In spite of the abundant literature, questions on the biological action of Li+ are far from being answered. In the present paper we demonstrate that modification of the salt composition of the medium for actin polymerization, by gradually replacing K+ with Li+, leads to a dose-related change in the time course of actin assembly. The presence of Li+ influences actin polymerization in vitro by enhancing nucleation and decreasing critical monomer concentration at steady state. Furthermore, Li+ stabilizes actin polymers mainly by lowering the absolute value of the dissociation rate constant (K-) and shifting (towards lower values of actin monomer concentrations) the range of G-actin concentrations in which filament-subunit flux can occur. The influence of Li+ on actin and tubulin polymerization in vitro suggests that cytoskeletal structures could be some of the cytoplasmic targets of this ion.

Effects of lithium ions on actin polymerization in the presence of magnesium ions / R. Colombo, A. Milzani, P. Contini, I. Dalle Donne. - In: BIOCHEMICAL JOURNAL. - ISSN 0264-6021. - 274:2(1991), pp. 421-425. [10.1042/bj2740421]

Effects of lithium ions on actin polymerization in the presence of magnesium ions

A. Milzani
Secondo
;
I. Dalle Donne
Ultimo
1991

Abstract

In spite of the abundant literature, questions on the biological action of Li+ are far from being answered. In the present paper we demonstrate that modification of the salt composition of the medium for actin polymerization, by gradually replacing K+ with Li+, leads to a dose-related change in the time course of actin assembly. The presence of Li+ influences actin polymerization in vitro by enhancing nucleation and decreasing critical monomer concentration at steady state. Furthermore, Li+ stabilizes actin polymers mainly by lowering the absolute value of the dissociation rate constant (K-) and shifting (towards lower values of actin monomer concentrations) the range of G-actin concentrations in which filament-subunit flux can occur. The influence of Li+ on actin and tubulin polymerization in vitro suggests that cytoskeletal structures could be some of the cytoplasmic targets of this ion.
rabbit skeletal-muscle; xenopus-laevis; rate constants; cell motility; mechanism; filaments; binding; fragmentation; proteins; monomer
Settore BIO/06 - Anatomia Comparata e Citologia
1991
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/2434/451573
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