TY - JOUR
T1 - Chapter 19
T2 - Ultrastructural immunocytochemical observations on the localization, metabolism and transport of glutamate in normal and ischemic brain tissue
AU - Storm-Mathisen, J.
AU - Danbolt, N. C.
AU - Rothe, F.
AU - Torp, R.
AU - Zhang, N.
AU - Aas, J. E.
AU - Kanner, B. I.
AU - Langmoen, I.
AU - Ottersen, O. P.
PY - 1992/1/1
Y1 - 1992/1/1
N2 - To study how glutamate (Glu) is handled in individual synapses, neuronal perikarya and glial cells, various methods are developed that allow the concentrations of Glu and related amino acids to be examined morphologically at the light and electron microscopic level. This technology is used to study dynamic changes in the localization of the amino acids following experimental manipulations, such as ischemia in vivo and depolarization-induced synaptic release in vitro. This chapter discusses additional examples of such use, and show how the power of the approach is further exploited by estimating the ratios of different amino acids measured simultaneously in individual tissue compartments. The localization of two proteins important for the synaptic handling of Glu— namely, glutamate dehydrogenase (GluDH) and the high-affinity [Na++K+]-coupled Glu transporter (GluTp) is discussed. GluDH catalyzes the reversible oxidative deamination of Glu to α-ketoglutarate and NH4+, and may therefore take part in the formation as well as in the breakdown of Glu. GluDH deficiency has been implicated as a pathogenetic factor in neurodegenerative disease. GluTp is responsible for clearing the synaptic cleft of Glu conserving it for reuse. However, reversed action of GluTp is probably responsible for the rise in extracellular Glu in energy-deficient state. It may therefore contribute to excitotoxic cell loss in the brain ischemia and related conditions, but may also play a role in neurodegenerative disorders.
AB - To study how glutamate (Glu) is handled in individual synapses, neuronal perikarya and glial cells, various methods are developed that allow the concentrations of Glu and related amino acids to be examined morphologically at the light and electron microscopic level. This technology is used to study dynamic changes in the localization of the amino acids following experimental manipulations, such as ischemia in vivo and depolarization-induced synaptic release in vitro. This chapter discusses additional examples of such use, and show how the power of the approach is further exploited by estimating the ratios of different amino acids measured simultaneously in individual tissue compartments. The localization of two proteins important for the synaptic handling of Glu— namely, glutamate dehydrogenase (GluDH) and the high-affinity [Na++K+]-coupled Glu transporter (GluTp) is discussed. GluDH catalyzes the reversible oxidative deamination of Glu to α-ketoglutarate and NH4+, and may therefore take part in the formation as well as in the breakdown of Glu. GluDH deficiency has been implicated as a pathogenetic factor in neurodegenerative disease. GluTp is responsible for clearing the synaptic cleft of Glu conserving it for reuse. However, reversed action of GluTp is probably responsible for the rise in extracellular Glu in energy-deficient state. It may therefore contribute to excitotoxic cell loss in the brain ischemia and related conditions, but may also play a role in neurodegenerative disorders.
UR - http://www.scopus.com/inward/record.url?scp=0027081175&partnerID=8YFLogxK
U2 - 10.1016/S0079-6123(08)61753-7
DO - 10.1016/S0079-6123(08)61753-7
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C2 - 1363142
AN - SCOPUS:0027081175
SN - 0079-6123
VL - 94
SP - 225
EP - 241
JO - Progress in Brain Research
JF - Progress in Brain Research
IS - C
ER -