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Characterization and Localization of Glutathione‐ S ‐Transferases in Rat Brain and Binding of Hormones, Neurotransmitters, and Drugs
Author(s) -
Abramovitz Mark,
Homma Hisato,
Ishigaki Seishi,
Tansey Francine,
Cammer Wendy,
Listowsky Irving
Publication year - 1988
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1988.tb13228.x
Subject(s) - glutathione , astrocyte , cytosol , biochemistry , dopamine , biology , chemistry , endocrinology , enzyme , central nervous system
Rat brain glutathione‐ S ‐transferases are rich in Y b type subunits with major RNA transcripts coding for a relatively uncommon Y b3 form. The Y b ‐containing isoenzymes of brain cytosol bind glucocorticoids and are covalently labeled with dexamethasone 21‐methanesulfonate. Certain neurotransmitters, hormones, and drugs, such as serotonin, dopamine, glucocorticoids, thyroxine, apomorphine, and benzodiazepine derivatives, are effective inhibitors of brain glutathione transferase activity. Immunocytochemical studies show that Y b forms are localized in ependymal cells, subventricular zone cells, astrocytes, tanycytes, and astrocyte foot processes on blood vessels, but Y b was not detected in oligodendrocytes or neurons. Based on their localization and binding properties, brain glutathione‐ S ‐transferases have the potential to function in intracellular binding of a variety of compounds and thereby govern their uptake and release in brain, transport to neurons, as well as in their detoxification.