439-2455.
    • (2012) Neurochem. Res. , vol.37 , pp. 2439-2455
    • Cooper, A.J.1
  • 7
    • 84939574170 scopus 로고    scopus 로고
    • Differential interaction of hGDH1 and hGDH2 with manganese: implications for metabolism and toxicity
    • Epub ahead of print
    • Dimovasili C., Aschner M., Plaitakis A., Zaganas I. Differential interaction of hGDH1 and hGDH2 with manganese: implications for metabolism and toxicity. Neurochem. Int. Mar 30 2015, pii: S0197-0186(15)00047-9, (Epub ahead of print). 10.1016/j.neuint.2015.03.004.
    • (2015) Neurochem. Int.
    • Dimovasili, C.1    Aschner, M.2    Plaitakis, A.3    Zaganas, I.4
  • 8
    • 0014444916 scopus 로고
    • The effect of NADPH on steroidogenesis by the human adrenal gland in vivo
    • Deshpande N., Jensen V., Bulbrook R.D., Doouss T.W. The effect of NADPH on steroidogenesis by the human adrenal gland in vivo. J. Endocrinol. 1969, 43:135-136.
    • (1969) J. Endocrinol. , vol.43 , pp. 135-136
    • Deshpande, N.1    Jensen, V.2    Bulbrook, R.D.3    Doouss, T.W.4
  • 10
    • 0029051291 scopus 로고
    • Routes and regulation of NADPH production in steroidogenic mitochondria
    • Hanukoglu I., Rapoport R. Routes and regulation of NADPH production in steroidogenic mitochondria. Endocr. Res. 1995, 21:231-241.
    • (1995) Endocr. Res. , vol.21 , pp. 231-241
    • Hanukoglu, I.1    Rapoport, R.2
  • 11
    • 35848964803 scopus 로고    scopus 로고
    • Properties and molecular evolution of human GLUD2 (neural and testicular tissue-specific) glutamate dehydrogenase
    • Kanavouras K., Mastorodemos V., Borompokas N., Spanaki C., Plaitakis A. Properties and molecular evolution of human GLUD2 (neural and testicular tissue-specific) glutamate dehydrogenase. J. Neurosci. Res. 2007, 85:1101-1109.
    • (2007) J. Neurosci. Res. , vol.85 , pp. 1101-1109
    • Kanavouras, K.1    Mastorodemos, V.2    Borompokas, N.3    Spanaki, C.4    Plaitakis, A.5
  • 13
    • 81855211988 scopus 로고    scopus 로고
    • Early steps in steroidogenesis: intracellular cholesterol trafficking
    • Miller W.L., Bose H.S. Early steps in steroidogenesis: intracellular cholesterol trafficking. J. Lipid Res. 2011, 52:2111-2135.
    • (2011) J. Lipid Res. , vol.52 , pp. 2111-2135
    • Miller, W.L.1    Bose, H.S.2
  • 14
    • 10644266103 scopus 로고    scopus 로고
    • Overview of steroidogenic enzymes in the pathway from cholesterol to active steroid hormones
    • Payne A.H., Hales D.B. Overview of steroidogenic enzymes in the pathway from cholesterol to active steroid hormones. Endocr. Rev. 2004, 25:947-970.
    • (2004) Endocr. Rev. , vol.25 , pp. 947-970
    • Payne, A.H.1    Hales, D.B.2
  • 16
    • 80052265272 scopus 로고    scopus 로고
    • The human GLUD2 glutamate dehydrogenase and its regulation in health and disease
    • Plaitakis A., Latsoudis H., Spanaki C. The human GLUD2 glutamate dehydrogenase and its regulation in health and disease. Neurochem. Int. 2011, 59:495-509.
    • (2011) Neurochem. Int. , vol.59 , pp. 495-509
    • Plaitakis, A.1    Latsoudis, H.2    Spanaki, C.3
  • 17
    • 0028036505 scopus 로고
    • Quantitative ultrastructural localization of glutamate dehydrogenase in the rat cerebellar cortex
    • Rothe F., Brosz M., Storm-Mathisen J. Quantitative ultrastructural localization of glutamate dehydrogenase in the rat cerebellar cortex. Neuroscience 1994, 62:1133-1146.
    • (1994) Neuroscience , vol.62 , pp. 1133-1146
    • Rothe, F.1    Brosz, M.2    Storm-Mathisen, J.3
  • 18
    • 0028341884 scopus 로고
    • Novel human glutamate dehydrogenase expressed in neural and testicular tissues and encoded by an X-linked intronless gene
    • Shashidharan P., Michaelidis T.M., Robakis N.K., Kresovali A., Papamatheakis J., Plaitakis A. Novel human glutamate dehydrogenase expressed in neural and testicular tissues and encoded by an X-linked intronless gene. J. Biol. Chem. 1994, 269:16971-16976.
    • (1994) J. Biol. Chem. , vol.269 , pp. 16971-16976
    • Shashidharan, P.1    Michaelidis, T.M.2    Robakis, N.K.3    Kresovali, A.4    Papamatheakis, J.5    Plaitakis, A.6
  • 20
    • 77952778182 scopus 로고    scopus 로고
    • Human GLUD2 glutamate dehydrogenase is expressed in neural and testicular supporting cells
    • Spanaki C., Zaganas I., Kleopa K.A., Plaitakis A. Human GLUD2 glutamate dehydrogenase is expressed in neural and testicular supporting cells. J. Biol. Chem. 2010, 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
  • 21
    • 84865790575 scopus 로고    scopus 로고
    • The complex regulation of human glud1 and glud2 glutamate dehydrogenases and its implications in nerve tissue biology
    • Spanaki C., Zaganas I., Kounoupa Z., Plaitakis A. The complex regulation of human glud1 and glud2 glutamate dehydrogenases and its implications in nerve tissue biology. Neurochem. Int. 2012, 61:470-481.
    • (2012) Neurochem. Int. , vol.61 , pp. 470-481
    • Spanaki, C.1    Zaganas, I.2    Kounoupa, Z.3    Plaitakis, A.4
  • 22
    • 84896718850 scopus 로고    scopus 로고
    • Heterogeneous cellular distribution of glutamate dehydrogenase in brain and in non-neural tissues
    • Spanaki C., Kotzamani D., Petraki Z., Drakos E., Plaitakis A. Heterogeneous cellular distribution of glutamate dehydrogenase in brain and in non-neural tissues. Neurochem. Res. 2014, 39:500-515.
    • (2014) Neurochem. Res. , vol.39 , pp. 500-515
    • Spanaki, C.1    Kotzamani, D.2    Petraki, Z.3    Drakos, E.4    Plaitakis, A.5
  • 24
    • 0030031783 scopus 로고    scopus 로고
    • Placental steroid hormone synthesis: unique features and unanswered questions
    • Strauss J.F., Martinez F., Kiriakidou M. Placental steroid hormone synthesis: unique features and unanswered questions. Biol. Reprod. 1996, 54:303-311.
    • (1996) Biol. Reprod. , vol.54 , pp. 303-311
    • Strauss, J.F.1    Martinez, F.2    Kiriakidou, M.3
  • 25
    • 84896735005 scopus 로고    scopus 로고
    • Intertissue differences for the role of glutamate dehydrogenase in metabolism
    • Treberg J.R., Banh S., Pandey U., Weihrauch D. Intertissue differences for the role of glutamate dehydrogenase in metabolism. Neurochem. Res. 2014, 39:516-526.
    • (2014) Neurochem. Res. , vol.39 , pp. 516-526
    • Treberg, J.R.1    Banh, S.2    Pandey, U.3    Weihrauch, D.4
  • 26
    • 0015233817 scopus 로고
    • Role of reversed electron transport in bovine corpus luteum mitochondrial steroid synthesis
    • Uzgiris V.I., McIntosh E.N., Alonso C., Salhanick H.A. Role of reversed electron transport in bovine corpus luteum mitochondrial steroid synthesis. Biochemistry 1971, 10:2916-2923.
    • (1971) Biochemistry , vol.10 , pp. 2916-2923
    • Uzgiris, V.I.1    McIntosh, E.N.2    Alonso, C.3    Salhanick, H.A.4
  • 27
    • 32044465506 scopus 로고    scopus 로고
    • TOR signaling in growth and metabolism
    • Wullschleger S., Loewith R., Hall M.N. TOR signaling in growth and metabolism. Cell 2006, 124:471-484.
    • (2006) Cell , vol.124 , pp. 471-484
    • Wullschleger, S.1    Loewith, R.2    Hall, M.N.3
  • 28
    • 0037135619 scopus 로고    scopus 로고
    • Single amino acid substitution (G456A) in the vicinity of the GTP binding domain of human housekeeping glutamate dehydrogenase markedly attenuates GTP inhibition and abolishes the cooperative behavior of the enzyme
    • Zaganas I., Plaitakis A. Single amino acid substitution (G456A) in the vicinity of the GTP binding domain of human housekeeping glutamate dehydrogenase markedly attenuates GTP inhibition and abolishes the cooperative behavior of the enzyme. J. Biol. Chem. 2002, 277:26422-26428.
    • (2002) J. Biol. Chem. , vol.277 , pp. 26422-26428
    • Zaganas, I.1    Plaitakis, A.2
  • 29
    • 0037195942 scopus 로고    scopus 로고
    • Substitution of Ser for Arg-443 in the regulatory domain of human housekeeping (GLUD1) glutamate dehydrogenase virtually abolishes basal activity and markedly alters the activation of the enzyme by ADP and L-leucine
    • Zaganas I., Spanaki C., Karpusas M., Plaitakis A. Substitution of Ser for Arg-443 in the regulatory domain of human housekeeping (GLUD1) glutamate dehydrogenase virtually abolishes basal activity and markedly alters the activation of the enzyme by ADP and L-leucine. J. Biol. Chem. 2002, 277:46552-46558.
    • (2002) J. Biol. Chem. , vol.277 , pp. 46552-46558
    • Zaganas, I.1    Spanaki, C.2    Karpusas, M.3    Plaitakis, A.4
  • 30
    • 84865755077 scopus 로고    scopus 로고
    • Expression of human GLUD2 glutamate dehydrogenase in human tissues: functional implications
    • Zaganas I., Spanaki C., Plaitakis A. Expression of human GLUD2 glutamate dehydrogenase in human tissues: functional implications. Neurochem. Int. 2012, 61:455-462.
    • (2012) Neurochem. Int. , vol.61 , pp. 455-462
    • Zaganas, I.1    Spanaki, C.2    Plaitakis, A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.