Transformation of actin-encapsulating liposomes induced by cytochalasin D

H. Miyata*, K. Kinosita

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

18 Citations (Scopus)


Liposomes encapsulating actin filaments were prepared by swelling at 0°C lipid film consisting of a mixture of dimyristoyl phosphatidylcholine and cardiolipin (equal amounts by weight) in 100 μM rabbit skeletal muscle actin and 0.5 mM CaCl2 followed by polymerization of actin at 30°C. Liposomes initially assumed either disk or dumbbell shape, but when cytochalasin D was added to the medium surrounding the liposomes, they were found to become spindle shaped. Liposomes containing bovine serum albumin that were given cytochalasin D and actin-containing liposomes that were given dimethylformamide, the solvent for cytochalasin D, did not transform. These results indicated actin-cytochalasin interaction is involved in the transformation process. Falling-ball viscometry and sedimentation analysis of actin solution indicated that cytochalasin cleaved actin filaments and caused depolymerization. The observation of polarized fluorescence of encapsulated actin labeled with acrylodan indicated that the actin filaments in the transformed liposomes aligned along the long axis of the liposomes. Because the actin filaments in the disk- or dumbbell-shaped liposomes formed bundles running along the liposome contour, the transformation was likely to be accompanied by the change in the actin filament arrangement in the liposomes, which was induced by actin-cytochalasin interaction.

Original languageEnglish
Pages (from-to)922-928
Number of pages7
JournalBiophysical Journal
Issue number2
Publication statusPublished - 1994
Externally publishedYes

ASJC Scopus subject areas

  • Biophysics


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