Literature DB >> 6661665

Postnatal changes in the activity of glutamate dehydrogenase and aspartate aminotransferase in the rat nervous system with special reference to the glutamate transmitter metabolism.

F Rothe, W Schmidt, G Wolf.   

Abstract

The activities of aspartate aminotransferase (AAT) and glutamate dehydrogenase (GIDH), the major glutamate metabolizing enzymes, were studied in hippocampal formation, cerebellar cortex, dorsal root ganglia, superior cervical ganglia and liver as a function of postnatal development. At birth, in all these nervous tissues the enzyme activities were quite low and showed similar levels (AAT 7-15 U/g wet weight; 0.18-0.23 U/mg protein; GIDH 3.4-13 U/g wet weight; 0.07-0.18 U/mg protein). Based on protein, AAT activity increased during the postnatal period studied 5.8 and 3.8 times in the hippocampal formation and cerebellar cortex, respectively, while the respective GIDH rise was 5.2 and 2.3 times. During postnatal maturation, enzyme activities in dorsal root ganglia showed only minor changes. In superior cervical ganglia, AAT and GIDH were remarkably constant. In liver the enzyme activities changed during postnatal development, but the activity curve profile was quite distinct from those obtained for brain regions. The steep rise of AAT and GIDH activities in brain regions is discussed as being a consequence of the maturation of preferably glutamatergic structures. Glutamatergic transmission processes obviously do not take place in superior cervical ganglia and dorsal root ganglia, and certainly not in liver. The present results suggest a quantitatively significant participation of glutamate transmitter metabolism in proportion to the whole glutamate metabolism of the CNS.

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Year:  1983        PMID: 6661665     DOI: 10.1016/0165-3806(83)90202-x

Source DB:  PubMed          Journal:  Brain Res        ISSN: 0006-8993            Impact factor:   3.252


  17 in total

1.  Neurochemical changes in the developing rat hippocampus during prolonged hypoglycemia.

Authors:  Raghavendra Rao; Kathleen Ennis; Jeffery D Long; Kamil Ugurbil; Rolf Gruetter; Ivan Tkac
Journal:  J Neurochem       Date:  2010-05-06       Impact factor: 5.372

2.  Changes in glutamate-related enzyme activities in the striatum of the rat following lesion of corticostriatal fibres.

Authors:  F Rothe; G Wolf
Journal:  Exp Brain Res       Date:  1990       Impact factor: 1.972

3.  High-affinity uptake of L-[3H]glutamate and D-[3H]aspartate during postnatal development of the hippocampal formation: a quantitative autoradiographic study.

Authors:  W Schmidt; G Wolf
Journal:  Exp Brain Res       Date:  1988       Impact factor: 1.972

4.  Histochemical demonstration of sodium-dependent glutamate uptake in brain tissues by glutamate dehydrogenase reaction.

Authors:  G Wolf; G Schünzel; F Rothe
Journal:  Exp Brain Res       Date:  1986       Impact factor: 1.972

Review 5.  The discovery of human of GLUD2 glutamate dehydrogenase and its implications for cell function in health and disease.

Authors:  Pullanipally Shashidharan; Andreas Plaitakis
Journal:  Neurochem Res       Date:  2013-12-19       Impact factor: 3.996

6.  Alanine aminotransferase in the rat nervous system during the postnatal development referring to the glutamate transmitter metabolism.

Authors:  F Rothe; G Wolf
Journal:  Neurochem Res       Date:  1984-05       Impact factor: 3.996

Review 7.  Heterogeneous cellular distribution of glutamate dehydrogenase in brain and in non-neural tissues.

Authors:  Cleanthe Spanaki; Dimitra Kotzamani; Zoe Petraki; Elias Drakos; Andreas Plaitakis
Journal:  Neurochem Res       Date:  2014-01-17       Impact factor: 3.996

Review 8.  In situ measurements of enzyme activities in the brain.

Authors:  P Kugler
Journal:  Histochem J       Date:  1993-05

9.  Regulation of malate dehydrogenases from neonatal, adolescent, and mature rat brain.

Authors:  P Malik; M C McKenna; J T Tildon
Journal:  Neurochem Res       Date:  1993-03       Impact factor: 3.996

10.  Ontogenetic development of glutamate metabolizing enzymes in cultured cerebellar granule cells and in cerebellum in vivo.

Authors:  J Drejer; O M Larsson; E Kvamme; G Svenneby; L Hertz; A Schousboe
Journal:  Neurochem Res       Date:  1985-01       Impact factor: 3.996

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