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RECORD NUMBER: 7 OF 17

OLS Field Name OLS Field Data
Main Title Effect of Selected Inhibitors on Cadmium, Nickel, and Benzo(a)pyrene Uptake into Brown Cells of 'Mercenaria mercenaria'.
Author Zaroogian, G. ; Yevich, P. ; Anderson, S. ;
CORP Author Science Applications International Corp., Narragansett, RI.;Environmental Research Lab., Narragansett, RI.
Publisher c1992
Year Published 1992
Report Number EPA-68-C1-0005; EPA/600/J-93/211 ; ERLN-1277
Stock Number PB93-204949
Additional Subjects Benzo(a)pyrene ; Cadmium ; Nickel ; Water pollution effects(Animals) ; Marine biology ; Metabolism ; Cells(Biology) ; Calcium channels ; Copper ; Chloroquine ; N-ethylmaleimide ; Verapamil ; Lysosomes ; Temperature ; Reprints ; Mercenaria mercenaria ; Buthionine sulfoximine ; Maleic acid/diethyl
Holdings
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Status
NTIS  PB93-204949 Most EPA libraries have a fiche copy filed under the call number shown. Check with individual libraries about paper copy. NTIS 11/22/1993
Collation 7p
Abstract
Uptake and inhibition studies were used to evaluate mechanisms of uptake of Ni(2+), Cd(2+), and B(a)P in the brown cells of M. mercenaria. Brown cells contain one or more vesicles that have been shown to be lysosomes. Cd(2+), Ni(2+), and B(a)P accumulation by brown cells was concentration-dependent and independent of time and temperature at 5 C. Metabolic inhibitors such as carbonyl cyanide-m-chlorophenyl hydrazone and NaF did not inhibit their uptake. N-ethylmaleimide facilitated Ni(2+) and Cd(2+) uptake, but inhibited B(a)P uptake. Buthionine-(S,R)-sulfoximine inhibited Ni(2+), Cd(2+), and B(a)P uptake in a dose-dependent manner, and diethylmaleate had no effect on Cd(2+) and B(a)P uptake, but increased Ni(2+) uptake. Chloroquine and copper, which accumulate in lysosomes, inhibited Ni(2+), Cd(2+), and B(a)P uptake. Verapamil inhibited Ni(2+) and B(a)P uptake, whereas it increased Cd uptake. The authors' results suggest that the brown cells of M. mercenaria are capable of accumulation of soluble foreign material and that membrane sulfhydrl groups, glutathione, and Cd(2+) channels are active in these processes. (Copyright (c) 1992 Elsevier Science Publishers Ltd, England.)