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PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
1990-11-2
pubmed:abstractText
Flow cytometric and light/fluorescence microscopic analysis of murine erythroleukemic cells (MELC) and electron microscopic investigation of porcine microsomal membrane preparations suggest that tributyltin (TBT) toxicity is mediated through fixation processes (protein denaturation, crosslinking, and so on) within the plasma membrane/cytoplasm complex. This hypothesis was derived from the following observations: 1. Exposure of the MELC to micromolar concentrations of TBT results in increased resistance to detergent-mediated cytolysis; 2. Exposure of porcine renal microsomal membrane preparations to similar concentrations results in inhibition of vanadate-mediated crystallization of Na+,K(+)-ATPase, a process requiring protein mobility within the membrane; 3. Flow cytometric and fluorescence microscopic analyses indicate that MELC exposed to submicromolar concentrations of TBT exhibit increased cellular carboxyfluorescein retention; and 4. Nuclei prepared from TBT-treated cells by detergent-mediated cytolysis exhibit increased axial light loss, 90 degrees light scatter, fluorescein isothiocyanate fluorescence, and the presence of adherent proteinaceous tags. The DNA distribution histogram of such nuclei also is perturbed.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0163-4984
pubmed:author
pubmed:issnType
Print
pubmed:volume
21
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
305-12
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed:articleTitle
Fixation of the plasma membrane/cytoplasm complex: a mechanism of toxic interaction of tributyltin with the cell.
pubmed:affiliation
Developmental and Cell Toxicology Division, US Environmental Protection Agency, Research Triangle Park, NC 27711.
pubmed:publicationType
Journal Article