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Main Title Flow Cytometric Comparison of the Effects of Trialkyltins on the Murine Erythroleukemic Cell.
Author Zucker, R. M. ; Elstein, K. H. ; Easterling, R. E. ; Massaro, E. J. ;
CORP Author Health Effects Research Lab., Research Triangle Park, NC. ;NSI Technology Services Corp., Research Triangle Park, NC.
Publisher c1989
Year Published 1989
Report Number EPA/600/J-89/341;
Stock Number PB90-201047
Additional Subjects Cell nucleus ; Graphs(Charts) ; Fluorescence ; Reprints ; Trialkyltin compounds ; Acute erythroblastic leukemia ; Cultured cells ; DNA replication ; Dose-response relationships ; Flow cytometry ; Cell membrane
Library Call Number Additional Info Location Last
NTIS  PB90-201047 Some EPA libraries have a fiche copy filed under the call number shown. 07/26/2022
Collation 15p
Cellular effects of exposure to tributyltin, triethyltin, or trimethyltin were investigated by flow cytometry employing the murine erythroleukemic cell as a model cellular system. Cell viability was investigated by the carboxyfluorescein diacetate (CFDA) uptake/propidium iodide (PI) exclusion method: above a critical concentration (exposure for 4 h), which was specific for each of the trialkyltin compounds, the cell becomes permeable to PI, indicating loss of viability. Cellular CF fluorescence (derived from intracellular hydrolysis of CFDA) increased as a function of alkyltin concentration below the critical concentration and decreased as viability decreased above the critical concentration. Relative membrane potential, monitored with a cyanine dye (DiOC6), correlated with viability (PI exclusion), remaining essentially unaltered below the critical concentration and decreasing above it. Fluorescence and interference microscopy revealed increased quantities of residual cytoplasmic tags adherent to the nuclei as a function of organotin dose, apparently resulting from increased cytoplasmic resistance to detergent-mediated solubilization. The effects of the trialkyltins correlated with their lipophilicity (octanol/water coefficient). These data support the hypothesis that fixation (protein denaturation, cross-linking, etc.) is an important mode of organotin cytotoxicity. (Copyright (c) 1989 Elsevier Scientific Publishers Ireland Ltd.)