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Published on: April 17, 2014
Fibronectin organization under and near cells
Kathy L De Jong1, Heather C MacLeod, Peter R Norton
1Department of Chemistry, University of Western Ontario, London, ON, Canada.
European Biophysics Journal : EBJ
|September 1, 2006
Summary
Cells reorganize fibronectin (Fn) into disordered networks for adhesion and ordered arrays during movement. This study reveals how cell motility influences the structure and organization of the extracellular matrix.
Area of Science:
- Cell biology
- Biophysics
- Extracellular matrix research
Background:
- Soluble fibronectin (Fn) molecules polymerize into visible networks.
- Cellular interactions with the extracellular matrix are crucial for adhesion and motility.
- Understanding fibronectin organization provides insights into matrix dynamics.
Purpose of the Study:
- To investigate the dynamic reorganization of fibronectin structures during cell adhesion and motility.
- To analyze the relationship between cell movement and the spatial arrangement of fibronectin fibers.
- To elucidate the forces involved in fibronectin fiber alignment by motile cells.
Main Methods:
- Utilizing fluorescently labeled fibronectin protomers and antibody labeling to visualize networks.
- Employing confocal microscopy and atomic force microscopy (AFM) for high-resolution imaging.
- Analyzing static patterns and dynamic changes in fibronectin organization relative to cell edges.
Main Results:
- Fibronectin networks appear as disordered arrays under the cell during adhesion.
- Ordered fibronectin arrays form perpendicular to the retracting cell edge during movement.
- AFM and confocal microscopy confirm fibronectin presence in cell-associated fibers.
- Cellular forces can reorganize fibronectin fibers into aligned arrays, with orientation influencing attachment.
Conclusions:
- Disorganized fibronectin fibers facilitate cell adhesion and spreading.
- Ordered fibronectin arrays outside the cell result from reorganization during cell motility.
- Cells actively generate forces to align fibronectin fibers, influencing matrix structure.
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