Cytoskeletal modifications induced by organotin compounds in human neutrophils

The polymerization of actin, a basic component of the cytoskeleton, was evaluated in human neutrophils after treatment with tributyltin (TBT), trimethyltin (TMT), triphenyltin (TPT), triethyltin (TET) or SnCl2 for 2-30 min at 37°C. TBT and TPT decreased the content of the polymerized form (F-actin) in resting neutrophils at all the times studied; in addition, after TBT and TPT treatment the response of the cells to a polymerizing stimulus (chemotactic peptide) was no longer detectable. These effects were observed under conditions where a cytotoxicity marker such as lactate dehydrogenase leakage remained unaffected. These results may explain the observed inhibition by TBT and TPT of basic cellular functions involving cell shape and motility, which are regulated by the cytoskeleton.