Allen Institute for Artificial Intelligence
supp.ai logo
supp.ai

Discover Supplement-Drug Interactions

Disclaimer: The information contained herein should NOT be used as a substitute for the advice of an appropriately qualified and licensed physician or other health care provider. The tool is not a substitute for the care provided… (more)
Last Updated: 3 years ago

Possible Interaction: Dihydroxyphenylalanine and Glutathione

Research Papers that Mention the Interaction

Abstract: … with l‐DOPA induced a … in GSH level in cultures of fetal rat mesencephalon, mouse neuroblastoma (Neuro‐2A), human neuroblastoma (SK‐N‐MC), pig kidney epithelial cells (LLC‐PK1), and glia from newborn rat brain, but not C6 glioma cells or neuronal cultures (no glia) from the mesencephalon.
Journal of neurochemistry  •  1996  |  View Paper
In addition, l‐DOPA (200 µm) or/and GCM‐treated cells increased their GSH extracellular levels (223, 257, 300% of controls) after 48 h of treatment.
Journal of neurochemistry  •  2001  |  View Paper
When DOPA and glutathione were added to the medium together, the maturation of melanosomes was promoted.
Journal of submicroscopic cytology and pathology  •  1998  |  View Paper
Iron or copper ions could also promote conjugate formation between GSH or cysteine and DA and l‐DOPA , especially if H2O2 was present.
Journal of neurochemistry  •  1998  |  View Paper
The decrease in cell viability by L‐DOPA (10±4% of control) or dopamine (15±4% of control) was markedly attenuated by antioxidants (ascorbic acid, glutathione , N‐acetyl‐L‐cysteine and sodium metabisulphite).
British journal of pharmacology  •  2002  |  View Paper
The relative quantities of GSH at the sites of DOPA quinone formation and the levels of its metabolising enzymes can influence the type of product formed.(ABSTRACT TRUNCATED AT 250 WORDS)
Journal of dermatological science  •  1991  |  View Paper
It is suggested that GSH may be involved in the steroidogenesis in the inhibition of nonenzymatic decarboxylation of DOPA and in the proteosynthesis in adrenals.
Endocrinologia experimentalis  •  1982  |  View Paper
The Km values of the three isozymes for L‐DOPA ranged from 8.7 to 10 raM. L‐ascorbic acid and β‐mercaptoethanol, glutathione and sodium diethyldithiocarbamate notably inhibited the enzymatic activities.
Biochemistry and molecular biology international  •  1998  |  View Paper