4-acetamido-4--isothiocyanatostilbene-2-2--disulfonic-acid has been researched along with diallyl-disulfide* in 2 studies
2 other study(ies) available for 4-acetamido-4--isothiocyanatostilbene-2-2--disulfonic-acid and diallyl-disulfide
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Induce defense response of DADS in eggplants during the biotrophic phase of Verticillium dahliae.
Verticillium wilt is a destructive vascular disease in eggplants. The complex defensive mechanisms of eggplant against this disease are very limited.. Our work examined the bioactive properties of garlic allelochemical diallyl disulfide (DADS) as potential biostimulants for defense against V. dahliae in eggplant seedlings. We, therefore, foliar sprayed DADS on eggplants to study the defense response during the early biotrophic phase of V. dahliae (a hemibiotroph).. DADS application significantly increased root peroxidase (POD), phenylalanine-ammonia lyase (PAL) enzyme activity, and reduced H. Our findings concluded that the biological function of garlic allelochemical DADS has a prominent role in the higher defense resistance of eggplants during the early infection of V. dahliae. Topics: 4-Acetamido-4'-isothiocyanatostilbene-2,2'-disulfonic Acid; Allyl Compounds; Disulfides; Hydrogen Peroxide; Solanum melongena; Verticillium | 2022 |
Glutathione- and thioredoxin-related enzymes are modulated by sulfur-containing chemopreventive agents.
We studied the effects of sulfur-containing chemopreventive agents, including allyl sulfides and isothiocyanates, on human redox networks. Isothiocyanates inhibited isolated redox-active enzymes in a time- and dose-dependent manner. As shown for the most active compound, benzyl isothiocyanate (BITC), on thioredoxin reductase, the inhibition has an initial competitive part (Ki=6.1+/-1.0 microM) followed by a time-dependent irreversible inhibition (k2=72.8+/-25.5 M(-1) s(-1)). Also, glutathione reductase and glutathione S-transferase were irreversibly modified by BITC. Sulforaphane led to irreversible inhibition of the studied redox enzymes, but with 5-10 times lower k2 values. In contrast, allyl sulfides had only moderate effects on the tested enzymes. However, diallyl disulfide was found to react directly with reduced glutathione (k2=100 M(-2) s(-1)). This reaction might contribute to enhanced oxidative stress and the induction of the selenoprotein glutathione peroxidase as determined on activity and transcript levels. All chemopreventive agents tested induced transcript levels of genes associated with cell cycle arrest and apoptosis. This upregulation was accompanied by a dose-dependent decrease in cell number. Our data indicate that modulation of cellular redox networks is likely to contribute to the effects of sulfur-containing chemopreventive agents. Topics: 4-Acetamido-4'-isothiocyanatostilbene-2,2'-disulfonic Acid; Allyl Compounds; Anticarcinogenic Agents; Cell Cycle; Cell Line, Tumor; Cell Proliferation; Disulfides; Dose-Response Relationship, Drug; Glutathione; Glutathione Peroxidase; Glutathione Transferase; Humans; Isothiocyanates; Oxidation-Reduction; Sulfur Compounds; Thioredoxin-Disulfide Reductase; Thioredoxins; Up-Regulation | 2007 |