Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: 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)

In the period of March 1988-March 1989, in 20 Lower Austrian sheep breeding farms blood samples were taken in two-month intervals from sheep of the following breeds: 130 Tyrolean Mountain sheep, 59 German Improved Land breed, 59 East Friesian and 57 German Blackheaded Mutton breed sheep. The following standards for sheep were evaluated: Erythrocytes 7,2-11,9 T/L, haematocrit 0,25-0,41 1/L, haemoglobin 82-147 g/L, lymphocytes 34-80%, segmented neutrophils 10-53%, band neutrophils 1-3%, eosinophilic granulocytes 0-24%, basophilic granulocytes 0-1%, monocytes 0-1%, calcium 1,8-2,8 mmol/L, phosphorus 1,0-2,6 mmol/L, magnesium 0,6-1,3 mmol/L, total protein 53-81 g/L, albumin 22-41 g/L, aspartate aminotransferase 27-81 U/L, alanine aminotransferase 3-25 U/L, gamma glutamic transaminase 24-59 U/L, alkaline phosphatase 44-355 U/L, creatine kinase 3-130 U/L, glutamic dehydrogenase 2,0-36,5 U/L, total bilirubin 0,7-5,1 mumol/L, cholesterol 1,1-3,2 mmol/l, urea nitrogen 1,3-12,7 mmol/l, creatinine 50-112 mumol/L. Apart from that, additional standards for the mentioned breeds of sheep were evaluated, revealing significant differences. Also the age and the time of the year proved to have an influence upon the ascertained blood values.
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PMID:[The hematologic parameters, concentrations of minerals and metabolic products and activities of enzymes in sheep]. 847 Oct 13

In Saccharomyces cerevisiae, carbon and nitrogen metabolisms are connected via the incorporation of ammonia into glutamate; this reaction is catalyzed by the NADP-dependent glutamate dehydrogenase (NADP-GDH) encoded by the GDH1 gene. In this report, we show that the GDH1 gene requires the CCAAT box-binding activator (HAP complex) for optimal expression. This conclusion is based on several lines of evidence: (1) overexpression of GDH1 can correct the growth defect of hap2 and hap3 mutants on ammonium sulfate as a nitrogen source, (ii) Northern (RNA) blot analysis shows that the steady-state level of GDH1 mRNA is strongly lowered in a hap2 mutant, (iii) expression of a GDH1-lacZ fusion is drastically reduced in hap mutants, (iv) NADP-GDH activity is several times lower in the hap mutants compared with that in the isogenic wild-type strain, and finally, (v) site-directed mutagenesis of two consensual HAP binding sites in the GDH1 promoter strongly reduces expression of GDH1 and makes it HAP independent. Expression of GDH1 is also regulated by the carbon source, i.e., expression is higher on lactate than on ethanol, glycerol, or galactose, with the lowest expression being found on glucose. Finally, we show that a hap2 mutation does not affect expression of other genes involved in nitrogen metabolism (GDH2, GLN1, and GLN3 encoding, respectively, the NAD-GDH, glutamine synthetase, and a general activator of several nitrogen catabolic genes). The HAP complex is known to regulate expression of several genes involved in carbon metabolism; its role in the control of GDH1 gene expression, therefore, provides evidence for a cross-pathway regulation between carbon and nitrogen metabolisms.
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PMID:The CCAAT box-binding factor stimulates ammonium assimilation in Saccharomyces cerevisiae, defining a new cross-pathway regulation between nitrogen and carbon metabolisms. 860 56

A new assay procedure for the measurement of ketoglutarate concentrations is described which is based on substrate-induced quenching (SIQ) of a fluorophore. The method makes use of the photoreaction between a fluorophore (thionine) and NADH. The latter is consumed during an enzymatic reaction between ketoglutarate and L-glutamic dehydrogenase. The conversion yield of cofactor from its reduced form to oxidized forms represented as an overall change in the population of the excited state population of the fluorophore thionine. An empirical relation is described that correlates initial substrate concentration to the observed yield of the cofactor conversion via a fluorescence recovery constant,Kt. The analysis of data obtained over a range of 0-500 microM results in a constant of 2748 M-1. The applicability of the proposed method is demonstrated by performing the assay for alpha-ketoglutarate in human urine. The ketoglutarate SIQ assay was not affected by the background interference that is inherent to this complex matrix.
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PMID:alpha-Ketoglutarate assay based on fluorescence quenching by NADH. 865 26

Glutamate, the major excitatory neurotransmitter, is preferentially catabolized in astrocytes by glutamate dehydrogenase (GDH). Treatment of an astrocytic cell line with hydrocortisone (10(-5) M) resulted in increased expression of GDH mRNA. Transfection of the cells with truncated parts of the GDH promoter showed that genomic responsive elements activated by hydrocortisone are localized in the -557/+1 region of the promoter. This control of GDH expression by glucocorticoids may be involved in their protective effect against glutamate excitotoxicity.
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PMID:Glucocorticoid upregulation of glutamate dehydrogenase gene expression in vitro in astrocytes. 873 68

Blood parameters, feed intake and milk yield were determined in 53 cows with a left displacement of the abomasum (LDA) on the day of surgery (ds; laparotomy and omentopexy) and during the following four days (d1-d4). Using histological methods severe (group SF), moderate (group MF) or no/mild (group NF) fatty liver was found in 32%, 40% and 28% of the patients, respectively. Moderate and severe fatty liver were found almost exclusively in cows in the first three weeks post partum. Post surgery, feed intake and daily milk yield increased steadily in cows of the NF- and MF-group; in cows suffering from severe fatty liver feed intake remained low (p < 0.05). On ds, mean serum levels of nonesterified fatty acids (NEFA), beta-hydroxybutyrate (BHB), total bilirubin, aspartate aminotransferase (ASAT), gammaglutamyl transpeptidase (GGT) and glutamic dehydrogenase (GLDH) in SF-cows were significantly (p < 0.05) higher and values of cholesterol significantly lower (p < 0.05) as compared to the NF- and MF-group; no significant differences were found between the groups in mean serum glucose concentrations. In the four day period following surgery, in all groups mean serum levels of ASAT, GGT, GLDH and cholesterol remained nearly unchanged, whereas total bilirubin, NEFA, BHB and glucose decreased significantly (p < 0.05). Apart from LDA, 55% of the patients were suffering from mastitis, endometritis or lameness. Within three weeks post surgery, 3 cows of the SF-group and 1 cow of the MF-group developed recumbency and liver coma, and were culled for that reason. In conclusion, post surgical convalescence of cows with LDA is clearly related to disturbances of energy metabolism and fatty liver. Therefore, successful treatment of cows suffering from LDA requires the effective treatment of excessive lipomobilization, ketosis and fatty liver along with the immediate surgical correction of LDA.
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PMID:Post surgical convalescence of dairy cows with left abomasal displacement in relation to fatty liver. 876 92

We studied the level(s) at which glutamate dehydrogenase (GDH; EC 1.4.1.2) expression is regulated in the livers of fed male and female rats. The cellular content of GDH mRNA, protein, and enzyme activity was determined quantitatively using image analysis for measurement of the absorbance in consecutive serial sections that were processed for in situ hybridization, immunohistochemistry, and enzyme histochemistry. In both males and females, GDH protein and activity patterns were similar, with pericentral values being twice as high as periportal values. GDH mRNA distribution patterns in female liver lobules reflected those of GDH protein and activity, but GDH mRNA distribution patterns in male rat livers were found to be homogeneous owing to a more than twofold lower cellular mRNA content in pericentral zones than in female rats. We conclude that gender affects GDH expression selectively in pericentral zones at posttranscriptional and pretranslational levels.
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PMID:Gender-dependent regulation of glutamate dehydrogenase expression in periportal and pericentral zones of rat liver lobules. 881 80

The degeneration of serotonergic neurons increases the expression of glutamate dehydrogenase (GDH) in hippocampal astrocytes. This process was demonstrated to be independent of the serotonin level. At the same time, upregulation of tumor necrosis factor (TNF) alpha and interleukin (IL)-1 alpha mRNA were observed, whereas levels of transforming growth factor (TGF) beta 1 mRNA remained unchanged. The level of GDH mRNA was increased in primary cultures of hippocampal astrocytes treated with TNF alpha and IL-1 alpha suggesting that these cytokines act on the GDH metabolism. TNF alpha and IL-1 alpha induced an increase in GDH promoter activity in C8S (an astrocytic cell line) transfected with constructs containing 5' flanking genomic sequences of GDH driving the expression of a reporter gene. These observations suggest that cytokines may be signals that upregulate the astrocytic GDH expression in response to the degeneration of serotonergic terminals in the hippocampus.
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PMID:Cytokines are increased in the rat hippocampus after serotonergic neuron degeneration and upregulate the expression of GDH, an enzyme involved in glutamate detoxification. 882 82

The main pathway for the hepatic oxidation of ethanol to acetaldehyde proceeds via ADH and is associated with the reduction of NAD to NADH; the latter produces a striking redox change with various associated metabolic disorders. NADH also inhibits xanthine dehydrogenase activity, resulting in a shift of purine oxidation to xanthine oxidase, thereby promoting the generation of oxygen-free radical species. NADH also supports microsomal oxidations, including that of ethanol, in part via transhydrogenation to NADPH. In addition to the classic alcohol dehydrogenase pathway, ethanol can also be reduced by an accessory but inducible microsomal ethanoloxidizing system. This induction is associated with proliferation of the endoplasmic reticulum, both in experimental animals and in humans, and is accompanied by increased oxidation of NADPH with resulting H2O2 generation. There is also a concomitant 4- to 10-fold induction of cytochrome P4502E1 (2E1) both in rats and in humans, with hepatic perivenular preponderance. This 2E1 induction contributes to the well-known lipid peroxidation associated with alcoholic liver injury, as demonstrated by increased rates of superoxide radical production and lipid peroxidation correlating with the amount of 2E1 in liver microsomal preparations and the inhibition of lipid peroxidation in liver microsomes by antibodies against 2E1 in control and ethanol-fed rats. Indeed, 2E1 is rather "leaky" and its operation results in a significant release of free radicals. In addition, induction of this microsomal system results in enhanced acetaldehyde production, which in turn impairs defense systems against oxidative stress. For instance, it decreases GSH by various mechanisms, including binding to cysteine or by provoking its leakage out of the mitochondria and of the cell. Hepatic GSH depletion after chronic alcohol consumption was shown both in experimental animals and in humans. Alcohol-induced increased GSH turnover was demonstrated indirectly by a rise in alpha-amino-n-butyric acid in rats and baboons and in volunteers given alcohol. The ultimate precursor of cysteine (one of the three amino acids of GSH) is methionine. Methionine, however, must be first activated to S-adenosylmethionine by an enzyme which is depressed by alcoholic liver disease. This block can be bypassed by SAMe administration which restores hepatic SAMe levels and attenuates parameters of ethanol-induced liver injury significantly such as the increase in circulating transaminases, mitochondrial lesions, and leakage of mitochondrial enzymes (e.g., glutamic dehydrogenase) into the bloodstream. SAMe also contributes to the methylation of phosphatidylethanolamine to phosphatidylcholine. The methyltransferase involved is strikingly depressed by alcohol consumption, but this can be corrected, and hepatic phosphatidylcholine levels restored, by the administration of a mixture of polyunsaturated phospholipids (polyenylphosphatidylcholine). In addition, PPC provided total protection against alcohol-induced septal fibrosis and cirrhosis in the baboon and it abolished an associated twofold rise in hepatic F2-isoprostanes, a product of lipid peroxidation. A similar effect was observed in rats given CCl4. Thus, PPC prevented CCl4- and alcohol-induced lipid peroxidation in rats and baboons, respectively, while it attenuated the associated liver injury. Similar studies are ongoing in humans.
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PMID:Role of oxidative stress and antioxidant therapy in alcoholic and nonalcoholic liver diseases. 889 26

Two cathepsin L proteinases, cathepsin L1 and cathepsin L2, secreted by liver flukes may be involved in tissue penetration, nutrition, and protection from immune attack. To ascertain the immunoprophylactic potential of these proteinases, and of another molecule, liver fluke hemoglobin (Hb), we performed vaccine trials in cattle. In the first vaccine trial various doses of cathepsin L1 were tested. The mean protection level obtained was 53.7%. In a second vaccine trial cathepsin L1 and Hb elicited 42.5 and 43.8% protection levels, respectively, while a combination of the two molecules induced a significantly higher level of protection (51.9%). Cathepsin L2 was not examined alone; however, vaccination of cattle with a combination of cathepsin L2 and Hb elicited the highest level of protection (72.4%). The animals that received cathepsin L1-Hb or cathepsin L2-Hb showed reduced liver damage as assessed by serum glutamic dehydrogenase and gamma-glutamyl transferase levels. Furthermore, a reduced viability was observed for fluke eggs recovered from all vaccine groups. This anti-embryonation effect of vaccination was particularly evident in the group that received cathepsin L2-Hb where >98% of the eggs recovered did not embryonate to miracidia. Although all vaccine preparations induced high antibody titers which were boosted following the challenge infection, there was no correlation between antibody titers and protection. The results of these trials demonstrate that cathepsin Ls and Hb could form the basis of a molecular vaccine that would not only reduce parasite burden but would also prevent transmission of liver fluke disease.
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PMID:Induction of protective immunity in cattle against infection with Fasciola hepatica by vaccination with cathepsin L proteinases and with hemoglobin. 894 48

Two distinct cDNA clones encoding NAD(H)-dependent glutamate dehydrogenase (NAD[H]-GDH) in Arabidopsis thaliana were identified and sequenced. The genes corresponding to these cDNA clones were designated GDH1 and GDH2. Analysis of the deduced amino acid sequences suggest that both gene products contain putative mitochondrial transit polypeptides and NAD(H)- and alpha-ketoglutarate-binding domains. Subcellular fractionation confirmed the mitochondrial location of the NAD(H)-GDH isoenzymes. In addition, a putative EF-hand loop, shown to be associated with Ca2+ binding, was identified in the GDH2 gene product but not in the GDH1 gene product. GDH1 encodes a 43.0-kD polypeptide, designated alpha, and GDH2 encodes a 42.5-kD polypeptide, designated beta. The two subunits combine in different ratios to form seven NAD(H)-GDH isoenzymes. The slowest-migrating isoenzyme in a native gel, GDH1, is a homohexamer composed of alpha subunits, and the fastest-migrating isoenzyme, GDH7, is a homohexamer composed of beta subunits. GDH isoenzymes 2 through 6 are heterohexamers composed of different ratios of alpha and beta subunits. NAD(H)-GDH isoenzyme patterns varied among different plant organs and in leaves of plants irrigated with different nitrogen sources or subjected to darkness for 4 d. Conversely, there were little or no measurable changes in isoenzyme patterns in roots of plants treated with different nitrogen sources. In most instances, changes in isoenzyme patterns were correlated with relative differences in the level of alpha and beta subunits. Likewise, the relative difference in the level of alpha or beta subunits was correlated with changes in the level of GDH1 or GDH2 transcript detected in each sample, suggesting that NAD(H)-GDH activity is controlled at least in part at the transcriptional level.
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PMID:Characterization and expression of NAD(H)-dependent glutamate dehydrogenase genes in Arabidopsis. 911 79


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