ArticleBiophysical journal1994
Transformation of actin-encapsulating liposomes induced by cytochalasin D.
Article in Biophysical journal, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed.
- Composite branched and linear F-actin maximize myosin-induced membrane shape changes in a biomimetic cell model.Communications biology · 2024Article
- Membrane tension induces F-actin reorganization and flow in a biomimetic model cortex.Communications biology · 2023Article
- Unveiling the physics underlying symmetry breaking of the actin cytoskeleton: An artificial cell-based approach.Biophysics and physicobiology · 2023Article
- Formation of giant liposomes promoted by divalent cations: critical role of electrostatic repulsion.Biophysical journal · 1998Article
- The auxin response of actin is altered in the rice mutant Yin-Yang.Protoplasma · 1998Article
- Preparation of giant liposomes in physiological conditions and their characterization under an optical microscope.Biophysical journal · 1996Article
Corrections and comments
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Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Liposomes encapsulating actin filaments were prepared by swelling at 0 degrees C lipid film consisting of a mixture of dimyristoyl phosphatidylcholine and cardiolipin (equal amounts by weight) in 100 microM rabbit skeletal muscle actin and 0.5 mM CaCl2 followed by polymerization of actin at 30 degrees 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.
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