Lithium preserves F-actin from the disarrangement induced by either DNase I or cytochalasin D.
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.
DalleDonne
I
I
University of Milan, Department of Biology, Italy.
Milzani
A
A
Fascio
U
U
Ratti
A
A
Colombo
R
R
D000199:Actins / Q000737:chemistry* / Q000378:metabolism; D000818:Animals; D003432:Cross-Linking Reagents; D015638:Cytochalasin D / Q000494:pharmacology*; D003850:Deoxyribonuclease I / Q000494:pharmacology*; D004591:Electrophoresis, Polyacrylamide Gel; D007700:Kinetics; D008027:Light; D008094:Lithium / Q000494:pharmacology*; D018021:Lithium Chloride / Q000494:pharmacology; D046911:Macromolecular Substances; D015636:Magnesium Chloride / Q000494:pharmacology; D008970:Molecular Weight; D011189:Potassium Chloride / Q000494:pharmacology; D011817:Rabbits; D012542:Scattering, Radiation; D013050:Spectrometry, Fluorescence; D014783:Viscosity
D000199:Actins; D003432:Cross-Linking Reagents; D046911:Macromolecular Substances; D015636:Magnesium Chloride; D015638:Cytochalasin D; D011189:Potassium Chloride; D008094:Lithium; D003850:Deoxyribonuclease I; D018021:Lithium Chloride