Collective cell migration on artificial extracellular matrix proteins containing full-length fibronectin domains
The discovery of the cell-adhesive properties of the Arg-Gly-Asp (RGD) sequence located in the tenth type III domain of fi bronectin triggered widespread use of RGD-functionalized materials for directing cell behavior. [ 1,2 ] In studies of cell adhesion and migration, however, cell responses on...
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sg-ntu-dr.10356-852622023-07-14T15:45:31Z Collective cell migration on artificial extracellular matrix proteins containing full-length fibronectin domains Fong, Eileen. Tirrell, David A. School of Materials Science & Engineering DRNTU::Engineering::Materials::Biomaterials The discovery of the cell-adhesive properties of the Arg-Gly-Asp (RGD) sequence located in the tenth type III domain of fi bronectin triggered widespread use of RGD-functionalized materials for directing cell behavior. [ 1,2 ] In studies of cell adhesion and migration, however, cell responses on RGD surfaces are never identical to those observed on fi bronectin. [ 3 ] For example, we recently examined the attachment and patterning of Rat-1 fi broblasts on elastin-based artifi cial extracellular matrix (aECM) proteins bearing a fi bronectin-derived RGD sequence and found the average projected area of such cells to be approximately 60% of those spread on fi bronectin. Accepted version 2011-07-29T01:27:42Z 2019-12-06T16:00:34Z 2011-07-29T01:27:42Z 2019-12-06T16:00:34Z 2010 2010 Journal Article Fong, E., & Tirrell, D. A. (2010). Collective Cell Migration on Artificial Extracellular Matrix Proteins Containing Full-Length Fibronectin Domains. Advanced Materials, 22, 5271-5275. https://hdl.handle.net/10356/85262 http://hdl.handle.net/10220/6946 10.1002/adma.201002448 20886461 156327 en Advanced materials © 2010 Wiley-VCH Verlag. application/pdf |
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DRNTU::Engineering::Materials::Biomaterials Fong, Eileen. Tirrell, David A. Collective cell migration on artificial extracellular matrix proteins containing full-length fibronectin domains |
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The discovery of the cell-adhesive properties of the Arg-Gly-Asp
(RGD) sequence located in the tenth type III domain of
fi bronectin triggered widespread use of RGD-functionalized
materials for directing cell behavior. [ 1,2 ] In studies of cell adhesion
and migration, however, cell responses on RGD surfaces
are never identical to those observed on fi bronectin. [ 3 ] For
example, we recently examined the attachment and patterning
of Rat-1 fi broblasts on elastin-based artifi cial extracellular matrix
(aECM) proteins bearing a fi bronectin-derived RGD sequence
and found the average projected area of such cells to be approximately
60% of those spread on fi bronectin. |
author2 |
School of Materials Science & Engineering |
author_facet |
School of Materials Science & Engineering Fong, Eileen. Tirrell, David A. |
format |
Article |
author |
Fong, Eileen. Tirrell, David A. |
author_sort |
Fong, Eileen. |
title |
Collective cell migration on artificial extracellular matrix proteins containing full-length fibronectin domains |
title_short |
Collective cell migration on artificial extracellular matrix proteins containing full-length fibronectin domains |
title_full |
Collective cell migration on artificial extracellular matrix proteins containing full-length fibronectin domains |
title_fullStr |
Collective cell migration on artificial extracellular matrix proteins containing full-length fibronectin domains |
title_full_unstemmed |
Collective cell migration on artificial extracellular matrix proteins containing full-length fibronectin domains |
title_sort |
collective cell migration on artificial extracellular matrix proteins containing full-length fibronectin domains |
publishDate |
2011 |
url |
https://hdl.handle.net/10356/85262 http://hdl.handle.net/10220/6946 |
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1772827046514262016 |