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:1.2.1.13 (glyceraldehyde-3-phosphate dehydrogenase)
6,511 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The purpose of this study was to develop a method by which endothelial cell nitric oxide synthase (ecNOS) mRNA expression could be measured in single coronary resistance arteries and to test the hypothesis that ecNOS gene expression is upregulated by exercise training. Yucatan miniature swine were randomly assigned to exercise-trained (ET; n = 5) or sedentary (Sed; n = 4) groups for 16 wk. Individual coronary resistance arteries (50-100 microns) were dissected, frozen in liquid nitrogen, and homogenized in a LiCl buffer, mRNA was isolated from each vessel, and ecNOS gene expression was assessed using reverse transcriptase (RT)-polymerase chain reaction (PCR) standardized by coamplifying ecNOS with glyceraldehyde 3-phosphate dehydrogenase (GAPHD). The ecNOS-to-GAPDH amplicon ratio was significantly greater in coronary resistance arteries isolated from ET pigs than in Sed controls. On the basis of these data, it is concluded that RT-PCR can be used on single coronary resistance arteries to assess cell-specific mRNA expression and that ecNOS gene expression is upregulated by exercise training in porcine coronary resistance arteries.
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PMID:Induction of nitric oxide synthase mRNA in coronary resistance arteries isolated from exercise-trained pigs. 943 89

The glyceraldehyde-3-phosphate dehydrogenase (gpd) promoter was used to drive expression of lip2, the gene encoding lignin peroxidase (LiP) isozyme H8, in primary metabolic cultures of Phanerochaete chrysosporium. The expression vector, pUGL, also contained the Schizophyllum commune ura1 gene as a selectable marker. pUGL was used to transform a P. chrysosporium Ura11 auxotroph to prototrophy. Ura+ transformants were screened for peroxidase activity in liquid cultures containing high-carbon and high-nitrogen medium. Recombinant LiP (rLiP) was secreted in active form by the transformants after 4 days of growth, whereas endogenous lip genes were not expressed under these conditions. Approximately 2 mg of homogeneous rLiP/liter was obtained after purification. The molecular mass, pI, and optical absorption spectrum of rLiPH8 were essentially identical to those of the wild-type LiPh8 (wt LiPH8), indicating that heme insertion, folding, and secretion functioned normally in the transformant. Steady-state and transient-state kinetic properties for the oxidation of veratryl alcohol between wtLiPH8 and rLiPH8 were also identical.
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PMID:Homologous expression of recombinant lignin peroxidase in Phanerochaete chrysosporium. 1010 66

A 3-h exposure to NO donors (spermine-NO, DETA-NO, or SNAP), or to NOS II-expressing cells (activated macrophages or EMT6 cells) reversibly inhibited DNA synthesis in K562 tumor cells. In GSH-depleted K562 cells, cytostasis remained reversible when induced by DETA-NO or NOS II activity, but became irreversible after exposure to spermine-NO or SNAP. Only SNAP and spermine-NO efficiently inhibited GAPDH, an enzyme with a critical thiol, in GSH-depleted cells. Thus, the irreversible cytostasis induced in GSH-depleted cells by spermine-NO or SNAP can be tentatively attributed to S-nitrosating or oxidizing species derived from NO. However, these species did not contribute significantly to the early antiproliferative effects of macrophages. Ribonucleotide reductase, a key enzyme in DNA synthesis. has been shown to be inhibited by NO. Supplementation of the medium with deoxyribonucleosides to bypass RNR inhibition restored DNA synthesis in target cells exposed to DETA-NO and NO-producing cells, but was inefficient for GSH-depleted cells previously submitted to spermine-NO or SNAP. These cells also exhibited a persistent depletion of the dATP pool. In conclusion, GSH depletion reveals striking qualitative differences in the nature of the toxic effectors released by various NO sources, questioning the significance of S-nitrosating or oxidizing nitrogen oxides in NOS II-dependent cytostasis.
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PMID:Differential cytostatic effects of NO donors and NO producing cells. 1038 Dec

Phex is the gene whose mutation is the cause of X-linked hypophosphatemia in humans and mice. The organs expressing Phex in normal animals, and their possible sensitivity to stimulation by low phosphate diets, are unknown. In this study, Phex expression was measured in 6-wk-old normal B6C3H male and female mice and in 135 g Sprague-Dawley rats fed a normal phosphate diet or a low phosphate diet with deionized water ad libitum for 7 d. The animals were then anesthetized, and a variety of organs were collected and frozen in liquid nitrogen. Phex mRNA expression was measured in each organ by reverse transcription-polymerase chain reaction (RT-PCR) with primers specific for both Phex and glyceraldehyde-3-phosphate dehydrogenase (G3PDH). Southern blots were prepared, hybridized with 32P-labeled internal oligonucleotides, and quantified with a phosphor imager. The Phex/G3PDH ratio was computed, and the data were compiled as the mean +/- SEM. In these growing animals, the highest Phexexpression levels were found in the gonads, brain, and lung. In contrast, Phex expression in calvaria and femur was markedly less. Two significant changes were found in animals that were fed a low phosphate diet. Spleen showed a significant decrease in Phex mRNA levels on low phosphate diet (60+/-10% of normal P diet, n = 12/group, p = 0.002). The pituitary gland showed a significant increase in Phex expression with low phosphate diet (851+/-127% of G3PDH) over normal P diet (569+/-78%, n = 24 - 25/group, p = 0.03). No significant change was found in femur, calvaria, or a variety of soft tissues. In summary, Phex mRNA was found in most tissues examined. Expression levels varied by two orders of magnitude from highest to lowest with more in gonads, brain, and lung and with less in bone. Increased Phex mRNA was found in the pituitary gland of animals that were fed a low phosphate diet.
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PMID:MRNA expression of Phex in mice and rats: the effect of low phosphate diet. 1105 Oct 50

In cattle, retinoic acid (RA) has been indirectly associated with developmental potential of the embryo. RA is transported by retinol-binding protein (RBP) and actions of RA are mediated by several subtypes of nuclear retinoic acid receptors (RAR). Bovine embryos, produced in vitro from oocytes harvested from ovaries collected at a local abattoir, were frozen in liquid nitrogen at the oocyte, 2-, 4-, 8-, 16 to 20-cell, morula, blastocyst, and hatched blastocyst stages. Employing reverse transcription polymerase chain reaction (RT-PCR) we investigated mRNA expression for RBP, RARalpha, RARbeta, RARgamma, and glyceraldehyde-3-phosphate dehydrogenase (GAPDH). Total RNA was extracted from 25 pooled embryos at each stage and RT-PCR analysis was repeated thrice. GAPDH transcript was detected in all stages. Transcripts for RBP, RARalpha, and RARgamma were also detected in all stages from the oocyte through to the hatched blastocyst. Expression of RARbeta was not detected at any stage. Whole-mount immunohistochemistry was performed with intact and hatched blastocysts using polyclonal antibodies against RARalpha and RARgamma2 to investigate if these embryonic mRNAs were translated to the mature protein. Strong immunostaining was observed for both RARalpha and RARgamma2 in the inner cell mass and trophectoderm of intact and hatched blastocysts. Expression of mRNA for RBP, RARalpha, RARgamma, and of the RARalpha and RARgamma2 receptor proteins in the bovine embryo suggests that RA is likely to directly regulate gene expression during preimplantation development in that species.
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PMID:Expression of retinol-binding protein messenger RNA and retinoic acid receptors in preattachment bovine embryos. 1159 39

Growth and starvation of baker's yeast was monitored by on-line microcalorimetry and cells originating from four different physiological states were stored at low temperature (4 degrees C) for up to 26 days. The different physiological states were designated F (respiro-Fermentative phase of growth), R (initial Respiratory phase of growth), -N (non-growing state because of Nitrogen depletion), and -NC (non-growing state because of both Nitrogen and Carbon depletion). The cells were tested before and after cold storage for their fermentative capacity, and characterised by 2D gel analysis (and subsequent quantitative silver staining and image analysis with software PDQUEST) for their levels of six enzymes of the glycolytic pathway (hexokinase 2 (Hxk2p), fructose bisphosphate aldolase (Fba1p), glyceraldehyde-3-phosphate dehydrogenase (Tdh3p), enolase A (Enolp), enolase B (Eno2p), and triose phosphate isomerase (Tpi1p)) and two enzymes of the fermentative branch (pyruvate decarboxylase (Pdc1p) and alcohol dehydrogenase (Adh1p)). The enzymes Hxk2p, Tdh3p, Eno2p, Pdc1p and Adh1p were down-regulated by 25-80% during the transition between the F and R states. During the transition to non-growing states (-N and -NC states), the levels of Hxk2p, Tdh3p and Eno2p were further reduced. However, after cold storage, the glycolytic and fermentative enzymes of the different physiological states were expressed to the same extent. In contrast, the fermentative capacity differed between the states; the R-state cells were superior compared to cells from the other states tested and preserved more than 50% of their initial fermentative capacity (6 mmol ethanol per gram dry weight and hour). Our data therefore clearly demonstrate that persistence of fermentative capacity during total starvation at low temperature after as long as 1 month is strongly dependent on the physiological state from which the cells originate. However, the level of expression of the glycolytic enzymes could not explain the difference in fermentative capacity of the different physiological states after cold storage.
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PMID:Fermentative capacity after cold storage of baker's yeast is dependent on the initial physiological state but not correlated to the levels of glycolytic enzymes. 1178 28

In cattle, administration of retinol at the time of superovulation has been indirectly associated with enhanced developmental potential of the embryo. Vitamin A and its metabolites influence several developmental processes by interacting with 2 different types of nuclear receptors, retinoic acid receptors and retinoid X receptors (RXRs). Given the limited information available concerning the RXR-mediated retinoid signaling system, particularly in species other than rodents, this study was performed to gain insight into the potential role of retinoid signaling during preattachment embryo development in the cow. Bovine embryos were produced in vitro from oocytes harvested from abattoir ovaries and frozen in liquid nitrogen at the oocyte, 2-, 4-, 8-, and 16- to 20-cell, morula, blastocyst, and hatched blastocyst stages. Reverse transcription polymerase chain reaction (PCR) and whole mount in situ hybridization were utilized to investigate mRNA expression for RXR alpha, RXR beta, RXR gamma, alcohol dehydrogenase I (ADH-I), retinaldehyde dehydrogenase 2 (RALDH2), peroxisome proliferator activated receptor gamma (PPAR gamma), and glyceraldehyde-3-phosphate dehydrogenase. Transcripts for RXR alpha, RXR beta, RALDH2, and PPAR gamma were detected in all stages beginning from the oocyte through to the hatched blastocyst. Whole mount in situ hybridization performed using digoxigenin-labeled antisense probes detected all 4 transcripts in both the inner cell mass and the trophectoderm of hatched blastocysts. PCR products obtained for ADH-I exhibited very low homology to known human and mouse sequences. Immunohistochemistry was performed using polyclonal anti-rabbit antibodies against RXR beta and PPAR gamma to investigate whether these embryonic mRNAs were translated to the mature protein. Strong immunostaining was observed for both RXR beta and PPAR gamma in the trophectoderm and inner cell mass cells of intact and hatched blastocysts. Messenger RNA was not detected at any stage for RXR gamma. Expression of mRNA for RXR alpha, RXR beta, RALDH2, and PPAR gamma suggests that the early embryo may be competent to synthesize retinoic acid and regulate gene expression during preattachment development in vitro.
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PMID:Expression patterns of retinoid X receptors, retinaldehyde dehydrogenase, and peroxisome proliferator activated receptor gamma in bovine preattachment embryos. 1187 76

Astrocytes play a key role in the pathogenesis of ammonia-induced neurotoxicity and hepatic encephalopathy. As shown here, ammonia induces protein tyrosine nitration in cultured rat astrocytes, which is sensitive to the N-methyl-D-aspartate (NMDA) receptor antagonist MK-801. A similar pattern of nitrated proteins is produced by NMDA. Ammonia-induced tyrosine nitration depends on a rise in [Ca2+]i, IkB degradation, and NO synthase (iNOS) induction, which are prevented by MK-801 and the intracellular Ca2+ chelator 1,2-bis(o-aminophenoxy)ethane-N,N,N',N'-tetraacetic acid (BAPTA-AM). Moreover, the increase in tyrosine nitration is blunted by L-NMMA, 1400W, uric acid, Cu, Zn-superoxide dismutase/catalase treatment, and methionine-sulfoximine, which indicate the involvement of reactive nitrogen intermediates and intracellular glutamine accumulation. Such reactive nitrogen intermediates additionally mediate ammonia-induced phosphorylation of the MAP-kinases Erk-1/Erk-2 and p38MAPK. Among the proteins, which are tyrosine -nitrated by ammonia, glyceraldehyde-3-phosphate dehydrogenase, the peripheral-type benzodiazepine receptor, Erk-1, and glutamine synthetase are identified. Ammonia-induced nitration of glutamine synthetase is associated with a loss of enzymatic activity. Astroglial protein tyrosine nitration is found in brains from rats after acute ammonia-intoxication or after portacaval anastomosis, indicating the in vivo relevance of the present findings. The production of reactive nitrogen intermediates and protein tyrosine nitration may alter astrocyte function and contribute to ammonia neurotoxicity.
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PMID:Ammonia induces MK-801-sensitive nitration and phosphorylation of protein tyrosine residues in rat astrocytes. 1192 23

S-Adenosyl-L-methionine(SAM) is an important metabolic intermediate in the metabolic flux of sulphur. SAM is involved in three key metabolic pathways: transmethylation, transsulfuration and polyamine synthesis. As a potential therapeutic agent, SAM is being used as over the counter drug and nutrient supplement. An expression vector, harboring SAM synthetase 2 gene from S. cerevisiae and regulated by the glyceraldehyde-3-phosphate dehydrogenase gene promoter P(GAP), was transformed into GS115 strain of P. pastoris. Through zeocin resistance and expression screening, a recombinant strain was obtained that had high SAM yield and the fermentation conditions were optimized. The results showed that carbon source, nitrogen source, pH and dissolved oxygen had significant effects on the accumulation of SAM. The SAM production of the recombinant cells reached 2.49 g/L after fermentation for three days under the optimized conditions. The present studies show that fermentation of recombinant P. pastoris strain, expressing heterologous SAM synthetase gene, may be a promising approach for the production of SAM.
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PMID:[Enhancement of the production of SAM by overexpression of SAM synthetase in Pichia pastoris]. 1254 18

Free radicals are reactive chemical species that differ from other compounds in that they have unpaired electrons in their outer orbitals. They are capable of damaging cellular components, and accumulating evidence suggests that they may contribute to various disease entities including inflammatory joint disease. Reactive oxygen species (ROS) as well as reactive nitrogen species (RNS) can directly or indirectly damage basic articular constituents and lead to the clinical expression of the inflammatory arthritis. Hydroxyl radicals degrade isolated proteoglycans, and HOCl fragments collagen. Hydrogen peroxide, which is very diffusible, readily inhibits cartilage proteoglycan synthesis, e.g. by interfering with ATP synthesis, in part by inhibiting the glycolytic enzyme glyceraldehyde-3-phosphate dehydrogenase in chondrocytes, aggravating the effects of proteolytic and free-radical-mediated cartilage degradation. Peroxynitrite and HOCl may facilitate cartilage damages by inactivating TIMPs. TIMP-1 inhibits stromelysins, collagenases and gelatinases and this ability is lost after ONOO(-) or HOCl treatment. HOCl can also activate latent forms of neutrophil collagenases and gelatinase with obvious consequences. Hypochlorous acid, ONOO(-) and O(2)(*-) react with ascorbate, which is essential for cartilage function, leading to low levels of ascorbate in synovial fluid. Low concentrations of H2O(2), O(2)(*-) or both, accelerate bone resorption by osteoclasts, whereas NO. inhibits it. NO. promotes chondrocyte apoptosis, inhibits proteoglycan synthesis and activates latent metalloproteinases and cyclooxygenase. ROS, produced by activated phagocytes, could alter the antigenic behaviour of immunoglobulin G, producing fluorescent protein aggregates that can further activate phagocytic cells. Radical-exposed IgG is able to bind rheumatoid factor and results in the generation of C3alpha. This reaction may be self-perpetuating within the rheumatoid joint, suggesting that free radicals play a role in the chronicity of the inflammatory reaction which is a key question regarding to which extent free radicals contribute to the consequences of inflammation, such as the cartilage and bone destruction. Reactive oxygen intermediates can also function as signaling messengers to activate transcription factors, like NFkB and AP-1, and induce gene expression. All this knowledge might serve to apply a rational selection of antioxidants for possible therapeutic purposes, enforcing combination therapy of the inflammatory joint disease.
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PMID:The role of free radicals in the pathogenesis of rheumatoid arthritis. 1268 16


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