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Article: Evaluation of the correlation between focal adhesion kinase phosphorylation and cell adhesion force using ‘DEP’ technology
Title | Evaluation of the correlation between focal adhesion kinase phosphorylation and cell adhesion force using ‘DEP’ technology |
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Authors | |
Keywords | Cell adhesion force Collagen DEP force Fibronectin Focal adhesion kinase |
Issue Date | 2012 |
Publisher | Molecular Diversity Preservation International. The Journal's web site is located at http://www.mdpi.net/sensors |
Citation | Sensors, 2012, v. 12 n. 5, p. 5951-5965 How to Cite? |
Abstract | Dielectrophoresis (DEP) is the phenomenon in which a particle, such as a living cell, is polarized and moved by electrical gravity in a non-uniform electric field. In the present study, the DEP force is utilized to act on the cells to induce spatial movement for investigating the correlation between the cell adhesion force and activation level of focal adhesion kinase (FAK). The DEP force produced by the non-uniform electric field was used to measure the cell adhesion force of ECV304 cells, on type 1 collagen (COL1)- and fibronectin (FN)-coated polydimethylsiloxane (PDMS) membranes. For COL1-coating, ECV304 cells revealed weak and variable adhesion force (0.343-0.760 nN) in the first eight hours of incubation. Interestingly, the cell adhesion force of ECV304 at two and five hours of cultivation was significantly high and matched their FAK activation level. In comparison, ECV304 on FN-coated membrane had higher and more stable cell adhesion force (0.577-2.053 nN). FN coating intensified the cell adhesion force of ECV304 with culture time and similar outcome was present on the activation level of FAK. Therefore, this study demonstrated a relationship between cell adhesion force and FAK activation level that was dependent on the choice of the extracellular matrix (ECM) component. Subsequently, two tyrosine kinase inhibitors (AG18 and genistein) and one PI3K inhibitor (LY294002) were applied to study the influence of protein phosphorylation on the cell adhesion force. FAK plays an important role on cell attachment and DEP force measurement is a useful technique for studying cell adhesion. |
Persistent Identifier | http://hdl.handle.net/10722/189316 |
ISSN | 2021 Impact Factor: 3.847 2020 SCImago Journal Rankings: 0.636 |
PubMed Central ID | |
ISI Accession Number ID |
DC Field | Value | Language |
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dc.contributor.author | Ay, C | en_US |
dc.contributor.author | Yeh, C-C | en_US |
dc.contributor.author | Hsu, M-C | en_US |
dc.contributor.author | Hurng, H-Y | en_US |
dc.contributor.author | Kwok, PCL | en_US |
dc.contributor.author | Chang, H-I | en_US |
dc.date.accessioned | 2013-09-17T14:35:07Z | - |
dc.date.available | 2013-09-17T14:35:07Z | - |
dc.date.issued | 2012 | en_US |
dc.identifier.citation | Sensors, 2012, v. 12 n. 5, p. 5951-5965 | en_US |
dc.identifier.issn | 1424-8220 | en_US |
dc.identifier.uri | http://hdl.handle.net/10722/189316 | - |
dc.description.abstract | Dielectrophoresis (DEP) is the phenomenon in which a particle, such as a living cell, is polarized and moved by electrical gravity in a non-uniform electric field. In the present study, the DEP force is utilized to act on the cells to induce spatial movement for investigating the correlation between the cell adhesion force and activation level of focal adhesion kinase (FAK). The DEP force produced by the non-uniform electric field was used to measure the cell adhesion force of ECV304 cells, on type 1 collagen (COL1)- and fibronectin (FN)-coated polydimethylsiloxane (PDMS) membranes. For COL1-coating, ECV304 cells revealed weak and variable adhesion force (0.343-0.760 nN) in the first eight hours of incubation. Interestingly, the cell adhesion force of ECV304 at two and five hours of cultivation was significantly high and matched their FAK activation level. In comparison, ECV304 on FN-coated membrane had higher and more stable cell adhesion force (0.577-2.053 nN). FN coating intensified the cell adhesion force of ECV304 with culture time and similar outcome was present on the activation level of FAK. Therefore, this study demonstrated a relationship between cell adhesion force and FAK activation level that was dependent on the choice of the extracellular matrix (ECM) component. Subsequently, two tyrosine kinase inhibitors (AG18 and genistein) and one PI3K inhibitor (LY294002) were applied to study the influence of protein phosphorylation on the cell adhesion force. FAK plays an important role on cell attachment and DEP force measurement is a useful technique for studying cell adhesion. | en_US |
dc.language | eng | en_US |
dc.publisher | Molecular Diversity Preservation International. The Journal's web site is located at http://www.mdpi.net/sensors | en_US |
dc.relation.ispartof | Sensors | en_US |
dc.subject | Cell adhesion force | - |
dc.subject | Collagen | - |
dc.subject | DEP force | - |
dc.subject | Fibronectin | - |
dc.subject | Focal adhesion kinase | - |
dc.subject.mesh | Blotting, Western | en_US |
dc.subject.mesh | Cell Adhesion - drug effects | en_US |
dc.subject.mesh | Electrophoresis | en_US |
dc.subject.mesh | Focal Adhesion Protein-Tyrosine Kinases - antagonists and inhibitors - metabolism | en_US |
dc.subject.mesh | Urinary Bladder - cytology - enzymology | en_US |
dc.title | Evaluation of the correlation between focal adhesion kinase phosphorylation and cell adhesion force using ‘DEP’ technology | en_US |
dc.type | Article | en_US |
dc.identifier.email | Kwok, PCL: pclkwok@hku.hk | en_US |
dc.identifier.authority | Kwok, PCL=rp01540 | en_US |
dc.description.nature | link_to_OA_fulltext | en_US |
dc.identifier.doi | 10.3390/s120505951 | en_US |
dc.identifier.pmid | 22778624 | en_US |
dc.identifier.pmcid | PMC3386723 | en_US |
dc.identifier.scopus | eid_2-s2.0-84861559438 | - |
dc.identifier.hkuros | 222411 | en_US |
dc.identifier.volume | 12 | en_US |
dc.identifier.issue | 5 | en_US |
dc.identifier.spage | 5951 | en_US |
dc.identifier.epage | 5965 | en_US |
dc.identifier.isi | WOS:000304539200045 | - |
dc.publisher.place | Switzerland | en_US |
dc.identifier.issnl | 1424-8220 | - |