Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P06889 (Mol)
 630,302 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The effects of castration and hormone administration on the activity of glucose-6-phosphate dehydrogenase in the rat levator ani muscle were studied. Castration caused a decrease in enzyme activity and in wet weight of the levator ani muscle. Chronic administration of testosterone propionate increased glucose-6-phosphate dehydrogenase activity in the levator ani muscle of castrated rats; the magnitude of the recovery of enzyme activity was related to the length of time of exposure to testosterone propionate after castration as well as to the length of time the animals were castrated. The longer the period of castration before exposure to testosterone propionate, the greater the effect. This result may be related to previously reported castration-mediated increases in androgen receptor binding in muscle. Dihydrotestosterone was less effective than testosterone propionate in enhancing glucose-6-phosphate dehydrogenase activity in the levator ani muscle from castrated rats; estradiol-17 beta alone was ineffective. Combined treatment with estradiol-17 beta and dihydrotestosterone, however, was as effective as testosterone alone. Thus, androgens and estrogens may exert synergistic effects on levator ani muscle.
Mol Cell Endocrinol 1984 Dec
PMID:Androgen-estrogen synergy in rat levator ani muscle: glucose-6-phosphate dehydrogenase. 651 May 48

We have used a cloned cDNA for hypoxanthine-guanine phosphoribosyltransferase (HGPRT) to analyze the HGPRT gene and mRNA in an HGPRT-deficient mutant of Chinese hamster cells (RJK10) and its HGPRT-positive revertants. By Southern blot analysis, no DNA rearrangements were detected within the genes from any of the cell lines examined. However, four of five spontaneous revertants each contained 10- to 20-fold more copies of the HGPRT gene than did RJK10 or wild-type cells. In contrast, the gene was not amplified in four mutagen-induced revertants. The RJK10 mutation did not alter the size or concentration of HGPRT mRNA and representatives of the revertants contained the mRNA in amounts proportional to the number of genes they carried. Examples of clones with either stable or unstable gene amplification were identified and their HGPRT-positive phenotypes were shown to be dependent on the gene amplification. In a stably amplified revertant, the extra genes were found to be syntenic with the X chromosome marker glucose-6-phosphate dehydrogenase. In an unstable revertant only one of the 10 to 20 copies of the gene could be shown to be X linked. Thus, we found that RJK10 can revert by at least two distinct mechanisms: amplification of the HGPRT gene, which occurred spontaneously, or point mutation, which predominated after exposure to mutagens.
Somat Cell Mol Genet 1984 Jan
PMID:Amplification versus mutation as a mechanism for reversion of an HGPRT mutation. 658 54

Exposure of single Chinese hamster ovary (CHO) cells to the mutagen, ethyl methane sulfonate, produces two types of mutant colonies lacking glucose-6-phosphate dehydrogenase activity: colonies uniformly deficient in enzyme activity, and mosaic colonies containing both mutant and nonmutant cell phenotypes in various relative proportions and sectored patterns (1/8, 1/4, 1/2). We find that the relative size of the mutant sector in these mosaic colonies primarily reflects the cell division at which the mutation was genetically fixed. Thus, the mutation-fixation event occurs before the first cell division in 1/2 sector and pure mutant colonies, between the first and second divisions for 1/4 sectors, and between the second and third divisions for 1/8 sectors. Delay in the formation of mutations could also explain the phenomenon of "mutation expression time" which is observed when drug resistance is used to select for mutants. Colony sectoring offers for the first time in mammalian cells the opportunity to observe an agent's effect on the timing of the mutational process.
Somat Cell Mol Genet 1984 Jul
PMID:Timing of mutation-fixation events in ethyl methane sulfonate-treated Chinese hamster cells. 658 95

By means of metaphase chromosomes, the genes for mink thymidine kinase (TK) and hypoxanthine-phosphoribosyltransferase (HPRT) were transferred to mutant mouse cells, LMTK-, A9 (HPRT-) and teratocarcinoma cells, PCC4-aza 1 (HPRT-). Eighteen colonies were isolated from LMTK- (series A), 9 from A9 (series B) and none from PCC4-aza 1. The transformed clones contained mink TK or HPRT. Analysis of syntenic markers in series B demonstrated that one clone contained mink glucose-6-phosphate dehydrogenase (G6PD) and the other alpha-galactosidase; in series A, nine clones contained mink galactokinase (GALK) and six mink aldolase C (ALDC). Analysis of 12 asyntenic markers located in ten mink chromosomes showed the presence of only aconitase-1 (ACON1) (the marker of mink chromosome 12) in three clones of series A. The clones lost mink ACON1 between the fifth to tenth passages. Cytogenetic analysis established the presence of a fragment of mink chromosome 8 in eight clones of series A, but not in series B. The clones of series A lost mink TK together with mink GALK and ALDC during back-selection; in B, back-selection retained mink G6PD. No stable TK+ phenotype was detected in clones with a visible fragment of mink chromosome 8. Stability analysis demonstrated that about half of the clones of series B have stable HPRT+ phenotype whereas only three clones of series A have stable TK+ phenotype. It is suggested that the recipient cells, LMTK- and A9, differ in their competence for genetic transformation and integration of foreign genes.
Mol Gen Genet 1984
PMID:Cotransfer and phenotypic stabilisation of syntenic and asyntenic mink genes into mouse cells by chromosome-mediated gene transfer. 659 20

To provide for bioluminescence measurements of the enzymatic activities of dehydrogenases, disturbing contaminants were removed from a bacterial luciferase extract by chromatography, using Blue Sepharose CL-6B, a cross-linked agarose to which Cibacrone Blue F3G-A is covalently attached. This compound has a strong affinity to the dinucleotide fold, which is a region in enzymes binding NAD(H) or NADP(H). In contrast to the absorbed dehydrogenases, both luciferase and oxidoreductase were easily eluted and appeared close to the main bulk of UV-absorbing but analytically less important material. A rapid recording of the elution of luciferase was accomplished with a new electrochemical bioluminescence assay. Due to this and the early elution of the desired material, it could be chromatographed, recognized and collected in less than two hours. Thereby the light-yielding capacity of the sensitive material was well preserved. For bioluminescence assay solutions composed of pooled oxidoreductase-luciferase fractions, FMN and a long chain aldehyde were prepared and supplemented with NAD+ and either lactate, malate or 3-hydroxybutyrate. The analyses were carried out in a single step performance by adding the enzyme sample to the luciferase solution. Minute amounts of lactate dehydrogenase, malate dehydrogenase and 3-hydroxybutyrate dehydrogenase yielded a linear light response permitting assay in the lower part of the femtomole region. In case a dehydrogenase does not occur as a contaminant of a commercial luciferase preparation, purification with Cibacrone Blue can be omitted as demonstrated for glucose-6-phosphate dehydrogenase.(ABSTRACT TRUNCATED AT 250 WORDS)
Mol Cell Biochem 1983
PMID:Single-step bioluminescence analyses of enzymes, using Cibacrone Blue chromatography for removal of interfering dehydrogenases. 663 14

The ability to carry out the initial reaction of the pentose phosphate pathway was investigated with extracts of mouse erythrocytes infected with Plasmodium chabaudi, purified merozoites of P. knowlesi, and schizonts of P. falciparum grown in vitro in human erythrocytes. Glucose-6-phosphate dehydrogenase activity (G-6pd) was detected in extracts of all the cells after electrophoresis on polyacrylamide gels. Separate host cell and parasite glucose-6-phosphate dehydrogenase activities were demonstrated with extracts of P. knowlesi and P. falciparum but not with P. chabaudi.
Mol Biochem Parasitol 1981 Feb
PMID:Detection of glucose-6-phosphate dehydrogenase in malarial parasites. 701 16

A glucose-negative mutant of Saccharomyces cerevisiae lacking 6-phosphogluconate dehydrogenase, the second enzyme of the pentose phosphate pathway, has been obtained by inositol starvation. Suppression of this mutant for growth on glucose takes place by the loss of glucose 6-phosphate dehydrogenase. A lesion in the latter enzyme alone leaves growth practically unaffected. The mutations define the respective structural genes.
Mol Gen Genet 1982
PMID:Pentose phosphate pathway mutants of yeast. 704 91

We studied the influence of sex hormones using the hormone-sensitive levator ani muscle as a model tissue and glucose-6-phosphate dehydrogenase as an indicator of hormone action. Injection of testosterone or estradiol cause a 50% increase in the specific activity of glucose-6-phosphate dehydrogenase. The effect was dose-dependent, and was maximal at a dose of 2.5mg/100g body weight. Estradiol increased glucose-6-phosphate dehydrogenase as early as 8 h after injection, while testosterone required 12 h. Injection of estradiol on 2 successive days increased enzyme activity by 80%. The effect of estradiol was abolished by actinomycin D, suggesting enzyme induction. The results indicate a direct effect of estrogen on striated muscle.
Mol Cell Endocrinol 1980 Feb
PMID:Effect of sex hormones on glucose-6-phosphate dehydrogenase in rat levator ani muscle. 736 48

Bioluminescence photokinetic assay of NADP+ is described, using the glucose-6-phosphate dehydrogenase reaction for conversion to its reduced form and subsequent measurement of this with luciferase extracts of Vibria fisherii. the analyses were applied to the determination of the activity of minute amounts of glutathione reductase using NADP+ as measurable product and for nucleotide assay in cell samples of 0.5--10 microgram dry weight. The sensitivity was sufficient for determining 0.5 picomoles NADP+. Previously, FMN, NADH, NAD+ and NADH have been analysed with the bacterial luciferase system. Its applicability has not been extended by the assay of NADP+.
Mol Cell Biochem 1980 Aug 29
PMID:Photokinetic microanalysis of NADP+, using bacterial luciferase. 744 56

We have cloned and characterized a homologue of the previously isolated GPD1 gene, encoding sn-glycerol 3-phosphate dehydrogenase (NAD+) in Saccharomyces cerevisiae. This second gene, called GPD2, encodes a protein of 384 amino acids that shares 69% sequence identity with GPD1. Like GPD1 it has an amino-terminal extension of unknown function. GPD2 is located on chromosome VII and cross-hybridizes with GPD1 at chromosome IV as well as with an unknown homologue at chromosome XV. Disruption of the GPD2 gene did not reveal any observable phenotypic effects, whereas overexpression resulted in a slight, but significant, increase of GPD enzyme activity in wild-type cells. Analysis of gene transcription by a CAT-reporter gene fused to the GPD promoters revealed decreased transcriptional activity of the GPD2 promoter in cells grown on nonfermentable as opposed to fermentable carbon sources, and no induction in cells exposed to high osmolarity or heat shock. Similar analysis of GPD1 demonstrated an 8-17-fold higher basal level of transcription compared to GPD2. Furthermore, such analysis revealed that the GPD1 promoter was induced by increased osmolarity essentially independent of the type of stress solute used, the level of GPD1 transcription being increased about sevenfold in cells growing at 1.4 M NaCl.
Mol Microbiol 1995 Jul
PMID:Cloning and characterization of GPD2, a second gene encoding sn-glycerol 3-phosphate dehydrogenase (NAD+) in Saccharomyces cerevisiae, and its comparison with GPD1. 747 12


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