By Kwang W. Jeon (Eds.)
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Considering that clustering of the ligand increased SF and FA formation, it is not surprising that similar effects were seen for cell migration. , 2000). New Insights into Focal Adhesions 33 However, the estimation of the spacing between clusters required for maximal SF and FA assembly determined by this group (9 nm for clusters of five ligands and 60 nm for clusters of nine ligands) was much lower than that concluded by Massia and Hubbell (140 nm) (Massia and Hubbell, 1991). The reason for this is unclear, but may reflect differences in cell type and experimental design.
In support of this, cells grown on the –COOHterminated SAMs were shown to adhere better, spread, and form FAs and SFs, while those on the –CH3-terminated SAMs did not adhere well or form FAs or SFs. These differences were attributed to better adsorption of ECM proteins to the carboxyl group (McClary and Grainger, 1999). Even when a constitutively active mutant of RhoA was overexpressed in the cells grown on the –CH3-terminated SAMs, FA assembly did not occur due to inadequate adhesion via integrins to the ECM ligand (McClary and Grainger, 1999).
2005). Biomaterial surfaces provide a reactive surface on which to couple a ligand of interest, and a nonadhesive (passivated) region in the areas between ligands. , 2005). To study integrin adhesion in cells on artificial surfaces, several features are typically varied, such as ligand structure, conformation, and spatial orientation. , 2003), or larger fragments or domains of an ECM protein (Cutler and Garcia, 2003). , 2000). , 2006, 2007). Such fine-tuned manipulations of the adhesive surface allows for a detailed analysis of which aspects of integrin adhesion are required for transmitting signals to the actin cytoskeleton.