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:4.1.2.13 (aldolase)
3,461 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Physiological acclimation that alters enzyme activity can compensate for the effect of temperature on function and may be achieved by altering enzyme concentration. This study uses phylogenetic analyses to investigate the evolutionary history of and to test several hypotheses about acclimation responses among all the glycolytic enzymes. These hypotheses are that (1) acclimation increases enzyme concentration at lower temperatures to compensate for reduced activity; (2) equilibrium enzymes tend to show acclimation responses; and (3) acclimation responses are more common in species whose populations experience either large temporal or geographical temperature variations. Using maximal activities as indices of enzyme concentration, the presence of acclimation responses in all the glycolytic enzymes in the heart ventricle was determined for five species in the teleost genus Fundulus. Three of these species are distributed along the steep thermal cline of the North American Atlantic coast, and thus these species experience both seasonal and geographical variation in temperature. The other two species are found in the Gulf of Mexico and experience seasonal variation similar to the Atlantic species but no geographical variation in temperature. Two Atlantic coast species, Fundulus heteroclitus and Fundulus majalis, have unique derived acclimation responses. No derived acclimation responses occur in the Gulf species. A conserved response in hexokinase was observed within one subgenus comprising both Atlantic and Gulf species. In F. heteroclitus, enolase responded to acclimation, and in F majalis, aldolase, triphosphate isomerase, and lactate dehydrogenase had acclimation responses. These enzymes are equilibrium enzymes, and the concentrations of all of them increase at lower temperatures, which would compensate for the effect of temperature on enzyme activity. The compensatory changes all occur in the Atlantic species and may be a mechanism for species to expand their ranges. These data suggest that physiological acclimation is evolutionarily labile.
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PMID:Phylogenetic analysis of thermal acclimation of the glycolytic enzymes in the genus Fundulus. 936 Nov 33

The organic hydroperoxides t-butyl hydroperoxide, cumene hydroperoxide, and peracetic acid were found to act similarly to hydrogen peroxide in causing inactivation of enzymes within intact spores of bacillus megaterium ATCC 19213 concomitant with mortality. Spores treated with lethal levels of the agents were germinated and permeabilized for enzyme assays. The hierarchy of sensitivities among enolase, glucose-6-phosphate dehydrogenase (G6Pdh), and pyruvate kinase to inactivation varied somewhat with the specific hydroperoxide used, possibly because of the differences in the types of radicals generated. However, each agent inactivated each of the enzymes, albeit at different rates. Comparative assessments of enzyme inactivation by lethal levels of H2O2 or by moist heat showed that some enzymes, such as G6Pdh, are highly sensitive to inactivation, while others, such as ATPases, are much more resistant. The enzymes G6Pdh and aldolase were highly sensitive to hydroperoxide inactivation and also to moist heat, while pyruvate kinase was much more sensitive to hydroperoxides than to moist heat. Our overall interpretation of the findings is that hydroperoxides and moist heat can produce cumulative damage to sensitive enzymes within spores, which progressively diminishes the capacities of the cells to undergo the outgrowth required for return to vegetative life.
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PMID:Inactivation of enzymes within spores of Bacillus megaterium ATCC 19213 by hydroperoxides. 974 72

The transcription rates of glycolytic enzyme genes are coordinately induced when cells are exposed to low oxygen tension. This effect has been described in many cell types and is not restricted to species or phyla. In mammalian cells, there are 11 distinct glycolytic enzymes, at least 9 of which are induced by hypoxia. Recent reports described a role for the hypoxia-inducible factor-1 (HIF-1) in the transcriptional activation of lactate dehydrogenase A, aldolase-A, phosphoglycerate kinase, and enolase-1 genes. It is not known whether the HIF-1 factor acts exclusively to regulate these genes during hypoxia, or how the other genes of the pathway are regulated. In this paper, we describe analyses of the muscle-specific pyruvate kinase-M and beta-enolase promoters that implicate additional mechanisms for the regulation of glycolytic enzyme gene transcription by hypoxia. Transient transcription of a reporter gene directed by either promoter was activated when transfected muscle cells were exposed to hypoxia. Neither of these promoters contain HIF-1 binding sites. Instead, the hypoxia response was localized to a conserved GC-rich element positioned immediately upstream of a GATAA site in the proximal promoter regions of both genes. The GC element was essential for both basal and hypoxia-induced expression and bound the transcription factors Sp1 and Sp3. Hypoxia caused the progressive depletion of Sp3 determined by DNA binding studies and Western analyses, whereas Sp1 protein levels remained unchanged. Overexpression of Sp3 repressed expression of beta-enolase promoters. It is concluded that hypoxia activates these glycolytic enzyme gene promoters by down-regulating Sp3, thereby removing the associated transcriptional repression.
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PMID:Hypoxia regulates beta-enolase and pyruvate kinase-M promoters by modulating Sp1/Sp3 binding to a conserved GC element. 974 88

Two different strains of mice with different susceptibilities to systemic candidiasis (BALB/c and CBA/H) were infected with Candida albicans SC5314. Immune sera were obtained on different days post-infection and assayed against two-dimensional polyacrylamide gel electrophoresis separation of cytoplasmic extracts obtained from protoplasts. More than 31 immunoreactive proteins were detected. Some of them were identified and found to correspond to (i) glycolytic enzymes, such as fructose biphosphate aldolase, triose phosphate isomerase (TPIS), glyceraldehyde-3-phosphate dehydrogenase, 3-phosphoglycerate kinase (PGK), enolase (ENO1) and pyruvate kinase, (ii) other metabolic enzymes, such as methionine synthase (METE), inosine-5'-monophosphate dehydrogenase (IMH3), alcohol dehydrogenase and aconitate hydratase and (iii) heat shock proteins: HS71 (or Ssa1p) and HS75 (or Ssb1p), both from the HSP70 family. This work reports for the first time antigenic properties for IMH3 and TPIS. Different profiles of antibody expression, depending on the mouse strain and the course of infection, were observed. ENO1 was the most immunogenic protein in infected BALB/c mice (the most resistant strain). On the other hand, sera from CBA/H mice (a more susceptible strain) showed a strong increase in reactivity along the infection against METE, HS75 and PGK. Many of these immunoreactive proteins have also been detected using sera from human patients with systemic candidiasis, thus indicating the usefulness of the murine model for studying the antibody response in systemic candidiasis. In this work we demonstrate that the combination of two-dimensional electrophoresis with immunoblotting using murine immune sera can be an important tool for the identification of C. albicans antigens and for monitoring the evolution of the disease.
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PMID:Analysis of the serologic response to systemic Candida albicans infection in a murine model. 1168 Dec 8

The hyperthermophilic, sulfate-reducing archaeon Archaeoglobus fulgidus strain 7324, rather than the type strain VC16, was found to grow on starch and sulfate as energy and carbon source. Fermentation products and enzyme activities were determined in starch-grown cells and compared to those of cells grown on lactate and sulfate. During exponential growth on starch, 1 mol of glucose-equivalent was incompletely oxidized with sulfate to approximately 2 mol acetate, 2 mol CO2 and 1 mol H2S. Starch-grown cells did not contain measurable amounts of the deazaflavin factor F420 (<0.03 nmol/mg protein) and thus did not show the F420-specific green-blue fluorescence. In contrast, lactate (1 mol) was completely oxidized with sulfate to 3 mol CO2 by strain 7324, and lactate-grown cells contained high amounts of F420 (0.6 nmol/mg protein). In extracts of starch-grown cells, the following enzymes of a modified Embden-Meyerhof pathway were detected: ADP-dependent hexokinase (ADP-HK), phosphoglucose isomerase, ADP-dependent 6-phosphofructokinase (ADP-PFK), fructose-1,6-phosphate aldolase, glyceraldehyde-3-phosphate:ferredoxin oxidoreductase (GAP:FdOR), phosphoglycerate mutase, enolase, and pyruvate kinase (PK). Specific activities of ADP-HK, ADP-PFK, GAP:FdOR, and PK were significantly higher in starch-grown cells than in lactate-grown cells, indicating induction of these enzymes during starch catabolism. Pyruvate conversion to acetate involved pyruvate:ferredoxin oxidoreductase and ADP-forming acetyl-CoA synthetase. The findings indicate that the archaeal sulfate reducer A. fulgidus strain 7324 converts starch to acetate via a modified Embden-Meyerhof pathway and acetyl-CoA synthetase (ADP-forming). This is the first report of growth of a sulfate reducer on starch, i.e. on a polymeric sugar.
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PMID:Sugar utilization in the hyperthermophilic, sulfate-reducing archaeon Archaeoglobus fulgidus strain 7324: starch degradation to acetate and CO2 via a modified Embden-Meyerhof pathway and acetyl-CoA synthetase (ADP-forming). 1170 74

Formation of mixed disulfides between glutathione and the cysteines of some proteins (glutathionylation) has been suggested as a mechanism through which protein functions can be regulated by the redox status. The aim of this study was to identify the proteins of T cell blasts that undergo glutathionylation under oxidative stress. To this purpose, we radiolabeled cellular glutathione with (35)S, exposed T cells to oxidants (diamide or hydrogen peroxide), and performed nonreducing, two-dimensional electrophoresis followed by detection of labeled proteins by phosphorimaging and their identification by mass spectrometry techniques. We detected several proteins previously not recognized to be glutathionylated, including cytoskeletal proteins (vimentin, myosin, tropomyosin, cofilin, profilin, and the already known actin), enzymes (enolase, aldolase, 6-phosphogluconolactonase, adenylate kinase, ubiquitin-conjugating enzyme, phosphoglycerate kinase, triosephosphate isomerase, and pyrophosphatase), redox enzymes (peroxiredoxin 1, protein disulfide isomerase, and cytochrome c oxidase), cyclophilin, stress proteins (HSP70 and HSP60), nucleophosmin, transgelin, galectin, and fatty acid binding protein. Based on the presence of several protein isoforms in control cells, we suggest that enolase and cyclophilin are heavily glutathionylated under basal conditions. We studied the effect of glutathionylation on some of the enzymes identified in the present study and found that some of them (enolase and 6-phosphogluconolactonase) are inhibited by glutathionylation, whereas the enzymatic activity of cyclophilin (peptidylprolyl isomerase) is not. These findings suggest that protein glutathionylation might be a common mechanism for the global regulation of protein functions.
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PMID:Identification by redox proteomics of glutathionylated proteins in oxidatively stressed human T lymphocytes. 1190 14

Expression of genes encoding enzymes involved in specialized metabolic pathways is assumed to be regulated coordinately to maintain homeostasis in plant cells. We analyzed transcript levels of rice (Oryza sativa L.) genes associated with glycolysis and alcohol fermentation under submergence stress. When each transcript was quantified at several times, two types (I and II) of mRNA accumulation were observed in response to submergence stress. Transcripts of type I genes reached a maximum after 24 h of submergence and were reduced by transfer to aerobic conditions or by partial exposure of shoot tips to air. In a submergence-tolerant rice cultivar, transcript amounts of several type I genes, such as glucose phosphate isomerase, phosphofructokinase, glyceraldehyde phosphate dehydrogenase, and enolase, increased significantly compared to an intolerant cultivar after 24 h of submergence. This suggests that the mRNA accumulation of type I genes increases in response to anaerobic stress. mRNA accumulation of type II genes, such as aldolase and pyruvate kinase, reached a maximum after 10 h of submergence. Following transfer to aerobic conditions, their transcript levels were not so rapidly decreased as were type I genes. These results suggest that the mRNA levels of genes engaged in glycolysis and alcohol fermentation may be regulated differentially under submergence stress.
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PMID:Differential Transcript Levels of Genes Associated with Glycolysis and Alcohol Fermentation in Rice Plants (Oryza sativa L.) under Submergence Stress. 1223 82

The viability of lactic acid bacteria in frozen, freeze-dried, and air-dried forms is of significant commercial interest to both the dairy and food industries. In this study we observed that when prestressed with either heat (50 degrees C) or salt (0.6 M NaCl), Lactobacillus rhamnosus HN001 (also known as DR20) showed significant (P < 0.05) improvement in viability compared with the nonstressed control culture after storage at 30 degrees C in the dried form. To investigate the mechanisms underlying this stress-related viability improvement in L. rhamnosus HN001, we analyzed protein synthesis in cultures subjected to different growth stages and stress conditions, using two-dimensional gel electrophoresis and N-terminal sequencing. Several proteins were up- or down-regulated after either heat or osmotic shock treatments. Eleven proteins were positively identified, including the classical heat shock proteins GroEL and DnaK and the glycolytic enzymes glyceraldehyde-3-phosphate dehydrogenase, lactate dehydrogenase, enolase, phosphoglycerate kinase, and triose phosphate isomerase, as well as tagatose 1,6-diphosphate aldolase of the tagatose pathway. The phosphocarrier protein HPr (histidine-containing proteins) was up-regulated in cultures after the log phase irrespective of the stress treatments used. The relative synthesis of an ABC transport-related protein was also up-regulated after shock treatments. Carbohydrate analysis of cytoplasmic contents showed higher levels (20 +/- 3 microg/mg of protein) in cell extracts (CFEs) derived from osmotically stressed cells than in the unstressed control (15 +/- 3 microg/mg of protein). Liquid chromatography of these crude carbohydrate extracts showed significantly different profiles. Electrospray mass spectrometry analysis of CFEs revealed, in addition to normal mono-, di-, tri-, and tetrasaccharides, the presence of saccharides modified with glycerol.
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PMID:Heat and osmotic stress responses of probiotic Lactobacillus rhamnosus HN001 (DR20) in relation to viability after drying. 1257 Oct 12

The influence of caloric restriction (CR) from 2 months of age on the activities of liver glycolytic enzymes and metabolite levels was studied in young and old mice. Livers were sampled 48 h after the last scheduled feeding time. Old mice on CR showed significant decreases in the activities of all the enzymes studied, except for aldolase, triosephosphate isomerase and phosphoglycerate mutase, which were unchanged. The metabolites glucose, glucose-6-phosphate, fructose-6-phosphate, pyruvate and lactate were lower while fructose-1,6-bisphosphate, glyceraldehyde-3-phosphate, dihydroxyacetone phosphate, 3-phosphoglycerate and phosphoenolpyruvate were increased in old CR. Young mice on CR also showed reduced enzyme activities, except for aldolase, triosephosphate isomerase and enolase which were unchanged when compared with young controls. The metabolites glucose, glucose-6-phosphate, fructose-6-phosphate and pyruvate were decreased when compared with young controls, while phosphoenolpyruvate was increased. Ketone bodies increased (65%) in old, but not young, CR mice while fructose-2,6-bisphosphate decreased in both young (22%) and old CR (28%) mice. The results indicate that decreased hepatic glucose levels in CR mice are associated with decreased enzyme activities but not a uniform decrease in metabolite levels. Increased ketone body levels indicate increased utilization of non-carbohydrate fuels while decreased fructose-2,6-bisphosphate level suggests its importance in the control of glycolysis in CR.
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PMID:Influence of age and caloric restriction on liver glycolytic enzyme activities and metabolite concentrations in mice. 1258 89

Ferriprotoporphyrin IX (FPIX) is a potentially toxic product of hemoglobin digestion by intra-erythrocytic malaria parasites. It is detoxified by biomineralization or through degradation by glutathione. Both processes are inhibited by the antimalarial drug chloroquine, leading to the accumulation of FPIX in the membranes of the infected cell and their consequent permeabilization. It is shown here that treatment of Plasmodium falciparum-infected erythrocytes with chloroquine also leads to the binding of FPIX to a subset of parasite proteins. Parasite enzymes such as aldolase, pyrimidine nucleaside monophosphate kinase and pyrimidine 5'-nucleotidase were inhibited by FPIX in vitro, but only the activity of 6-phosphogluconate dehydrogenase was reduced significantly in cells after drug treatment. Additional proteins were extracted from parasite cytosol by their ability to bind FPIX. Sequencing of these proteins identified heat shock proteins 90 and 70, enolase, elongation factor 1-alpha, phoshoglycerate kinase, glyceraldehyde 3-phosphate dehydrogenase, L-lactate dehydrogenase and gametocytogenesis onset-specific protein. The possible involvement of these proteins in the antimalarial mode of action of chloroquine is discussed. It is concluded that drug-induced binding of FPIX to parasite glycolytic enzymes could underlie the demonstrable inhibition of glycolysis by chloroquine. The inhibition of 6-phosphogluconate dehydrogenase could explain the reduction of the activity of the hexose monophosphate shunt by the drug. Inhibition of both processes is deleterious to parasite survival. Binding of FPIX to other proteins is probably inconsequential to the rapid killing of the parasite by chloroquine.
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PMID:The treatment of Plasmodium falciparum-infected erythrocytes with chloroquine leads to accumulation of ferriprotoporphyrin IX bound to particular parasite proteins and to the inhibition of the parasite's 6-phosphogluconate dehydrogenase. 1266 48


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