1983
DOI: 10.1152/physrev.1983.63.2.547
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Mitochondrial metabolism of glutamine and glutamate and its physiological significance.

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Cited by 359 publications
(220 citation statements)
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“…There are no differences in luminal uptake between GLU liberated from proteins, natural free GLU and additive GLU. All GLU taken up is used for the diverse synthesis processes in intracellular compartments (Kovacevic and McGivan, 1983;Hundal et al, 1986;Low et al, 1992).…”
Section: Physiology Of Glutamatementioning
confidence: 99%
“…There are no differences in luminal uptake between GLU liberated from proteins, natural free GLU and additive GLU. All GLU taken up is used for the diverse synthesis processes in intracellular compartments (Kovacevic and McGivan, 1983;Hundal et al, 1986;Low et al, 1992).…”
Section: Physiology Of Glutamatementioning
confidence: 99%
“…1,2 Mammalian glutaminase (GLS) is an enzyme responsible for the hydrolytic deamidation of Gln into Glutamate (Glu) and ammonium ions. Two paralogous genes on separate chromosomes encode distinct GLS isozymes: the kidney-type isozyme, GLS1, and the liver-type isozyme, GLS2.…”
Section: Introductionmentioning
confidence: 99%
“…Two paralogous genes on separate chromosomes encode distinct GLS isozymes: the kidney-type isozyme, GLS1, and the liver-type isozyme, GLS2. 3,4 Although early studies showed that GLS1 is ubiquitously expressed, 2 and that GLS2 is mainly expressed in the liver, 4 more recent observations indicate that the expression pattern is more complex. Indeed, GLS2 has also been detected in brain, 5 pancreas, 6 cancer cells, 7 and cells of the immune system.…”
Section: Introductionmentioning
confidence: 99%
“…As one of the most abundant amino acids in plasma, L-Gln is synthesised and stored in several tissues, including both lung and skeletal muscle. L-Gln becomes conditionally essential in states of severe stress in which intracellular L-Gln levels can fall by~50% and plasma concentrations by 30% (Kovacevic and McGivan 1983). A study by Singleton and Wischmeyer (2006) showed that in rats previously administered with L-Gln orally and then exposed to hyperthermic conditions, HSP expression in gut tissues was enhanced, gut permeability was reduced, and plasma endotoxin concentrations were lower than in rats exposed to hyperthermia without L-Gln supplementation.…”
Section: Heat Shock Proteins and Thermo-tolerancementioning
confidence: 99%