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Catecholestrogens are postulated to contribute to carcinogenesis by causing DNA damage mediated by reactive oxygen species generated during redox cycling between catechol and quinone estrogens, and by quinone estrogens that can form depurinating adducts. The above hypothesis is based principally on studies of the cancers that develop in renal cortex of(More)
Electron microscopic observations were made of the microinnervation of the thyroids of normal mice and of mice given false adrenergic neurotransmitters, and the effects of the drugs on thyroidal norepinephrine uptake were measured. In addition to adrenergic nerve terminals on thyroid blood vessels, structures resembling nerve endings were seen in close(More)
The involvement of estrogens in carcinogenic processes within estrogen-responsive tissues has been recognized for a number of years. Classically, mitogenicity associated with estrogen receptor-mediated cellular events was believed to be the mechanism by which estrogens contributed to carci-nogenesis. Recently, the possibility that estrogens might contribute(More)
When cortical slices are incubated with adenine-(14)C, adenine nucleotides are labeled in a small and relatively stable pool. The ATP-(14)C of this pool is readily converted to cAMP-(14)C during incubations with depolarizing agents, such as K(+), ouabain, veratridine, or batrachotoxin. During incubations with these agents, release of acetylcholine and of(More)
Catechol-O-methyltransferase (COMT)(EC 2.1.1.6) was localized using fluorescence immunohistochemistry in rat liver and kidney and in rat, chinchilla, and bovine brains. In the brain, specific fluorescence was visable only in non-neuronal cellular elements in all three species. Ventricular ependymal cells and cells of the choroid plexuses exhibited the(More)
Light microscopic immunocytochemical observations of catechol-O-methyl-transferase (COMT) localization in the pregnant rat uterus were made with a specific antibody to soluble rat liver COMT and the peroxidase-antiperoxidase technique. The changes in cellular localization of COMT were followed from the onset of pregnancy to 12 h after delivery of the last(More)
[3H]Batrachotoxinin A benzoate ( [3H]BTX-B) binds with high affinity to sites on voltage-dependent sodium channels in a vesicular preparation from guinea pig cerebral cortex. In this preparation, local anesthetics competitively antagonize the binding of [3H]BTX-B. The potencies of some 40 classical local anesthetics and a variety of catecholamine,(More)