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PMID: 6715359 Published · ppublish English Journal Article Research Support, U.S. Gov't, Non-P.H.S.

Distinctions between mechanisms of cytochalasin D activity for Mg2+- and K+-induced actin assembly.

The Journal of biological chemistry ·Vol. 259 ·No. 9 ·1984-05-10 ·Pages 5549-54

Mozo-Villarías A, Ware BR

Abstract

The fraction of assembled actin and the diffusion coefficients of filamentous and nonfilamentous species have been determined by fluorescence photobleaching recovery. For both Mg2+-induced and K+-induced actin assembly, a higher concentration of cation leads to longer filaments. Cytochalasin D reduces the fraction of actin present as assembled filaments. In the absence of Mg2+, the accompanying increase in diffusion coefficient of the filaments is of an appropriate magnitude to be accounted for by shortening of filaments as a result of net depolymerization. In the presence of Mg2+, cytochalasin D induces a dose-dependent increase in diffusion coefficient up to about a factor of 10. This increase indicates a shortening of filaments consistent with extensive filament cleavage. Under all conditions studied, the unassembled actin is present primarily as monomer.

MeSH Terms
Actins/metabolism Animals Cytochalasin D Cytochalasins/metabolism Kinetics Macromolecular Substances Magnesium/pharmacology Mathematics Muscles/metabolism Potassium/pharmacology Rabbits Rats Spectrometry, Fluorescence
Chemicals
Actins Cytochalasins Macromolecular Substances Cytochalasin D Magnesium Potassium
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Mozo-Villarías A
Ware B R
Article Info
Journal
The Journal of biological chemistry
Abbr.
J Biol Chem
ISSN
0021-9258
Published
1984-05-10
Pages
5549-54
Language
English
Region
United States
NLM ID
2985121R
Subset
IM
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