Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:1.4.1.2 (glutamate dehydrogenase)
 4,380 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

As part of a detailed analysis of the specific enzyme metabolism in individual hypothalamic nuclei during different endocrinological and behavioral states, quantitative distribution of a group of enzymes representative of major metabolic pathways was examined. Malic dehydrogenase (MDH), representative of the citric acid cycle, lactic dehydrogenase (LDH), of glycolysis, glutamic dehydrogenase (GDH), of glutamate metabolism, and glucoseo-6-phosphate dehydrogenase (G-6-PDH), of the pentose pathway, were measured in 11 hypothalamic nuclei, the cerebral cortex, and the cerebellum of adult female rats neonatally treated with testosterone propionate (TP). Several significant metabolic changes occurred in specific hypothalamic nuclei following neonatal TP (1 mg) treatment. MDH activity was significantly reduced in the suprachiasmatic (11%), supraoptic (13%), and anterior (9%) nuclei. No statistically significant changes occurred in nuclei of the middle or posterior hypothalamus. LDH was significantly elevated only in the lateral preoptic areas (23%). Several significant increases of G-6-PDH activity occurred in the following nuclei of the anterior hypothalamus: medial preoptic (32%), lateral preoptic (33%), supraoptic (13%), and paraventricular (23%). No statistically significant changes occurred in nuclei of the middle or posterior hypothalamus; these results were similar to those for MDH and LDH. GDH activity was generally elevated in all of the hypothalamic nuclei examined, except in the anterior nucleus. Significant increases of enzyme level were found in each of the major divisions of the hypothalamus. In the anterior hypothalamus, GDH activity in the paraventricular nucleus rose significantly (16%); in the middle hypothalamus, lateral ventromedial and arcuate nuclear levels were elevated (14 and 17%), and medial and posterior nuclear levels were higher than control values (32 and 36%) in the posterior hypothalamus.
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PMID:Quantitative histochemical studies of the hypothalamus: dehydrogenase enzymes following androgen sterilization. 41 65

In a detailed study focused on the methodological problems in dehydrogenase histochemistry [e.g., fixation, diffusion of enzymes and of reduced inermediates, conversion of NADPH and NADP to NADH and NAD, respectively, penetration of tetrazolium salt and formazan substantivity, 'nothing dehydrogenase' reaction, use of exogenous CoQ10 and of flavoprotein substitute (PMS)], the distribution and activity of succinate dehydrogenase, NAD(P)H-tetrazolium reductase, glucose-6-phosphate dehydrogenase, lactate dehydrogenase (H and M types), and of L-glutamate dehydrogenase (E.C.1.4.1.2 and E.C.1.4.1.3) have been investigated in the rat cerebellum. It was evident from the study that reliable results could only be obtained if all the aforementioned factors had been considered. The image of actual concentration of SDH in the neuropil of the molecular layer could only be recorded by adding CoQ10, while other structures exhibited greater balance between SDH and endogenous mitochondrial CoQ. Contrary to previous studies, a reversed localization of the activity of G-6-PDH and LDH was noticed. The elements of molecular and Purkinje layers were rich in G-6-PDH, while the granular layer was nearly depleted. The actual level of LDH could only be recorded if NADH-tetrazolium reductase was bypassed with PMS. The H and M types of LDH coexisted in the three cortical layers, the H type being prevalent and the M type attaining its highest level in synaptic glomeruli followed by the structures of the molecular layer and the Purkinje cells. High activity of GDH was noticed in Bergmann glia followed by synaptic glomeruli, while most other structures showed weak to moderate activity. The two GDH types coexisted in all structures showing activity, except for Bergmann cells, which only showed presence of the E.C. 1.4.1.3 type. Furthermore, Bergmann glia was exceptional by showing no activity of SDH and LDH, but strong activity of G-6-PDH and NADPH-tetrazolium reductase. The granular cells were exceptional by showing weak or no activity of all enzymes in question.
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PMID:Methodological aspects of the histochemical localization and activity of some cerebellar dehydrogenases. 66 87

Within the uterine glands, the following enzymes were demonstrated by histochemical methods after 30, 58, 80, 100, and 110 d of pregnancy, respectively: beta-N-acetyl-hexosaminidase, beta-galactosidase, beta-glucuronidase, alpha-mannosidase, acid phosphatase, alkaline phosphatase, esterases, cytochrome oxidase, 5-nucleotidase, leucine aminopeptidase, adenosine triphosphatase, diaphorases (NADH, NADPH), glucose-6-phosphate dehydrogenase, 6-phosphogluconate dehydrogenase, succinate dehydrogenase, isocitrate dehydrogenase (NAD, NADP), beta-hydroxybutyrate dehydrogenase, glycero-3-phosphate dehydrogenase, NAD-glycero-3-phosphate dehydrogenase, glutamate dehydrogenase (NAD, NADP), lactate dehydrogenase. The results show that the activities of G-6-PDH, 6-PGDH, and cytochrome oxidase increase within secreting cells during the 2nd half of pregnancy. The activities of the other enzymes remained almost unchanged during the period of investigation. The description of our results distinguishes between gland neck, middle, and distal part of the secretory unit, respectively. In general, the enzyme activities are similar within the middle and distal gland segments, but lower in the epithelia of the neck region. The activity of dehydrogenases was medium to intensive within the middle and distal gland segments, but only low to medium within the neck portion. Of the hydrolases, the acid phosphatase, ATPase, leucine aminopeptidase, and beta-galactosidase demonstrated an intensive activity within activity secreting cells. The enzyme activities of the gland epithelia are compared with these of the uterine surface epithelia and the histochemical results are discussed in context with their significance in histiotrophic nutrition.
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PMID:[Enzyme histochemistry of the pig placenta. III. Histotopics of enzymes in the uterine epithelium]. 309 49

Primary roots of soybean [Glycine max (L.), cv Harosoy 63] seedlings were inoculated with zoospores from either race 1 (incompatible, host resistant) or race 3 (compatible, host susceptible) of Phytophthora megasperma f. sp. glycinea (Pmg) and the activities of phenylalanine ammonia-lyase (PAL), chalcone synthase (CHS), isoflavone synthase, and dihydroxypterocarpan 6a-hydroxylase related to phytoalexin (glyceollin) biosynthesis, and of glucose-6-phosphate dehydrogenase (Glc-6-PDH) and glutamate dehydrogenase (Glu-DH) were determined at various times after inoculation. About 2-4 h after inoculation with race 1, the activities of PAL, CHS, and pterocarpan 6a-hydroxylase were higher than after inoculation with race 3 and increased considerably thereafter. In contrast, activities of these enzymes in the compatible interaction were equal to or only slightly higher than in the controls over the entire infection period investigated (2-8 h). Isoflavone synthase did not increase until 7 h after inoculation with race 1. There were no significant differences in activities for Glc-6-PDH and Glu-DH between inoculated roots and controls. The results show that infection of soybean roots with zoospores of Pmg race 1 causes a race:cultivar-specific early induction of enzymes involved in glyceollin synthesis, whereas such an induction does not occur with zoospores of race 3. These findings are in agreement with the race:cultivar-specific accumulation of glyceollin in soybean roots reported previously [M. G. Hahn, A. Bonhoff, and H. Grisebach (1985) Plant Physiol. 77, 591-601].
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PMID:Race:cultivar-specific induction of enzymes related to phytoalexin biosynthesis in soybean roots following infection with Phytophthora megasperma f. sp. glycinea. 396 19

In porcine interareolar placental epithelia, the following enzymes were demonstrated by histochemical methods after 30, 58, 80, 100, and 110 d of pregnancy, respectively: beta-N-acetylhexosaminidase, beta-galactosidase, beta-glucuronidase, alpha-mannosidase, acid phosphatase, alkaline phosphatase, nonspecific esterases, cytochrome oxidase, 5-nucleotidase, leucine aminopeptidase, adenosine triphosphatase, diaphorases (NADH, NADPH), glucose-6-phosphate dehydrogenase, 6-phosphogluconate dehydrogenase, succinate dehydrogenase, isocitrate dehydrogenase (NAD, NADP), beta-hydroxybutyrate dehydrogenase, glycero-3-phosphate dehydrogenase, NAD-glycero-3-phosphate dehydrogenase, glutamate dehydrogenase (NAD, NADP), lactate dehydrogenase. The results show that most of the enzyme activities remained almost unchanged during the period of investigation. Only G-6-PDH and 6-PGDH activities increased within the uterine epithelium and nonspecific esterase activity within uterine as well as chorionic epithelia during the 2nd half of pregnancy. Within chorionic and uterine epithelia, hydrolases but not dehydrogenases demonstrated a higher activity at the bases of chorionic villi as compared to the apices and flanks of the latter. The action and influence of the demonstrated enzymes on metabolism, energy transfer, secretory, and resorptive activities of chorionic and uterine epithelia are discussed.
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PMID:[Enzyme histochemical studies of the swine placenta. Histoptics of enzymes in interareolar placental epithelia]. 643 35

1. All enzymes tested: malate dehydrogenase (MDH), glutamate dehydrogenase (GDH), glucose-6-phosphate dehydrogenase (G-6-PDH), and 6-phosphogluconate dehydrogenase (6-P-GDH)_behaved rhythmically during a period of continuous white light interrupted by darkness. All showed approximately the same frequency of 12-15 h. 2. The enzymes of the tricarboxylic-acid cycle (MDH and GDH) are in phase with each other but are out of phase with those of the oxidative pentose-phosphate pathway (G-6-PDH and 6-P-GDH) which are in turn in phase with each other. 3. GDH appears to be activated by the addition of Hoagland's solution which leads to an overt rhythm 24 h prior to darkness. The rhythms of MDH, G-6-PDH and 6-P-GDH cannot be demonstrated prior to the onset of darkness due to an inhibition of the MDH and pentose-phosphate cycle enzymes by light. 4. The control of the frequency and phase of these rhythms are discussed in relation to a positive correlation of the rhythms in enzyme activity presented here and the rhythms of the pyridine nucleotides presented elsewhere.
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PMID:Endogenous rhythmicity and energy transduction : IV. Rhythmic control of enzymes involved in the tricarboxylic-acid cycle and the oxidative pentose-phosphate pathway in Chenopodium rubrum L. 2445 97