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Last Updated: 3 years ago

Possible Interaction: Antioxidants and Buthionine Sulfoximine

Research Papers that Mention the Interaction

The activity of CPCD in HL-60 and K562 cells was modulated by glutathione (GSH), since depletion of this intracellular thiol-based antioxidant with buthionine sulfoximine resulted in significantly ( p < 0.05) greater potency in antiproliferation assays.
Journal of natural products  •  2018  |  View Paper
Exposure of HaCaT cells with BSO leads to altered expression of antioxidant genes and proteins, i.e., thioredoxin reductase (TrxR) and peroxiredoxin 6 (Prx6) whereas, in our study, pretreatment of PEGylated CeNPs reduces the need for induction of genes that produce enzymes involved in the defense against oxidative stress.
Langmuir : the ACS journal of surfaces and colloids  •  2016  |  View Paper
The antioxidant system can partially compensate the damage induced by BSO plus 1,25(OH)2D3.
Anti-cancer drugs  •  2014  |  View Paper
The cell’s antioxidant defences can be compromised by, for example, inhibiting catalas0 activity by 3-aminotriazole or depleting glutathione levels using buthionine sulphoximine.
Biochemical Society transactions  •  1997  |  View Paper
Also, BSO treatment increased the activity of phase II antioxidant enzyme, NAD(P)H: quinone oxidoreductase-1 (NQO-1).
Clinical and experimental hypertension  •  2020  |  View Paper
As these changes may depend on the oxidative status, we administrated buthionine sulfoximine (BSO) to decrease the antioxidant capacity of some birds.
Molecular ecology  •  2019  |  View Paper
BSO exposure resulted in several detrimental effects, decreasing glutamate-cysteine ligase (GCL) activity, cystine uptake, GSH intracellular content and the activities of the antioxidant enzymes glutathione peroxidase (GPx) and glutathione reductase (GR).
Molecular and Cellular Biochemistry  •  2016  |  View Paper
Results: Inhibition of GSH production by BSO enhanced CD36 translational efficiency to induce CD36 protein expression and lipid accumulation that was blocked by antioxidant (enzyme).
The Journal of Biological Chemistry  •  2015  |  View Paper
Antioxidants such as trolox or N-acetyl cysteine prevented this synergistic toxicity of SAMe plus AA or SAMe plus BSO , respectively.
American journal of physiology. Gastrointestinal and liver physiology  •  2006  |  View Paper
The translocation of PKC-epsilon by BSO was blocked by antioxidant trolox , suggesting the PKC-epsilon as a downstream of reactive oxygen species (ROS) elevated by BSO.
Biochemical and biophysical research communications  •  2004  |  View Paper
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