Lithium preserves F-actin from the disarrangement induced by either DNase I or cytochalasin D.

I. DalleDonne, A. Milzani, U. Fascio, A. Ratti, R. Colombo

Research output: Contribution to journalArticlepeer-review

Abstract

Light scattering at 546 nm, which is mainly related to the presence of rodlike particles longer than 50 nm, showed that Li+ accelerates the formation of actin filaments. Intermolecular cross-linking with N,N'-1,4-phenylene-bismaleimide proved that the observed enhancement in the light-scattering intensity is caused by the increase in the concentration of actin oligomers, which gradually elongate to form longer filaments. DNase-I-related F-actin disassembly was reduced in the presence of lithium ions, as demonstrated by fluorimetric and viscometric experiments. Li(+)-F-actin showed an apparently similar behaviour when exposed to cytochalasin D. We confirm that Li+ acts on actin polymerization by stabilizing actin nuclei and polymers. The stabilization of cytoskeletal polymers really appears as one of the mechanisms by which lithium ions influence some of the cell activities.

Original languageEnglish
Pages (from-to)440-446
Number of pages7
JournalBiochemistry and Cell Biology
Volume71
Issue number9-10
Publication statusPublished - Sept 1993

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)
  • Biochemistry
  • Cell Biology

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