Comparative transcriptome and metabolome analysis reveal glutathione metabolic network and functional genes underlying blue and red-light mediation in maize seedling leaf

Abstract Background Light quality severely affects biosynthesis and metabolism-associated process of glutathione. However, the role of specific light is still unclear on the glutathione metabolism. In this article, comparatively transcriptome and metabolome methods are used to fully understand the blue and red-light conditions working on the glutathione metabolism in maize seedling leaf. Results There are 20 differently expressed genes and 4 differently expressed metabolites in KEGG pathway of glutathione metabolism. Among them, 12 genes belong to the glutathione S-transferase family, 3 genes belong to the ascorbate peroxidase gene family and 2 genes belong to the ribonucleoside-diphosphate reductase gene family. Three genes, G6PD, SPDS1, and GPX1 belong to the gene family of glucose 6-phosphate dehydrogenase, spermidine synthase, and glutathione peroxidase, respectively. Four differently expressed metabolites are identified. Three of them, Glutathione disulfide, Glutathione, and l-γ-Glutamyl-L-amino acid are decreased while L-Glutamate is increased. In addition, Through PPI analysis, two annotated genes gst16 and DAAT, and 3 unidentified genes 100381533, pco105094 and umc2770, identified as RPP13-like3, BCAT-like1and GMPS, were obtained. By the analysis of protein sequence and PPI network, we predict that pco105094 and umc2770 were involved in the GSSG-GSH and AsA-GSH cycle in the network of glutathione metabolism. Conclusions Compared to red light, blue light remarkably changed the transcription signal transduction and metabolism of glutathione metabolism. Differently expressed genes and metabolic mapped to the glutathione metabolism signaling pathways. In total, we obtained three unidentified genes, and two of them were predicted in current glutathione metabolism network. This result will contribute to the research of glutathione metabolism of maize.

Download Full-text

Glutathione metabolism in heart and liver of the aging rat

Biochemistry and Cell Biology ◽

10.1139/o94-010 ◽

1994 ◽

Vol 72 (1-2) ◽

pp. 58-61 ◽

Cited By ~ 35

Author(s):

M. Stio ◽

T. Iantomasi ◽

F. Favilli ◽

P. Marraccini ◽

B. Lunghi ◽

...

Keyword(s):

Rat Heart ◽

Reduced Glutathione ◽

Age Groups ◽

Glutathione Metabolism ◽

Oxidized Glutathione ◽

Glutathione S Transferase ◽

Age Related ◽

Glutamylcysteine Synthetase ◽

Old Rats ◽

Glucose 6 Phosphate Dehydrogenase

A comprehensive study on glutathione metabolism in rat heart and liver as a function of age was performed. In the heart, reduced glutathione, total glutathione, and the glutathione redox index showed a decrease during aging, while oxidized glutathione levels increased in 5-month-old rats with respect to the young animals and remained quite constant in 14- and 27-month-old rats. In the liver, the highest levels of reduced glutathione were found in the 2-month-old rats, while oxidized glutathione reached a peak at 5 months. Glutathione-associated enzymes showed age-related changes. Glutathione peroxidase, unaffected by aging in the heart, decreased in the liver of the 27-month-old rats. In the heart and the liver, the highest values of glutathione S-transferase were found at 5 months and 27 months, respectively. Glucose-6-phosphate dehydrogenase followed a similar trend in both heart and liver. Glutathione reductase also showed the same behaviour in heart and in liver, increasing in old rats with respect to the other age groups. A decrease in γ-glutamylcysteine synthetase was found in the heart and liver of 27-month-old rats in comparison with the 2-month-old ones. In conclusion, a decreased antioxidant capability has been demonstrated in both heart and liver of old rats.Key words: glutathione metabolism, age, rat heart, rat liver.

Download Full-text

Physiological changes in glutathione metabolism in foetal and newborn rat liver

Biochemical Journal ◽

10.1042/bj2740891 ◽

1991 ◽

Vol 274 (3) ◽

pp. 891-893 ◽

Cited By ~ 41

Author(s):

F V Pallardo ◽

J Sastre ◽

M Asensi ◽

F Rodrigo ◽

J M Estrela ◽

...

Keyword(s):

Amino Acid ◽

Isolated Hepatocytes ◽

Glutathione Metabolism ◽

Glutathione S Transferase ◽

Adult Rats ◽

Adult Transition ◽

Glutathione Redox Cycle ◽

Glucose 6 Phosphate Dehydrogenase ◽

Low Activity ◽

Glutathione Redox

Glutathione metabolism was studied in isolated hepatocytes from foetal, newborn and adult rats. The GSH/GSSG ratio decreased 15-20-fold through the foetal-neonatal-adult transition. This was mainly due to an increase in GSSG. All enzyme activities involved in the glutathione redox cycle tend to increase during that transition, but the relative increases in glutathione peroxidase and glutathione S-transferase were 3-5 times those of glutathione reductase or glucose-6-phosphate dehydrogenase. GSH synthesis from methionine as a sulphur source was 6 times lower in foetal than in adult hepatocytes. However, when N-acetylcysteine was used as a sulphur donor to by-pass the cystathionine pathway, the rates of GSH synthesis were similar in foetal and adult cells. This is due to the fact that cystathionase activity in foetal cells is very low. This low activity is reflected in the blood amino acid pattern, where the concentration of cysteine rises from 8 to 52 microM from foetuses to adult rats. This supports the idea that cysteine may be an essential amino acid for the premature animal.

Download Full-text

The glutathione S-transferase D genes. A divergently organized, intronless gene family in Drosophila melanogaster

Journal of Biological Chemistry ◽

10.1016/s0021-9258(18)98410-3 ◽

1993 ◽

Vol 268 (13) ◽

pp. 9737-9746

Author(s):

Y.P. Toung ◽

T.S. Hsieh ◽

C.P. Tu

Keyword(s):

Drosophila Melanogaster ◽

Gene Family ◽

Glutathione S Transferase ◽

Intronless Gene

Download Full-text

EVALUATION OF ENZYMIC AND NON-ENZYMIC ANTIOXIDANT LEVELS IN VERNONIA CINEREA EXTRACTS

Asian Journal of Pharmaceutical and Clinical Research ◽

10.22159/ajpcr.2018.v11i7.22109 ◽

2018 ◽

Vol 11 (7) ◽

pp. 167

Author(s):

Nishadh Abubakker

Keyword(s):

Ethyl Acetate ◽

Fine Powder ◽

Ethanolic Extract ◽

Maximum Activity ◽

Glutathione S Transferase ◽

Reduced Pressure ◽

Methanolic Extracts ◽

Enzymic Antioxidants ◽

Glucose 6 Phosphate Dehydrogenase ◽

Vernonia Cinerea

Objective: The objective of this study was to evaluate the enzymic and non-enzymic antioxidant levels in various solvent extracts of Vernonia cinerea leaves.Methods: The fine powder of leaf (180 g) was extracted successively with methanol, ethanol, petroleum ether (40–60°C), benzene, acetone, ethyl acetate, chloroform, and aqueous in a Soxhlet extractor for 18 h. The extracts were concentrated under reduced pressure at low temperature (40– 50°C), and the extracts were analyzed for the antioxidant enzymes such as catalase (CAT), superoxide dismutase (SOD), peroxidise, glutathione S-transferase (GST), glutathione peroxidase (GPx), polyphenol oxidase, glutathione (GSH) reductase, and glucose-6-phosphate dehydrogenase and non-enzymic antioxidants such as Vitamin A, C, E, reduced GSH, and total phenol.Results: Significant activities of enzymic antioxidants such as CAT (23.68 μ mole of H2O2 decomposed/min/mg protein, SOD (19.75 inhibition of 50% nitrite form/min/mg protein), and GST (73.28 μ mole of 1-chloro-2,4-dinitrobenzene conjugate formed/min) were observed higher in the methanolic extracts. Whereas, ethanolic extract exhibits maximum activity of GPx (1.054 μ mole of GSH utilized/min) and Px (102.1 μ mole of pyrogallol oxidized/ min/mg protein). Total GSH (172.3 μM/g), Vitamin E (23.76 μM/g), and total phenols were significantly predominant in the ethanolic extracts followed by methanol and ethyl acetate extracts.Conclusion: V. cinerea seems to be a promising plant in respect of its antioxidant potential, there is a lot more to be done to understand the mechanisms behind these effects as well as to employ them as possible therapeutic agents.

Download Full-text

Comparative Transcriptome Analysis of Gill Tissue in Response to Hypoxia in Silver Sillago (Sillago sihama)

Animals ◽

10.3390/ani10040628 ◽

2020 ◽

Vol 10 (4) ◽

pp. 628

Author(s):

Wanida Saetan ◽

Changxu Tian ◽

Jiawang Yu ◽

Xinghua Lin ◽

Feixiang He ◽

...

Keyword(s):

Cytochrome P450 ◽

Molecular Mechanisms ◽

Gill Tissue ◽

Gene Families ◽

Glutathione Metabolism ◽

Glutathione S Transferase ◽

Treatment Groups ◽

Hypoxia Stress ◽

Group A ◽

Sillago Sihama

Silver sillago (Sillago sihama) is a commercially important marine fish species in East Asia. In this study, we compared the transcriptome response to hypoxia stress in the gill tissue of S. sihama. The fish were divided into four groups, such as 1 h of hypoxia (hypoxia1h, DO = 1.5 ± 0.1 mg/L), 4 h of hypoxia (hypoxia4h, DO = 1.5 ± 0.1 mg/L), 4 h of reoxygen (reoxygen4h, DO = 8.0 ± 0.2 mg/L) after 4 h of hypoxia (DO = 1.5 mg/L), and normoxia or control (DO = 8.0 ± 0.2 mg/L) groups. Compared to the normoxia group, a total of 3550 genes were identified as differentially expressed genes (DEGs) (log2foldchange > 1 and padj < 0.05), including 1103, 1451 and 996 genes in hypoxia1h, hypoxia4h and reoxygen4h groups, respectively. Only 247 DEGs were differentially co-expressed in all treatment groups. According to Kyoto Encyclopedia of Genes and Genomes (KEGG) pathway analysis, DEGs were significantly enriched in steroid biosynthesis, biosynthesis of amino acids, glutathione metabolism and metabolism of xenobiotics by cytochrome P450, ferroptosis and drug metabolism—cytochrome P450 pathways. Of these, the cytochrome P450 (CYP) and glutathione S-transferase (GST) gene families were widely expressed. Our study represents the insights into the underlying molecular mechanisms of hypoxia stress.

Download Full-text

Effect of diallyldisulphide on an antioxidant enzyme system in Candida species

Canadian Journal of Microbiology ◽

10.1139/w10-066 ◽

2010 ◽

Vol 56 (10) ◽

pp. 816-821 ◽

Cited By ~ 5

Author(s):

Snowber Yousuf ◽

Aijaz Ahmad ◽

Amber Khan ◽

Nikhat Manzoor ◽

Luqman Ahmad Khan

Keyword(s):

Oxidative Stress ◽

Candida Species ◽

Allium Sativum ◽

Enzyme System ◽

Antioxidant Systems ◽

Glutathione S Transferase ◽

Antioxidant Enzyme System ◽

Antioxidant Metabolites ◽

Glucose 6 Phosphate Dehydrogenase ◽

Sublethal Concentrations

This study was carried out to show the effect of diallyldisulphide (DADS), an important organosulphur compound found in garlic ( Allium sativum ), on antioxidant systems in Candida species. Changes in antioxidant metabolites and antioxidant activity in the presence of DADS were found in Candida albicans and Candida tropicalis . Candida cells were treated with sublethal concentrations of DADS. DADS caused a decrease in the activity of all antioxidant enzymes except catalase, resulting in oxidative stress and damaged cells. The amount of oxidative stress generated by DADS was found to be a function of its concentration. A significant decrease in superoxide dismutase, glutathione-S-transferase, and glutathione peroxidase activities but an increase in catalase activity were observed. Increased levels of lipid peroxidation and decreased levels of glutathione were observed in treated cells. Activity of glucose-6-phosphate dehydrogenase decreased significantly following DADS treatment and could be correlated with a decrease in glutathione concentration in both Candida species. These results indicate that diallyl disulphide acts as a pro-oxidant to Candida species and hence may act as a potent antifungal in the management of candidiasis.

Download Full-text