Relevant bibliographies by topics / Glutathione oxidized molecule

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Academic literature on the topic 'Glutathione oxidized molecule'

Author: Grafiati
Published: 6 September 2023

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Journal articles on the topic "Glutathione oxidized molecule"

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Tu, Benjamin P., and Jonathan S. Weissman. "Oxidative protein folding in eukaryotes." Journal of Cell Biology 164, no. 3 (February 2, 2004): 341–46. http://dx.doi.org/10.1083/jcb.200311055.

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The endoplasmic reticulum (ER) provides an environment that is highly optimized for oxidative protein folding. Rather than relying on small molecule oxidants like glutathione, it is now clear that disulfide formation is driven by a protein relay involving Ero1, a novel conserved FAD-dependent enzyme, and protein disulfide isomerase (PDI); Ero1 is oxidized by molecular oxygen and in turn acts as a specific oxidant of PDI, which then directly oxidizes disulfide bonds in folding proteins. While providing a robust driving force for disulfide formation, the use of molecular oxygen as the terminal electron acceptor can lead to oxidative stress through the production of reactive oxygen species and oxidized glutathione. How Ero1p distinguishes between the many different PDI-related proteins and how the cell minimizes the effects of oxidative damage from Ero1 remain important open questions.
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Darley-Usmar, V. M., A. Severn, V. J. O'Leary, and M. Rogers. "Treatment of macrophages with oxidized low-density lipoprotein increases their intracellular glutathione content." Biochemical Journal 278, no. 2 (September 1, 1991): 429–34. http://dx.doi.org/10.1042/bj2780429.

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Macrophages derived from the human monocyte cell line THP-1 or isolated from the peritoneum of C3H/HEJ mice were incubated with oxidized low-density lipoprotein (LDL) and the total glutathione content (oxidized plus reduced) was measured. An initial depletion of glutathione was followed by an increase, such that after a period of 24 h the glutathione content has approximately doubled. This response required the oxidation of the lipid phase of the LDL molecule, since both native LDL and acetylated LDL had little effect on glutathione levels. The response of the cells to oxidized LDL was dependent on the extent of oxidative modification of the protein. It was also found that 4-hydroxynonenal had a similar effect on THP-1 cells, and we suggest that this or other aldehydes present in oxidized LDL causes the induction of glutathione synthesis in response to an initial oxidative stress and consequent glutathione depletion. In addition, we found that both cell types possess transferases and peroxidases capable of detoxifying aldehydes and peroxides. However, treatment of cells with oxidized LDL or 4-hydroxynonenal for a period of 24 h had no effect on the activities of these enzymes.
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Iskusnykh, Igor Y., Anastasia A. Zakharova, and Dhruba Pathak. "Glutathione in Brain Disorders and Aging." Molecules 27, no. 1 (January 5, 2022): 324. http://dx.doi.org/10.3390/molecules27010324.

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Glutathione is a remarkably functional molecule with diverse features, which include being an antioxidant, a regulator of DNA synthesis and repair, a protector of thiol groups in proteins, a stabilizer of cell membranes, and a detoxifier of xenobiotics. Glutathione exists in two states—oxidized and reduced. Under normal physiological conditions of cellular homeostasis, glutathione remains primarily in its reduced form. However, many metabolic pathways involve oxidization of glutathione, resulting in an imbalance in cellular homeostasis. Impairment of glutathione function in the brain is linked to loss of neurons during the aging process or as the result of neurological diseases such as Huntington’s disease, Parkinson’s disease, stroke, and Alzheimer’s disease. The exact mechanisms through which glutathione regulates brain metabolism are not well understood. In this review, we will highlight the common signaling cascades that regulate glutathione in neurons and glia, its functions as a neuronal regulator in homeostasis and metabolism, and finally a mechanistic recapitulation of glutathione signaling. Together, these will put glutathione’s role in normal aging and neurological disorders development into perspective.
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Yang, Wei-Yu, Jueting Zheng, Xia-Guang Zhang, Li-Chuan Chen, Yu Si, Fei-Zhou Huang, and Wenjing Hong. "Charge transport through a water-assisted hydrogen bond in single-molecule glutathione disulfide junctions." Journal of Materials Chemistry C 8, no. 2 (2020): 481–86. http://dx.doi.org/10.1039/c9tc05686f.

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Wei, Yongfeng, Zhuoqun Su, Xiao-feng Kang, Yanli Guo, and Xiaoxue Mu. "Single-molecule transformation and analysis of glutathione oxidized and reduced in nanopore." Talanta 167 (May 2017): 526–31. http://dx.doi.org/10.1016/j.talanta.2017.02.059.

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Wróblewska, Joanna, Marcin Wróblewski, Iga Hołyńska-Iwan, Martyna Modrzejewska, Jarosław Nuszkiewicz, Weronika Wróblewska, and Alina Woźniak. "The Role of Glutathione in Selected Viral Diseases." Antioxidants 12, no. 7 (June 22, 2023): 1325. http://dx.doi.org/10.3390/antiox12071325.

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During inflammatory processes, immunocompetent cells are exposed to substantial amounts of free radicals and toxic compounds. Glutathione is a cysteine-containing tripeptide that is an important and ubiquitous antioxidant molecule produced in human organs. The intracellular content of GSH regulates the detoxifying capacity of cells, as well as the inflammatory and immune response. GSH is particularly important in the liver, where it serves as the major non-protein thiol involved in cellular antioxidant defense. There are numerous causes of hepatitis. The inflammation of the liver can be caused by a variety of infectious viruses. The relationship between oxidative stress and the hepatitis A virus (HAV), hepatitis B virus (HBV), hepatitis C virus (HCV), and hepatitis E virus (HEV) infection is not fully known. The aim of this study was to examine the relationship between hepatotropic viruses and glutathione status, including reduced glutathione (GSH) and oxidized glutathione (GSSG), as well as antioxidant enzymes, e.g., glutathione peroxidase (GPx), glutathione reductase (GR) and glutathione-S-transferase (GST) in liver diseases.
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Ivanov, V. V., Ye V. Shakhristova, Ye A. Stepovaya, and V. V. Novitsky. "Effect of alloxan on glutathione system and oxidative protein modification in adipocytes of rats at experimental diabetes." Bulletin of Siberian Medicine 10, no. 3 (June 28, 2011): 44–47. http://dx.doi.org/10.20538/1682-0363-2011-3-44-47.

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There was carried out a research of the development of oxidative stress, the condition of glutathione dependant system of antioxidant protection in adipocytes of epididymal adipose tissue of rats when injecting alloxan. The development of oxidative stress in adipocytes was characterized by the increase of lipids hydroperoxide concentration, products reacting with thiobarbituric acid, and the increase of carbonylderived protein. Redox-condition in adipocytes was considerably changing that was specified by the decrease of the content of the reduced form of glutathione and tendency to the increase of glutathione disulfide content, decrease of ratio between reduced and oxidized forms of threepeptide. Damage of protein molecule at oxidative stress may lead to the abnormality of transduction of insulinic signal and appearance of insulin resistance in adipose tissue.
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Ewald, S. J., and P. H. Refling. "Co-immunoprecipitation of the Ly-5 molecule and an endogenous protease: a proteolytic system requiring a reducing agent and Ca2+1." Journal of Immunology 134, no. 4 (April 1, 1985): 2513–19. http://dx.doi.org/10.4049/jimmunol.134.4.2513.

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Abstract Sodium [3H]borohydride- and [35S]methionine-labeled Ly-5 molecules from mouse thymocytes and T lymphoma cells were isolated with specific antibody and Staphylococcus aureus Cowan I (SaCI) strain; after extensive washing of the complexes, elution with Laemmli's reducing buffer (0.05 M Tris [pH 6.8 or 6.0], 4% sodium dodecyl sulfate [SDS], and 2% 2-mercaptoethanol [2-ME]) resulted in partial breakdown of the isolated Ly-5 molecules from a Mr = 175,000 to 150,000. Other proteins present during the elution step showed no evidence of proteolysis. 2-ME and SDS were required for proteolysis; although addition of exogenous Ca2+ during elution was not necessary, both EDTA and EGTA inhibited breakdown of the molecule that could be overcome by excess Ca2+. Of a variety of protease inhibitors and thiol-reactive agents tested, only TAME and oxidized glutathione blocked proteolysis almost completely. SaCI, serum, and contaminating antibodies were ruled out as the source of the proteolytic activity. More stringent preclearing and washing conditions did not eliminate endogenous proteolysis of the Ly-5 molecule. The endogenous proteolytic fragment had a Mr distinct from the tryptic fragment of the Ly-5 molecule. We conclude that the Ly-5 molecule may be autolytic or tightly associated with a distinct cellular protease.
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Morgan, Bruce. "Reassessing cellular glutathione homoeostasis: novel insights revealed by genetically encoded redox probes." Biochemical Society Transactions 42, no. 4 (August 1, 2014): 979–84. http://dx.doi.org/10.1042/bst20140101.

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Glutathione is the most abundant small molecule thiol in nearly all eukaryotes. Whole-cell levels of oxidized (GSSG) and reduced (GSH) glutathione are variable and responsive to genetic and chemical manipulations, which has led to their relative levels being widely used as a marker of the ‘cellular redox state’ and to indicate the level of ‘oxidative stress’ experienced by cells, tissues and organisms. However, the applicability of glutathione as a marker for a generalized ‘cellular redox state’ is questionable, especially in the light of recent observations in yeast cells. In yeast, whole-cell GSSG changes are almost completely dependent upon the activity of an ABC-C (ATP-binding cassette-C) transporter, Ycf1 (yeast cadmium factor 1), which mediates sequestration of GSSG to the vacuole. In the absence of Ycf1 whole-cell GSSG content is strongly decreased and extremely robust to perturbation. These observations are consistent with highly specific redox-sensitive GFP probe-based measurements of the cytosolic glutathione pool and indicate that cytosolic GSSG reductive systems are easily able to reduce nearly all GSSG formed, even following treatment with large concentrations of oxidant. In the present paper, I discuss the consequences of these new findings for our understanding of glutathione homoeostasis in the eukaryotic cell.
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Abdillah, Ariq, Prasad M. Sonawane, Donghyeon Kim, Dooronbek Mametov, Shingo Shimodaira, Yunseon Park, and David G. Churchill. "Discussions of Fluorescence in Selenium Chemistry: Recently Reported Probes, Particles, and a Clearer Biological Knowledge." Molecules 26, no. 3 (January 28, 2021): 692. http://dx.doi.org/10.3390/molecules26030692.

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In this review from literature appearing over about the past 5 years, we focus on selected selenide reports and related chemistry; we aimed for a digestible, relevant, review intended to be usefully interconnected within the realm of fluorescence and selenium chemistry. Tellurium is mentioned where relevant. Topics include selenium in physics and surfaces, nanoscience, sensing and fluorescence, quantum dots and nanoparticles, Au and oxide nanoparticles quantum dot based, coatings and catalyst poisons, thin film, and aspects of solar energy conversion. Chemosensing is covered, whether small molecule or nanoparticle based, relating to metal ion analytes, H2S, as well as analyte sulfane (biothiols—including glutathione). We cover recent reports of probing and fluorescence when they deal with redox biology aspects. Selenium in therapeutics, medicinal chemistry and skeleton cores is covered. Selenium serves as a constituent for some small molecule sensors and probes. Typically, the selenium is part of the reactive, or active site of the probe; in other cases, it is featured as the analyte, either as a reduced or oxidized form of selenium. Free radicals and ROS are also mentioned; aggregation strategies are treated in some places. Also, the relationship between reduced selenium and oxidized selenium is developed.
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Dissertations / Theses on the topic "Glutathione oxidized molecule"

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Senapati, Dillip Kumar. "Study of Structure and Dynamics of Bioactive Natural and Synthetic Peptides by NMR Spectroscopy and In silico Methods." Thesis, 2021. https://etd.iisc.ac.in/handle/2005/5173.

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The thesis covers conformational analysis of several bioactive peptides using solution and solid-state NMR along with in silico analysis of some of them compiled in five chapters. It starts with an introduction to solution and solid-state NMR along with basics of peptides/ proteins and in silico methods in chapter 1. Chapter 2 covers work carried out on conformational analysis of Glutathione oxidized (GSSG) molecule investigated through solution NMR which suggests an antiparallel structure with different hydrogen bonding pattern and includes a comparison of the results obtained earlier in the solid-state NMR. In addition, influence of pH alterations on GSSG conformation is also reported which indicate GSSG to sample a broad range of conformational space depending on its surrounding environment. Chapter 3 discusses the structure elucidation of the missing central part of AICD (Amyloid precursor protein Intra Cellular Domain) 12 residue fragment along with in silico analysis of the whole stretch incorporating the newly determined central stretch. It also covers metal and polyphenol interactions with the AICD16-27 peptide indicating Histidines to be more prone for interaction. Chapter 4 deals with conformational analysis of Selenocysteine peptides where Selenium replaces the Sulphur atom in the amino acid Cysteine. An analysis based on 1- and 2-dimensional solid-state NMR spectra have been made suggesting multiple conformations in a unit cell and complementary DFT calculations are also given. Finally in chapter 5, N-terminal A-beta fragments structure comparison is carried out as fragment size increases along with metal and polyphenol interactions which indicate involvement of aromatic and charge residues. Hence it is useful to understand the aggregation effects leading to fibril formation in Alzheimer’s disease. Overall, the studies aim at understanding bioactive peptide conformations which may help in drug discovery for prevention of various diseases.
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Book chapters on the topic "Glutathione oxidized molecule"

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Owen, Joshua B., and D. Allan Butterfield. "Measurement of Oxidized/Reduced Glutathione Ratio." In Methods in Molecular Biology, 269–77. Totowa, NJ: Humana Press, 2010. http://dx.doi.org/10.1007/978-1-60761-756-3_18.

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Mathews, Thomas P. "Quantitation of Glutathione and Oxidized Glutathione Ratios from Biological Matrices Using LC-MS/MS." In Methods in Molecular Biology, 133–48. New York, NY: Springer US, 2023. http://dx.doi.org/10.1007/978-1-0716-3247-5_11.

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Jablonkai, Istvan. "Molecular Defense Mechanisms in Plants to Tolerate Toxic Action of Heavy Metal Environmental Pollution." In Plant Defense Mechanisms [Working Title]. IntechOpen, 2022. http://dx.doi.org/10.5772/intechopen.102330.

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Toxic action of heavy metals on plants growing in contaminated soils intensified the research on detoxification and sequestering mechanisms existing in plants to understand and manipulate defense mechanisms that confer tolerance against metal ions. Increased biosynthesis of plant biomolecules to confer tolerance during toxic action of heavy metals is an intrinsic ability of plants. Induced formation of low-molecular weight amino acids, peptides or proteines as chelators such as proline (Pro), glutathione (GSH), phytochelatins (PCs) or metallothioneins (MTs) under heavy metal stress enhances metal binding and detoxification capability of plants. In addition, proline and GSH related enzymes such as GSH reductase, GSH peroxidases and glutathione S-transferases are also key components of the antioxidant defense system in the cells to scavenge reactive oxygen species (ROS). Protective action of oxidized fatty acids oxylipins at toxic levels of heavy metals is considered to activate detoxification processes as signaling molecules.
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Akkaya Fırat, Asuman. "Ferroptosis: Can Iron be the Last or Cure for a Cell?" In Iron Metabolism - Iron a Double‐Edged Sword [Working Title]. IntechOpen, 2021. http://dx.doi.org/10.5772/intechopen.101426.

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Ferroptosis is one of the forms of programmed cell death. Besides being a necessary micronutrient, iron is the key element that initiates ferroptosis in the cell. Intracellular unstable iron accumulation increases the amount of intracellular ROS, especially by the peroxidation of unsaturated membrane phospholipids. Insufficient antioxidant capacity and decreased glutathione levels play an important role in this process. The research reveals that an imbalance between unoxidized polyunsaturated fatty acids (PUFAs) and oxidized PUFAs, particularly oxidized arachidonic acid, accelerates ferroptosis. These oxidative reactions change the permeability of lysosomal and cellular membranes and cell death occurs. Iron chelators, lipophilic antioxidants, and specific inhibitors prevent ferroptosis. In addition to being accepted as a physiological process, it seems to be associated with tissue reperfusion damage, ischemic, neurodegenerative diseases, hematological and nephrological disorders. Ferroptosis is also being explored as a treatment option where it may offer a treatment option for some types of cancer. In this section, the brief history of ferroptosis, its morphological, molecular, and pathophysiological features are mentioned. Ferroptosis seems to be a rich field of research as a treatment option for many diseases in the future.
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Conference papers on the topic "Glutathione oxidized molecule"

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Jamaluddin, Moideen P., C. Sreedevi, Ancy Thomas, and Lissy K. Krishnan. "A MOLECULAR MECHANISM FOR THE DITHI0THREIT0L-MEDIAT5D PLATELET AGGREGATION." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644495.

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Biochemical mechanisms of stimulus response coupling is an intricate problem in platelet biochemistry. Recently we obtained evidence that support the view that conformational changes of an (unsaturated fatty acid – and U46619-binding) haemoprotein induced by the binding of arachidonic acid, H2O2 or PGH2 liberated in apparently different platelet compartments in response to different stimuli could constitute a mechanism (L.K. Krishnan … M.P. Jamaluddin, FEBS Lett, in the press). We investigated the effect of dithiothreitol (DTT), a platelet agonist whose mechanism of action is unknown, on the purified haemoprotein. DTT was found by spectral measurements and gelfiltration experiments to bring about a slow time-dependent conformational .change and oligomerization of the protein concomitantly with its oxidation. Oxidised DTT (trans-4,5-dihy-droxy-1,2-dithiane) was found to induce a similar conformational change by binding to the protein (halfsaturation cancn. 2 mM). Oligomerization changed the charge characteristics of the protein, from net positive to net negative, ait pH 7.4. Protein-protein association is associated with large volume increases. Excluded volume effects and changes in charge distribution at the side of protein conformational change could trigger actin polymerization, pseudopod formation and aggregation, modulated by protein phosphorylation and Ca2+ concentration. In conformity with these ideas oxidized DTT near its half-maximal saturation concentration for the protein, was found to aggregate gelfiltered calf platelets. Presumably it functions as a thioanalogue of PGH2. Oxidized glutathione or oxidized 2-mercaptoethanol could also bring about protein conformational change and platelet aggregation.
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Ismail, Rabah Mahmoud Ahmad, Edith Ajiroghene Enemose, Marwa Al-Jamal, Sathish Kumar Ramachandran, Hashem Al-Mattarneh, and Durgaprasad Gangodkar. "Co-MoF Derived Colorimetric Sensors for Detection of Environmental Toxic Heavy Metal Analysis." In International Conference on Recent Advancements in Biomedical Engineering. Switzerland: Trans Tech Publications Ltd, 2022. http://dx.doi.org/10.4028/p-6pqbv5.

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The Co-MoF was identified as better catalyst for colorimetric sensing for effective detection of Hg2+ ions. The mimicking activities and oxidise the TMB in the existence of hydrogen peroxide (H2O2) to create a blue-colored sample. The oxidation of TMB was greatly delayed or reduced in the existence of bio-molecule Glutathione since of its stronger cations to repair capability. GSH substrates are oxidised when Hg2+ is introduced because of the higher interaction of mercury ions for GSH's thiol groups. Hg2+ concentrations ranged from 1 to 50 nM, and it exhibits a LOD of 0.28 nM reached in this study. To our surprise, the proposed sensor technology for detecting mercury contamination from industrial wastewater shows great potential.
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