Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0038187 (starvation)
 24,951 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Glutathione (GSH; gamma-L-glutamyl-L-cysteinyl-glycine), a non-protein thiol with a very low redox potential (E'0 = 240 mV for thiol-disulfide exchange), is present in high concentration up to 10 mM in yeasts and filamentous fungi. GSH is concerned with basic cellular functions as well as the maintenance of mitochondrial structure, membrane integrity, and in cell differentiation and development. GSH plays key roles in the response to several stress situations in fungi. For example, GSH is an important antioxidant molecule, which reacts non-enzymatically with a series of reactive oxygen species. In addition, the response to oxidative stress also involves GSH biosynthesis enzymes, NADPH-dependent GSH-regenerating reductase, glutathione S-transferase along with peroxide-eliminating glutathione peroxidase and glutaredoxins. Some components of the GSH-dependent antioxidative defence system confer resistance against heat shock and osmotic stress. Formation of protein-SSG mixed disulfides results in protection against desiccation-induced oxidative injuries in lichens. Intracellular GSH and GSH-derived phytochelatins hinder the progression of heavy metal-initiated cell injuries by chelating and sequestering the metal ions themselves and/or by eliminating reactive oxygen species. In fungi, GSH is mobilized to ensure cellular maintenance under sulfur or nitrogen starvation. Moreover, adaptation to carbon deprivation stress results in an increased tolerance to oxidative stress, which involves the induction of GSH-dependent elements of the antioxidant defence system. GSH-dependent detoxification processes concern the elimination of toxic endogenous metabolites, such as excess formaldehyde produced during the growth of the methylotrophic yeasts, by formaldehyde dehydrogenase and methylglyoxal, a by-product of glycolysis, by the glyoxalase pathway. Detoxification of xenobiotics, such as halogenated aromatic and alkylating agents, relies on glutathione S-transferases. In yeast, these enzymes may participate in the elimination of toxic intermediates that accumulate in stationary phase and/or act in a similar fashion as heat shock proteins. GSH S-conjugates may also form in a glutathione S-transferases-independent way, e.g. through chemical reaction between GSH and the antifugal agent Thiram. GSH-dependent detoxification of penicillin side-chain precursors was shown in Penicillium sp. GSH controls aging and autolysis in several fungal species, and possesses an anti-apoptotic feature.
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PMID:Glutathione, altruistic metabolite in fungi. 1551 28

The levels of the lipid peroxidation products (LPO), different forms of protein SH-groups and their oxidation rate in the homogenates of the mesencephalon, hypothalamus and sensorymotor cortex of normal and GSH-deficient rats under 3-day food starvation were studied. It was shown, that the basic level of LPO products--lipid hydroperoxides and malonic dialdehyde (MDA) in hypothalamus and sensorymotor cortex of normal animals are by 20-30% (p < 0.05) higher and reduced glutathione (GSH) content is 2 times higher, than these values in mesencephalon. Under 3 day starvation of normal animals activation of the LPO observed only in the hypothalamus and sensorymotor cortex, whereas under 3 day starvation of the GSH-deficient rats formed by the intraparenteraly injection of diethylmaleate in a dose of 2.5 mmol/kg of body weight in all investigated structures the lipid hydroperoxides and MDA increased many times (2-3 times), the content of the surface and masked protein SH-groups decreased and essentially increased the oxidation rate of these functional groups. It was proposed that GSH and its enzymes participate in the LPO regulation and protection of protein SH-groups from oxidative damage at this event the intensity of this prosesse depends on structural and functional organization of nervous tissues.
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PMID:[Glutathione-deficient state of nervous tissues in starved animals intensifies lipid peroxidation and oxidation of protein SH-groups]. 1590 25

Glutathione (GSH) is the most abundant non-protein thiol in eukaryotic cells and acts as reducing equivalent in many cellular processes. We investigated the role of glutathione in Dictyostelium development by disruption of gamma-glutamylcysteine synthetase (GCS), an essential enzyme in glutathione biosynthesis. GCS-null strain showed glutathione auxotrophy and could not grow in medium containing other thiol compounds. The developmental progress of GCS-null strain was determined by GSH concentration contained in preincubated media before development. GCS-null strain preincubated with 0.2 mM GSH was arrested at mound stage or formed bent stalk-like structure during development. GCS-null strain preincubated with more than 0.5 mM GSH formed fruiting body with spores, but spore viability was significantly reduced. In GCS-null strain precultured with 0.2 mM GSH, prestalk-specific gene expression was delayed, while prespore-specific gene and spore-specific gene expressions were not detected. In addition, GCS-null strain precultured with 0.2 mM GSH showed prestalk tendency and extended G1 phase of cell cycle. Since G1 phase cells at starvation differentiate into prestalk cells, developmental defect of GCS-null strain precultured with 0.2 mM GSH may result from altered cell cycle. These results suggest that glutathione itself is essential for growth and differentiation to prespore in Dictyostelium.
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PMID:Glutathione is required for growth and prespore cell differentiation in Dictyostelium. 1599 6

L-glutamine (Gln) withdrawal rapidly triggers apoptosis in the murine hybridoma cell line Sp2/0-Ag14 (Sp2/0). In this report, we examined the possibility that Gln deprivation of Sp2/0 cells triggers an oxidative stress which would contribute to the activation of apoptotic pathways. Gln withdrawal triggered an oxidative stress in Sp2/0 cells, as indicated by an increased accumulation of reactive oxygen species (ROS) and an increase in the intracellular content in protein carbonyl groups. Gln starvation also caused a decrease in the intracellular levels of glutathione (GSH). However, a decrease in GSH was not sufficient to induce Sp2/0 cell death since reducing GSH levels with DL-buthionine-[S,R]-sulfoximine did not affect cell viability. The antioxidant N-acetyl-L-cysteine (NAC), while effective in inhibiting ROS accumulation and oxidative stress, did not prevent the loss in cell viability or the processing and activation of caspase-3 triggered by Gln starvation. On the other hand, NAC did reduce the formation of apoptotic bodies in dying cells. Altogether these results indicate that in Sp2/0 cells, Gln deprivation leads to the induction of an oxidative stress which, while involved in the formation of apoptotic bodies, is not essential to the activation of the cell death program.
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PMID:Oxidative stress is not required for the induction of apoptosis upon glutamine starvation of Sp2/0-Ag14 hybridoma cells. 1641 32

In a previous study we analysed the effect of diesel seawater contamination in the digestive gland of the Antarctic limpet Nacella concinna. We observed that antioxidant enzyme activities decreased after one-week starvation prior to the experiment, and this was considered in the analysis of the obtained results. To know whether the digestive gland oxidant-antioxidant status may be altered by starvation and experimental conditions, we evaluated the food deprivation effect in limpets from the nearshore shallow waters of Potter Cove, Antarctica. Organisms were acclimated to laboratory conditions and were divided in fed and starved groups, and maintained in these conditions during one month. Every week 20 limpets were sampled from each group. Digestive glands were dissected and kept frozen until they were processed. Superoxide dismutase (SOD), catalase (CAT) and glutathione S-transferase (GST) activities, as well as lipid peroxidation (LPO) measured as thiobarbituric reactive substances (TBARS), protein oxidation (PO) and reduced glutathione (GSH) were measured. For both groups of limpets, SOD increased its activity in the first week of the exposure period, with a maximum in the second week. CAT activity increased significantly in the second week, only for the starved group. Similarly, GST activity also increased for starved group in the second week; but maintained this tendency for both groups until the fourth week. In fed and starved limpets, TBARS values increased significantly, during the first week and then returned to normal values. The PO levels in the starved group increased only during the first week. The GSH content, for the fed group, increased significantly after the third week. The obtained results indicate that biochemical or physiological studies conducted with N. concinna should consider the effects of food deprivation and time spent under experimental conditions.
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PMID:Does starvation influence the antioxidant status of the digestive gland of Nacella concinna in experimental conditions? 1719 86

In a laboratory-selected Cr-tolerant strain of the unicellular green alga Scenedesmus acutus, the capacity to synthesize higher amounts of cysteine (Cys) and reduced glutathione (GSH) than the wild-type was demonstrated to underlie tolerance to Cd and Cr(VI). In photosynthetic organisms sulfate constitutes the main sulfur source for the biosynthesis of GSH and its precursor Cys, hence it was hypothesized that the sensitivity of the two strains to Cr(VI) could be modified after culturing in sulfate-deprived medium. Both strains were grown in the presence of different concentrations or in the absence of sulfate (sulfur-starved) and then assayed for Cr(VI) tolerance in standard medium. Unstarved, sulfur-starved and sulfur-replete cells (cells maintained in standard medium after S-starvation) were analysed for Cys, GSH and sulfur content. Sulfur-starved cells showed a greater tolerance to Cr(VI) than unstarved ones. The increased tolerance was ascribable to a transient physiological change and can be considered as specifically due to sulfur deprivation, since it was lost after a 3-day culture in standard medium and was not exhibited by nitrogen-starved cells. The comparison between Cys, GSH and sulfur content in sulfur-starved and sulfur-replete cells of the two strains suggests that the higher tolerance to Cr(VI) after S-starvation could depend on the up-regulation of sulfate uptake mechanisms, and that the primary reason for the higher tolerance to chromium in the selected strain could be due to greater sensitivity to the decrease in negative intracellular end-products (free Cys and GSH) leading to an earlier up-regulation of sulfate assimilation processes.
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PMID:Sulfur starvation and chromium tolerance in Scenedesmus acutus: a possible link between metal tolerance and the regulation of sulfur uptake/assimilation processes. 1772 73

In studying the regulation of GSH11, the structural gene of the high-affinity glutathione transporter (GSH-P1) in Saccharomyces cerevisiae, a cis-acting cysteine responsive element, CCGCCACAC (CCG motif), was detected. Like GSH-P1, the cystathionine gamma-lyase encoded by CYS3 is induced by sulfur starvation and repressed by addition of cysteine to the growth medium. We detected a CCG motif (-311 to -303) and a CGC motif (CGCCACAC; -193 to -186), which is one base shorter than the CCG motif, in the 5'-upstream region of CYS3. One copy of the centromere determining element 1, CDE1 (TCACGTGA; -217 to -210), being responsible for regulation of the sulfate assimilation pathway genes, was also detected. We tested the roles of these three elements in the regulation of CYS3. Using a lacZ-reporter assay system, we found that the CCG/CGC motif is required for activation of CYS3, as well as for its repression by cysteine. In contrast, the CDE1 motif was responsible for only activation of CYS3. We also found that two transcription factors, Met4 and VDE, are responsible for activation of CYS3 through the CCG/CGC and CDE1 motifs. These observations suggest a dual regulation of CYS3 by factors that interact with the CDE1 motif and the CCG/CGC motifs.
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PMID:Transcriptional regulation of Saccharomyces cerevisiae CYS3 encoding cystathionine gamma-lyase. 1831 67

This work aims to elucidate the relationship between nitrogen depletion and Glutathione (GSH) level in Schizosaccharomyces pombe. The total GSH level was much higher in the Pap1-positive KP1 cells than in the Pap1-negative TP108-3C cells, suggesting that synthesis of GSH is dependent on Pap1. When the Pap1-positive KP1 cells were transferred to the nitrogen-depleted medium, total GSH level significantly increased up to 6 h and then slightly declined after 9 h. Elevation of the total GSH level was observed to be much less with the Pap1-negative cells. However, glucose deprivation was not able to enhance the GSH level in the KP1 cells. Activity of gamma-glutamyltranspeptidase (gamma-GT), an enzyme in the first step of GSH catabolism, also increased during nitrogen depletion. The total GSH level was more significantly enhanced in the KP1 cells overexpressing gamma-GT2 than gamma-GT1 during nitrogen starvation. Reactive oxygen species (ROS) levels were not changed during nitrogen starvation in both Pap1-positive and Pap1-negative cells. Collectively, nitrogen depletion causes up-regulation of GSH synthesis and gamma-GT in a Pap1-dependent manner.
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PMID:Nitrogen depletion causes up-regulation of glutathione content and gamma-glutamyltranspeptidase in Schizosaccharomyces pombe. 1833 96

We have recently shown that carnitine deficiency could represent a risk factor in paracetamol hepatotoxicity. By the same token, d-carnitine-induced carnitine deficiency aggravated carboplatin nephropathy following challenge with a single dose (35mg/kg, IP) of the platinum drug in male Swiss albino rats. The combination modality induced marked degenerative changes and severe inflammation in kidney tissues that surpassed either carboplatin or d-carnitine given alone. The combined regimen synergistically increased the serum levels of creatinine, blood urea nitrogen (BUN), tumor necrosis factor alpha (TNF-alpha), palmitate, and kidney malondialdehyde (MDA), adenosine triphosphate (ATP), nitric oxide (NO) contents as well as kidney myeloperoxidase (MPO) activity. The only parameter that has been notably decreased was the kidney reduced glutathione (GSH) level. Exaggeration by carnitine deficit of the deleterious effects of carboplatin is most probably ascribed to energy starvation. The reduction in kidney content of ATP parcels was associated with elevation of serum palmitate level that reflected debilitated fatty acid oxidation, and this further deteriorated energy resources in kidney tissues. Compromising the oxidant/anti-oxidant balance and modulating the release of some inflammatory endocoids namely, TNF-alpha and NO could also possibly account for such combinatorial detrimental toxicity. The current study was further extended to elucidate any possible nephroprotective effects of l-carnitine. Interestingly, carnitine supplementation ahead of carboplatin challenge ameliorated and almost normalized all the biochemical parameters and also mitigated the injurious effects of the cytotoxic drug. Thus, one could conclude that carnitine deficiency, whether being a causative clue or a sequela, might represent a risk factor in carboplatin nephropathy.
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PMID:Carnitine deficiency aggravates carboplatin nephropathy through deterioration of energy status, oxidant/anti-oxidant balance, and inflammatory endocoids. 1885 9

The structural gene encoding bacterioferritin comigratory protein (Bcp) was amplified using PCR from the genomic DNA of Schizosaccharomyces pombe, and transferred into the shuttle vector pRS316 to generate the recombinant plasmid pBCPlO. The bcp(+) mRNA level in the pBCPlO-containing yeast cells was significantly higher than that in the control yeast cells, indicating that the cloned gene is functioning. The S. pombe cells harboring the plasmid pBCPIO exhibited higher survival on the solid minimal media with hydrogen peroxide, tert-BOOH or cadmium than the control yeast cells. They also exhibited enhanced cellular viability in the liquid media containing the stressful agents. The increased viabilities of the fission yeast cells harboring the plasmid pBCP10 were also obtained with 0.4% glucose or 0.4% sucrose as a sole carbon source, and nitrogen starvation, compared with those of the control yeast cells. The total glutathione (GSH) content and total GSH/GSSG ratio were significantly higher in the yeast cells harboring the plasmid pBCP10 than in the control yeast cells. In brief, the S. pombe Bcp plays a protective role in the defensive response to oxidative stress possibly via up-regulation of total and reduced glutathione levels.
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PMID:Overexpression of bacterioferritin comigratory protein (Bcp) enhances viability and reduced glutathione level in the fission yeast under stress. 1922 92


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