Lateral spacing of integrin ligands influences cell spreading and focal adhesion assembly

被引:294
作者
Cavalcanti-Adam, EA
Micoulet, A
Blümmel, J
Auernheimer, J
Kessler, H
Spatz, JP
机构
[1] Heidelberg Univ, Inst Chem Phys, Dept Biophys Chem, D-69120 Heidelberg, Germany
[2] Max Planck Inst Met Res, Dept New Mat & Biosyst, D-70569 Stuttgart, Germany
[3] MIT, Dept Mat Sci & Engn, Cambridge, MA 02139 USA
[4] Tech Univ Munich, Inst Organ Chem & Biochem, D-85747 Garching, Germany
关键词
nanotechnology; focal adhesion; integrin clustering; RGD peptides;
D O I
10.1016/j.ejcb.2005.09.011
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
Cell-extracellular matrix (cell-ECM) interactions mediated by integrin receptors are essential for providing positional and environmental information necessary for many cell functions, such as proliferation, differentiation and survival. In vitro studies on cell adhesion to randomly adsorbed molecules on substrates have been limited to sub-micrometer patches. thus preventing the detailed study of structural arrangement of integrins and their ligands. In this article, we illustrate the role of the distance between integrin ligands, namely the RGD (arginine-glycine-aspartate) sequence present in ECM proteins, in the control of cell adhesion. By using substrates, which carry cyclic RGD peptides arranged in highly defined nanopatterns, we investigated the dynamics of cell spreading and the molecular composition of adhesion sites in relation to a fixed spacing between the peptides on the surface. Our novel approach for in vitro studies on cell adhesion indicates that not only the composition, but also the spatial organization of the extracellular environment is important in regulating cell-ECM interactions. (c) 2005 Elsevier GmbH. All rights reserved.
引用
收藏
页码:219 / 224
页数:6
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