Literature DB >> 6893836

Sonic vibration induces the nucleation of actin in the absence of magnesium ions and cytochalasins inhibit the elongation of the nuclei.

K Maruyama.   

Abstract

Polymerization of actin was completely inhibited by metal chelating agents, such as EDTA or diaminocyclohexanetetraacetic acid, even in the presence of 0.1 M KCl and excess ATP. Addition of 1 mM MgCl2, but not CaCl2, caused full polymerization in the presence of 10 mM diaminocyclohexanetetraacetic acid, suggesting that micromolar concentrations of Mg ions are required for the polymerization of actin. However, it turned out that sonic vibration induced a very rapid polymerization of actin in the absence of Mg ions. The sonication-induced polymerization of actin was greatly inhibited by cytochalasins D and B, and partially by beta-actinin. This can be explained by assuming that the fast growing ends of the formed nuclei are blocked by the cytochalasins, and the slowly growing ends with beta-actinin. The elongation of added F-actin fragments was also similarly inhibited by the cytochalasins and beta-actinin in the absence of Mg ions. It appears that sonic vibration enhances nuclei formation of actin monomers by mechanical agitation in the absence of Mg ions, which stabilize formed nuclei.

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Year:  1981        PMID: 6893836

Source DB:  PubMed          Journal:  J Biol Chem        ISSN: 0021-9258            Impact factor:   5.157


  4 in total

1.  An alternative pathway of actin filament elongation. The condensation of small oligomers.

Authors:  E Grazi
Journal:  J Muscle Res Cell Motil       Date:  1989-08       Impact factor: 2.698

2.  Characterization of the ATP-G-actin aggregates formed at low potassium chloride concentration.

Authors:  E Grazi; A Aleotti; A Ferri
Journal:  Biochem J       Date:  1984-04-01       Impact factor: 3.857

3.  54Mn2+ as a tracer of the polymerization of actin. Intermediate oligomers condense to give F-actin.

Authors:  E Grazi
Journal:  Biochem J       Date:  1984-11-01       Impact factor: 3.857

4.  An actin-depolymerizing protein (depactin) from starfish oocytes: properties and interaction with actin.

Authors:  I Mabuchi
Journal:  J Cell Biol       Date:  1983-11       Impact factor: 10.539

  4 in total

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