F-actin levels but not actin polymerization are affected by triphenyltin in HL-60 cells

Marina Marinovich, Marina Guizzetti, Enrico Grazi, Giorgio Trombetta, Corrado Lodovico Galli

Research output: Contribution to journalArticlepeer-review

3 Scopus citations


The toxin triphenyl tin (TPT), Sn(C6H5)3+ caused a rapid decrease in the F-actin content of promyelocytic human leukemia cells (HL-60) chemically differentiated to neutrophils. Prior incubation (2 min) of the cells with 10 μM TPT did not modify the extent of actin polymerization inducible either by a receptor-mediated stimulus (chemotactic peptide fMLP) or by a direct activator of G proteins (AIF4-). The inorganic tin salts SnCl4, and SnCl4 did not affect F-actin content or production of HL-60 cells. Microfilament thiol groups were not reduced by exposure of cells to TPT, but even increased. When F-actin was exposed to 10 μM triphenyltin in a cell-free system, the depolymerizing effect was not detectable. Thus, TPT does not affect cytoskeletal protein directly but depends for its toxicity on some other induced change, probably ionic/osmotic in the intact cell.

Original languageEnglish (US)
Pages (from-to)13-20
Number of pages8
JournalEnvironmental Toxicology and Pharmacology
Issue number1
StatePublished - Feb 15 1996
Externally publishedYes


  • F-actin
  • HL-60 cell
  • Triphenyltin

ASJC Scopus subject areas

  • Toxicology
  • Pharmacology
  • Health, Toxicology and Mutagenesis


Dive into the research topics of 'F-actin levels but not actin polymerization are affected by triphenyltin in HL-60 cells'. Together they form a unique fingerprint.

Cite this