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)

Triiodothyronine added at 0.1 nM to 3T3-F442A cells cultured in adipogenic medium having endogenous hormone concentrations similar to those of hypothyroid serum stimulated adipose conversion; activities of both lipogenic enzymes, glycerophosphate dehydrogenase and malic enzyme, increased with hormone treatment. The number of adipocytes was also augmented by L-T3 addition but the number of fat cell clusters remained the same as compared to non-treated cultures, suggesting that thyroid hormone increased the number of adipocytes probably through stimulating selective multiplication of precursor adipose cells. Hormone addition to cells cultured with non-adipogenic medium did not promote conversion showing that L-T3 is not an adipogenic factor by itself. Triiodothyronine added at concentrations similar to those found in hyperthyroidism, from 10 nM up to 10 microM, also increased the proportion of adipocytes without changing the number of fat cell clusters, but they decreased the activity of both lipogenic enzymes and lipid accumulation in mature adipocytes. It can be concluded that during 3T3-F442A differentiation into adipocytes L-T3 increases the number of differentiated adipocytes and, at low concentrations, also enhances lipogenic enzyme activities, whereas at the hyperthyroid hormone levels these enzyme activities are significantly reduced, remaining at levels similar to those of cells cultured with hypothyroid medium. This cloned cell line seems to be a useful model to study thyroid hormone action at both molecular and cellular level.
Mol Cell Biochem 1987 Jul
PMID:Thyroid hormone stimulates adipocyte differentiation of 3T3 cells. 362 13

The glycosomes of in vitro grown procyclic trypomastigote forms of Trypanosoma brucei were purified by three different procedures and the results compared by electron microscopy, enzyme assays and sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Centrifugation on a self-forming Percoll gradient followed by a sucrose gradient centrifugation resulted in the least enriched glycosomal preparation. Centrifugation on a pre-formed Nycodenz gradient gave an improved preparation but the most homogeneous preparation of intact glycosomes was obtained after centrifugation on two successive sucrose gradients. Glycosomes purified by both the Nycodenz and double sucrose gradient procedures appeared larger than in situ glycosomes presumably due to an osmotic effect resulting from disruption of the granular matrix of the organelles. Nevertheless, there appears to be no loss of cisternal contents due to the swelling of the organelles. The glycosomes of the bloodstream form trypomastigotes purified by the same procedures show, however, no sign of swelling. A comparison of glycosomes purified from procyclic trypomastigotes and bloodstream form trypomastigotes prepared by the same double sucrose procedure demonstrated that in the glycosome of procyclic trypomastigotes: activities of hexokinase, phosphoglucose isomerase, phosphofructose kinase, aldolase and phosphoglycerate kinase and diminished by 80-100%; activities of glyceraldehyde-3-phosphate dehydrogenase, triose phosphate isomerase and glycerol-3-phosphate dehydrogenase remain unchanged or are only slightly reduced; there is an appearance of four major new proteins, among which could be phosphoenol pyruvate carboxykinase and malate dehydrogenase. These observations are in basic agreement with those by Hart et al. (Mol. Biochem. Parasitol. 12, 25-35, 1984).
Mol Biochem Parasitol 1986 Dec
PMID:An improved purification of glycosomes from the procyclic trypomastigotes of Trypanosoma brucei. 380 43

After a single intravenous injection of suramin the rate of removal of the drug from the plasma into other tissue compartments of the rat is independent of initial concentration. The data can be fitted to the sum of two exponential functions, consistent with a two-compartment, open model system. Trypanosomes take up only small amounts of suramin in vivo and do not actively concentrate the drug within the cell. Uptake is apparently by a non-saturable process that decreases with time and is dependent on the amount of suramin already taken up. Once within the cell, suramin progressively inhibits respiration and glycolysis, such that, for a given exposure in vivo, inhibition of oxygen consumption is proportional to the total amount of suramin absorbed. It can be calculated that only a fraction (4--9%) of this total is required to inhibit respiration to the extent found in broken cell preparations. The combined inhibition of two key enzymes in glycolysis--the sn-glycerol-3-phosphate oxidase (EC unassigned) and the glycerol-3-phosphate dehydrogenase (NAD+) (sn-glycerol-3-phosphate: NAD+ 2-oxidoreductase, EC 1.1.1.8)--are sufficient to account for the differential inhibition of glucose and oxygen consumption and of pyruvate production, together with the small, but significant, production of glycerol. Even at the highest dose of suramin tolerated by the rat, trypanosomes continue to increase exponentially in the bloodstream for at least 6 h. The mean doubling time is increased from 4.6 h to a maximum of about 12.5 h in rats treated with doses of suramin in the range 25--150 mg/kg. In the light of these and other findings, it is concluded that part of the trypanocidal action of suramin results from the inhibition of ATP production by glycolysis.
Mol Biochem Parasitol 1980 Oct
PMID:Uptake of the trypanocidal drug suramin by bloodstream forms of Trypanosoma brucei and its effect on respiration and growth rate in vivo. 610 10

Enzyme induction by hydrocortisone (HC) and dibutyryl cyclic AMP (dbcAMP) was studied in C6 rat glioma cells, FU5AH rat hepatoma cells, and five C6 x FU5AH hybrids. Hormone responsive enzymes from both parental lines were studied, including: tyrosine aminotransferase (TAT), alanine aminotransferase (AAT), glycerol phosphate dehydrogenase (GPDH), lactate dehydrogenase (LDH), and 2',3'-cyclic nucleotide 3'-phosphohydrolase (CNP). There was no overall dominance of one parental phenotype over the other in expression of uninduced or induced enzyme activity after fusion, and the hybrids possessed some enzymatic properties characteristic of both parents. GPDH was induced by dbcAMP in all five hybrids, and TAT was induced by dbcAMP in four of the hybrids, although neither of these enzymes were induced by dbcAMP in the parents. Furthermore, synergistic induction of these enzymes by HC and dbcAMP was observed in the hybrids but not in the parents. These hybrids provide a model system to study hormone interaction in enzyme induction.
Somat Cell Mol Genet 1984 Mar
PMID:Synergistic enzyme induction by glucocorticoids and cyclic AMP observed in glioma x hepatoma cell hybrids but not in their parents. 614 8

Seven mutant strains defective for utilization of glycerol, glyceraldehyde or dihydroxyacetone were isolated. One strain was deficient for NAD-linked glycerol-3-phosphate dehydrogenase, two for glycerol kinase, and four had no detected enzymatic deficiency, although one of the latter strains was deficient in glycerol uptake. Glycerol uptake was increased by incubation in glycerol, glycerol-3-phosphate, erythritol, and propanediol, and was protein-mediated below 0.14 mM glycerol, but at higher concentrations free diffusion predominated. Glycerol uptake was decreased by cycloheximide and was more sensitive to sodium azide than to iodoacetate.
Mol Gen Genet 1983
PMID:Uptake and dissimilation of glycerol by wild type and glycerol nonutilizing strains of Neurospora crassa. 622 38

Glycerol-3-phosphate dehydrogenase (gylB) mutations (which cause glycerol sensitivity), and presumed glycerol kinase (gylA) and/or regulatory mutations eliminating both glycerol-3-phosphate dehydrogenase and glycerol kinase activities, map close to the argA locus of Streptomyces coelicolor A3(2). Using the plasmid vector pIJ702 and restriction enzymes BglII and SstI, extensively overlapping S. coelicolor DNA fragments of 2.74 kb and 2.84 kb were isolated, either of which could restore the wild-type phenotype to gylB and some gylA mutants. Genetic and biochemical analyses of mutants carrying the cloned gyl DNA suggested that a functional gyl promoter had not been cloned, and that restoration of the Gyl+ phenotype was achieved by recombination between the cloned and chromosomal gyl DNA sequences. After subcloning parts of this DNA into the phage vector phi C31 KC400, "gene disruption" analysis was carried out, which confirmed the absence of the gyl promoter, and indicated that a polycistronic mRNA traverses gylA and then gylB.
Mol Gen Genet 1984
PMID:The glycerol utilization operon of Streptomyces coelicolor: genetic mapping of gyl mutations and the analysis of cloned gylDNA. 631 46

Evidence is presented for the occurrence of glycosomes (organelles resembling peroxisomes) in four major species of Leishmania (viz. L. major, L.m. mexicana, L. b. braziliensis and L. donovani), based on latency as well as differential and isopycnic centrifugation studies. The enzymes involved in glycolysis; (hexokinase, phosphoglucose isomerase, phosphofructokinase, fructose-1,6-bisphosphate aldolase, triosephosphate isomerase, glyceraldehyde-phosphate dehydrogenase and phosphoglycerate kinase); glycerol metabolism (sn-glycerol-3-phosphate dehydrogenase and glycerol kinase); carbon dioxide fixation (phosphoenolpyruvate carboxykinase and possibly malate dehydrogenase); together with an enzyme involved in the beta-oxidation of fatty acids (3-beta-hydroxybutyryl coenzyme A dehydrogenase); a key enzyme in the synthesis of ether lipids (dihydroxyacetone phosphate acyltransferase) as well as the ADP utilising enzyme adenylate kinase, were all found associated, at least in part, with a subcellular organelle which had a buoyant density in sucrose gradients of 1.21 to 1.24 g cm-3. Little variance in enzyme composition was found between the different species of Leishmania or in comparison with other members of the Trypanosomatidae, supporting the unifying principle that glycosomes are a unique characteristic of this family. The occurrence of important catabolic, anabolic and anaplerotic pathways in the glycosomes of Leishmania renders them prime targets for chemotherapy.
Mol Biochem Parasitol 1984 Oct
PMID:The occurrence of glycosomes (microbodies) in the promastigote stage of four major Leishmania species. 644 18

We compared subcellular activities in brain and liver at various times after thyroidectomy. Male S.D. rats were used on days 5, 10 or 60 after surgery. Mitochondrial properties were estimated by determining the respective activities of oxidative phosphorylation, succinate oxidase, succinate and beta-hydroxybutyrate cytochrome c reductase and alpha-glycerophosphate dehydrogenase. Nuclear activity was estimated by measuring the RNA polymerase I activity. In brain, RNA polymerase I activity already declined at 5 days after thyroidectomy, whereas mitochondrial respiratory enzymes decreased significantly only after 60 days. In liver, nuclear RNA polymerase I and mitochondrial enzyme activities were observed to drop simultaneously by the 5th day after thyroid removal. On the other hand, daily T3 s.c. injections, 0.25 microgram/100 g B.W., were given for 10 days to rats immediately after thyroidectomy (10 days Tx) or to chronically hypothyroid rats (60 days Hth). Hormonal treatment either maintained or restored subcellular activities to their normal level, both in brain and liver. These data suggest that the metabolic properties of brain mitochondria are sensitive to thyroid hormones, but that the brain needs less iodothyronines than other organs. The fast reduction of RNA polymerase I by thyroidectomy and its subsequent restoration by T3 suggest that the nuclear activity greatly depends on thyroid status.
Mol Cell Endocrinol 1983 Dec
PMID:Effects of short- and long-term thyroidectomy on mitochondrial and nuclear activity in adult rat brain. 665 72

It is shown that the Notch8 deficiency in Drosophila melanogaster affects a number of enzyme activities localized in the mitochondria, such as NADH oxidase (activity of the complete respiratory chain), NADH dehydrogenase (the first step in the respiratory chain before transfer to ubiquinone), Succinate dehydrogenase and alpha-glycerophosphate dehydrogenase. The experiments reported here do not exclude the possibility of involvement of other genes in the deficiency. The effect of duplications of the Notch locus on NADH oxidase and NADH dehydrogenase suggest that the locus determines the enzyme activities. The dosage effects of the Notch locus on activity suggest that this locus contains the structural genes for these enzymes.
Mol Gen Genet 1981
PMID:The action of the notch locus in Drosophila melanogaster. I. Effects of the notch8 deficiency on mitochondrial enzymes. 679 Sep 11

Procyclic culture forms of Trypanosoma brucei stock 427 have been screened for the presence of enzymes involved in glycolysis, mitochondrial energy metabolism and threonine degradation. The enzyme activities in the procyclics were compared with those of the blood stream forms. The specific activities of glycolytic enzymes represented 30-70% of the respective levels in the blood stream form, except for hexokinase which was 25-fold reduced. Cell fractionation showed that the enzymes involved in the early sequence of the glycolytic pathway, i.e. from hexokinase to phosphoglycerate kinase, and the enzymes NAD+-linked glycerol-3-phosphate dehydrogenase and glycerol kinase were all present in glycosomes equilibrating at a density of 1.23 g/cm3 in sucrose gradients. Malate dehydrogenase was 8-fold more active in procyclics than in bloodstream forms. This increase in activity was the result of the appearance of malate dehydrogenase in the glycosomes of the procyclics, in addition to mitochondrial and cell-sap activities which were present in both stages of the life cycle. Glycosomes contained part of the adenylate kinase activity, which was also associated with the mitochondrion. Succinate dehydrogenase and sn-glycerol-3-phosphate dehydrogenase, together with oligomycin-sensitive ATPase, were located in the mitochondrion which had a density in sucrose ranging from 1.16 to 1.18 g/cm3. This organelle also contained L-threonine 3-dehydrogenase and carnitine acetyltransferase, two enzymes involved in threonine catabolism. The latter two enzymes had activities which were, respectively, 15-and 13-fold higher in the procyclics than in the bloodstream form. Mitochondrial sn-glycerol-3-phosphate dehydrogenase was decreased 4-fold.
Mol Biochem Parasitol 1981 Dec 31
PMID:Localization of malate dehydrogenase, adenylate kinase and glycolytic enzymes in glycosomes and the threonine pathway in the mitochondrion of cultured procyclic trypomastigotes of Trypanosoma brucei. 680 9


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