gyy-4137 and sodium-sulfide

gyy-4137 has been researched along with sodium-sulfide* in 8 studies

Other Studies

8 other study(ies) available for gyy-4137 and sodium-sulfide

ArticleYear
Effect of Hydrogen Sulfide on Essential Functions of Polymorphonuclear Leukocytes.
    Toxins, 2023, 03-04, Volume: 15, Issue:3

    Impaired polymorphonuclear leukocyte (PMNL) functions contribute to increased infections and cardiovascular diseases in chronic kidney disease (CKD). Uremic toxins reduce hydrogen sulfide (H

    Topics: Cysteine; Escherichia coli; Hydrogen Sulfide; Neutrophils; Phosphatidylinositol 3-Kinases

2023
Divergent effect of fast- and slow-releasing H
    Scientific reports, 2020, 04-16, Volume: 10, Issue:1

    Hydrogen sulphide (H

    Topics: Animals; Antioxidants; Humans; Hydrogen Sulfide; Male; Morpholines; Organothiophosphorus Compounds; Oxidative Stress; Sperm Motility; Spermatozoa; Sulfides; Swine

2020
Hydrogen sulfide impacts on inflammation-induced adipocyte dysfunction.
    Food and chemical toxicology : an international journal published for the British Industrial Biological Research Association, 2019, Volume: 131

    A dual role of hydrogen sulfide (H

    Topics: 3T3-L1 Cells; Adipocytes; Adipogenesis; Alkynes; Animals; Cell Differentiation; Gene Expression; Glycine; Hydrogen Sulfide; Inflammation; Mice; Morpholines; Organothiophosphorus Compounds; Sulfides

2019
Parenteral Na
    Acta biochimica Polonica, 2017, Volume: 64, Issue:3

    Hydrogen sulfide (H

    Topics: Animals; Blood Pressure; Buffers; Drug Stability; Half-Life; Hydrogen Sulfide; Hydrogen-Ion Concentration; Infusions, Intravenous; Injections, Intraperitoneal; Male; Morpholines; Organothiophosphorus Compounds; Rats, Wistar; Sulfides

2017
Protein sulfhydration.
    Methods in enzymology, 2015, Volume: 555

    Hydrogen sulfide (H2S) is one of the gasotransmitters that modulates various biological processes and participates in multiple signaling pathways. H2S signals by a process termed sulfhydration. Sulfhydration has recently been recognized as a posttranslational modification similar to nitrosylation. Sulfhydration occurs at reactive cysteine residues in proteins and results in the conversion of an -SH group of cysteine to an -SSH or a persulfide group. Sulfhydration is highly prevalent in vivo, and aberrant sulfhydration patterns have been observed under several pathological conditions ranging from heart disease to neurodegenerative diseases such as Parkinson's disease. The biotin switch assay, originally developed to detect nitrosylation, has been modified to detect sulfhydration. In this chapter, we discuss the physiological roles of sulfhydration and the methodologies used to detect this modification.

    Topics: Biotin; Cell Line; Cysteine; Glyceraldehyde 3-Phosphate Dehydrogenase (NADP+); Humans; Hydrogen Sulfide; Maleimides; Morpholines; Organothiophosphorus Compounds; Oxidation-Reduction; Phenanthrolines; Protein Processing, Post-Translational; Signal Transduction; Staining and Labeling; Streptavidin; Sulfides

2015
Hydrogen sulfide promotes calcium uptake in larval zebrafish.
    American journal of physiology. Cell physiology, 2015, Jul-01, Volume: 309, Issue:1

    Hydrogen sulfide (H2S) can act as a signaling molecule for various ion channels and/or transporters; however, little is known about its potential involvement in Ca(2+) balance. Using developing zebrafish (Danio rerio) as an in vivo model system, the present study demonstrated that acute exposure to H2S donors increased Ca(2+) influx at 4 days postfertilization, while chronic (3-day) exposure caused a rise in whole body Ca(2+) levels. The mRNA expression of Ca(2+)-transport-related genes was unaffected by H2S exposure, suggesting that posttranscriptional modifications were responsible for the altered rates of Ca(2+) uptake. Indeed, treatment of fish with the protein kinase A inhibitor H-89 abolished the H2S-mediated stimulation of Ca(2+) influx, suggesting that H2S increased Ca(2+) influx by activating cAMP-protein kinase A pathways. Cystathionine β-synthase (CBS) and cystathionine γ-lyase (CSE) are two key enzymes in the endogenous synthesis of H2S. Using an antisense morpholino knockdown approach, we demonstrated that Ca(2+) influx was reduced in CBS isoform b (CBSb)- but not in CSE-deficient fish. Interestingly, the reduction in Ca(2+) influx in CBSb-deficient fish was observed only in fish that were acclimated to low-Ca(2+) water (i.e., 25 μM Ca(2+); control: 250 μM Ca(2+)). Similarly, mRNA expression of cbsb but not cse was increased in fish acclimated to low-Ca(2+) water. Results from whole-mount immunohistochemistry further revealed that CBSb was expressed in Na(+)-K(+)-ATPase-rich cells, which are implicated in Ca(2+) uptake in zebrafish larvae. Collectively, the present study suggests a novel role for H2S in promoting Ca(2+) influx, particularly in a low-Ca(2+) environment.

    Topics: Animals; Animals, Genetically Modified; Calcium; Cyclic AMP-Dependent Protein Kinases; Cystathionine beta-Synthase; Gene Knockdown Techniques; Hydrogen Sulfide; Ion Transport; Larva; Morpholines; Morpholinos; Oligonucleotides, Antisense; Organothiophosphorus Compounds; Protein Kinase Inhibitors; Sodium-Potassium-Exchanging ATPase; Sulfides; Time Factors; Zebrafish; Zebrafish Proteins

2015
H2S relaxes isolated human airway smooth muscle cells via the sarcolemmal K(ATP) channel.
    Biochemical and biophysical research communications, 2014, Mar-28, Volume: 446, Issue:1

    Here we explored the impact of hydrogen sulfide (H2S) on biophysical properties of the primary human airway smooth muscle (ASM)-the end effector of acute airway narrowing in asthma. Using magnetic twisting cytometry (MTC), we measured dynamic changes in the stiffness of isolated ASM, at the single-cell level, in response to varying doses of GYY4137 (1-10mM). GYY4137 slowly released appreciable levels of H2S in the range of 10-275 μM, and H2S released was long lived. In isolated human ASM cells, GYY4137 acutely decreased stiffness (i.e. an indicator of the single-cell relaxation) in a dose-dependent fashion, and stiffness decreases were sustained in culture for 24h. Human ASM cells showed protein expressions of cystathionine-γ-lyase (CSE; a H2S synthesizing enzyme) and ATP-sensitive potassium (KATP) channels. The KATP channel opener pinacidil effectively relaxed isolated ASM cells. In addition, pinacidil-induced ASM relaxation was completely inhibited by the treatment of cells with the KATP channel blocker glibenclamide. Glibenclamide also markedly attenuated GYY4137-mediated relaxation of isolated human ASM cells. Taken together, our findings demonstrate that H2S causes the relaxation of human ASM and implicate as well the role for sarcolemmal KATP channels. Finally, given that ASM cells express intrinsic enzymatic machinery of generating H2S, we suggest thereby this class of gasotransmitter can be further exploited for potential therapy against obstructive lung disease.

    Topics: Bronchi; Bronchodilator Agents; Cells, Cultured; Cystathionine gamma-Lyase; Glyburide; Humans; Hydrogen Sulfide; KATP Channels; Morpholines; Muscle Relaxation; Myocytes, Smooth Muscle; Organothiophosphorus Compounds; Pinacidil; Sarcolemma; Sulfides

2014
Polysulfides link H2S to protein thiol oxidation.
    Antioxidants & redox signaling, 2013, Nov-20, Volume: 19, Issue:15

    Hydrogen sulfide (H2S) is suggested to act as a gaseous signaling molecule in a variety of physiological processes. Its molecular mechanism of action was proposed to involve protein S-sulfhydration, that is, conversion of cysteinyl thiolates (Cys-S(-)) to persulfides (Cys-S-S(-)). A central and unresolved question is how H2S-that is, a molecule with sulfur in its lowest possible oxidation state (-2)-can lead to oxidative thiol modifications.. Using the lipid phosphatase PTEN as a model protein, we find that the "H2S donor" sodium hydrosulfide (NaHS) leads to very rapid reversible oxidation of the enzyme in vitro. We identify polysulfides formed in NaHS solutions as the oxidizing species, and present evidence that sulfane sulfur is added to the active site cysteine. Polysulfide-mediated oxidation of PTEN was induced by all "H2S donors" tested, including sodium sulfide (Na2S), gaseous H2S, and morpholin-4-ium 4-methoxyphenyl(morpholino) phosphinodithioate (GYY4137). Moreover, we show that polysulfides formed in H2S solutions readily modify PTEN inside intact cells.. Our results shed light on the previously unresolved question of how H2S leads to protein thiol oxidation, and suggest that polysulfides formed in solutions of H2S mediate this process.. This study suggests that the effects that have been attributed to H2S in previous reports may in fact have been mediated by polysulfides. It also supports the notion that sulfane sulfur rather than sulfide is the actual in vivo agent of H2S signaling.

    Topics: Catalytic Domain; Cell Line; Cysteine; Enzyme Activation; Humans; Hydrogen Sulfide; Kinetics; Morpholines; Organothiophosphorus Compounds; Oxidation-Reduction; Proteins; PTEN Phosphohydrolase; Solutions; Sulfhydryl Compounds; Sulfides

2013