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- Publisher Website: 10.1098/rsif.2014.0071
- Scopus: eid_2-s2.0-84901475921
- PMID: 24671936
- WOS: WOS:000335639900018
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Article: Single-site sonoporation disrupts actin cytoskeleton organization
Title | Single-site sonoporation disrupts actin cytoskeleton organization |
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Authors | |
Keywords | Actin cytoskeleton Characteristic time F-actin disassembly G-actin accumulation Single-site sonoporation Structure tensor analysis |
Issue Date | 2014 |
Publisher | The Royal Society. The Journal's web site is located at http://publishing.royalsociety.org/index.cfm?page=1572 |
Citation | Journal of the Royal Society. Interface, 2014, v. 11 n. 95, p. article no. 20140071 How to Cite? |
Abstract | Sonoporation is based upon an ultrasound-microbubble cavitation routine that physically punctures the plasma membrane on a transient basis. Over such process, the actin cytoskeleton may be disrupted in tandem since this network of subcellular filaments is physically interconnected with the plasma membrane. Here, by performing confocal fluorescence imaging of single-site sonoporation episodes induced by ultrasound-triggered collapse of a single targeted microbubble, we directly observed immediate rupturing of filamentary actin (F-actin) at the sonoporation site (cell type: ZR-75-30; ultrasound frequency: 1 MHz; peak negative pressure: 0.45 MPa; pulse duration: 30 cycles; bubble diameter: 2-4 m). Also, through conducting a structure tensor analysis, we observed further disassembly of the F-actin network over the next 60 min after the onset of sonoporation. The extent of F-actin disruption was found to be more substantial in cells with higher uptake of sonoporation tracer. Commensurate with this process, cytoplasmic accumulation of globular actin (G-actin) was evident in sonoporated cells, and in turn the G:F-actin ratio was increased in a trend similar to drug-induced (cytochalasin D) actin depolymerization. These results demonstrate that sonoporation is not solely a membrane-level phenomenon: organization of the actin cytoskeleton is concomitantly perturbed. |
Persistent Identifier | http://hdl.handle.net/10722/195913 |
ISSN | 2023 Impact Factor: 3.7 2023 SCImago Journal Rankings: 1.101 |
ISI Accession Number ID |
DC Field | Value | Language |
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dc.contributor.author | Chen, X | en_US |
dc.contributor.author | Leow, RS | en_US |
dc.contributor.author | Hu, Y | en_US |
dc.contributor.author | Wan, JMF | en_US |
dc.contributor.author | Yu, ACH | en_US |
dc.date.accessioned | 2014-03-21T02:19:28Z | - |
dc.date.available | 2014-03-21T02:19:28Z | - |
dc.date.issued | 2014 | - |
dc.identifier.citation | Journal of the Royal Society. Interface, 2014, v. 11 n. 95, p. article no. 20140071 | en_US |
dc.identifier.issn | 1742-5689 | - |
dc.identifier.uri | http://hdl.handle.net/10722/195913 | - |
dc.description.abstract | Sonoporation is based upon an ultrasound-microbubble cavitation routine that physically punctures the plasma membrane on a transient basis. Over such process, the actin cytoskeleton may be disrupted in tandem since this network of subcellular filaments is physically interconnected with the plasma membrane. Here, by performing confocal fluorescence imaging of single-site sonoporation episodes induced by ultrasound-triggered collapse of a single targeted microbubble, we directly observed immediate rupturing of filamentary actin (F-actin) at the sonoporation site (cell type: ZR-75-30; ultrasound frequency: 1 MHz; peak negative pressure: 0.45 MPa; pulse duration: 30 cycles; bubble diameter: 2-4 m). Also, through conducting a structure tensor analysis, we observed further disassembly of the F-actin network over the next 60 min after the onset of sonoporation. The extent of F-actin disruption was found to be more substantial in cells with higher uptake of sonoporation tracer. Commensurate with this process, cytoplasmic accumulation of globular actin (G-actin) was evident in sonoporated cells, and in turn the G:F-actin ratio was increased in a trend similar to drug-induced (cytochalasin D) actin depolymerization. These results demonstrate that sonoporation is not solely a membrane-level phenomenon: organization of the actin cytoskeleton is concomitantly perturbed. | en_US |
dc.language | eng | en_US |
dc.publisher | The Royal Society. The Journal's web site is located at http://publishing.royalsociety.org/index.cfm?page=1572 | - |
dc.relation.ispartof | Journal of the Royal Society. Interface | en_US |
dc.subject | Actin cytoskeleton | - |
dc.subject | Characteristic time | - |
dc.subject | F-actin disassembly | - |
dc.subject | G-actin accumulation | - |
dc.subject | Single-site sonoporation | - |
dc.subject | Structure tensor analysis | - |
dc.title | Single-site sonoporation disrupts actin cytoskeleton organization | en_US |
dc.type | Article | en_US |
dc.identifier.email | Wan, JMF: jmfwan@hku.hk | en_US |
dc.identifier.email | Yu, ACH: alfred.yu@hku.hk | en_US |
dc.identifier.authority | Wan, JMF=rp00798 | en_US |
dc.identifier.authority | Yu, ACH=rp00657 | en_US |
dc.identifier.doi | 10.1098/rsif.2014.0071 | en_US |
dc.identifier.pmid | 24671936 | - |
dc.identifier.scopus | eid_2-s2.0-84901475921 | - |
dc.identifier.hkuros | 228302 | en_US |
dc.identifier.volume | 11 | - |
dc.identifier.issue | 95 | - |
dc.identifier.spage | article no. 20140071 | - |
dc.identifier.epage | article no. 20140071 | - |
dc.identifier.isi | WOS:000335639900018 | - |
dc.publisher.place | United Kingdom | - |
dc.identifier.issnl | 1742-5662 | - |