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Microscale mechanisms of agarose-induced disruption of collagen remodeling

Title
Microscale mechanisms of agarose-induced disruption of collagen remodeling
Authors
Ulrich, Theresa A.Lee, Tae GeolShon, Hyun KyongMoon, Dae WonKumar, Sanjay
DGIST Authors
Ulrich, Theresa A.; Lee, Tae Geol; Shon, Hyun Kyong; Moon, Dae Won; Kumar, Sanjay
Issue Date
2011-08
Citation
Biomaterials, 32(24), 5633-5642
Type
Article
Keywords
BrainCell adhesionHydrogelECM (extracellular matrix)Mechanical propertiesElasticityMESENCHYMAL STEM-CELLSION MASS-SPECTROMETRYNONLINEAR ELASTICITYHYDROGELSPROTEINORIENTATIONREORGANIZATIONINTERFACECHEMISTRYMIGRATION
Author Keywords
BrainCell adhesionHydrogelECM (extracellular matrix)Mechanical propertiesElasticity
Keywords
MESENCHYMAL STEM-CELLSION MASS-SPECTROMETRYNONLINEAR ELASTICITYHYDROGELSPROTEINORIENTATIONREORGANIZATIONINTERFACECHEMISTRYMIGRATION
ISSN
0142-9612
Abstract
Cells are strongly influenced by the local structure and mechanics of the extracellular matrix (ECM). We recently showed that adding agarose to soft collagen ECMs can mechanically stiffen these hydrogels by two orders of magnitude while limiting 3D cell motility, which we speculated might derive from agarose-mediated inhibition of collagen fiber deformation and remodeling. Here, we directly address this hypothesis by investigating the effects of agarose on cell-collagen interactions at the microscale. Addition of agarose progressively restricts cell spreading, reduces stress fiber and focal adhesion assembly, and inhibits macroscopic gel compaction. While time-of-flight secondary ion mass spectrometry and scanning electron microscopy fail to reveal agarose-induced alterations in collagen ligand presentation, the latter modality shows that agarose strongly impairs cell-directed assembly of large collagen bundles. Agarose-mediated inhibition of cell spreading and cytoarchitecture can be rescued by β-agarase digestion or by covalently crosslinking the matrix with glutaraldehyde. Based on these results, we argue that cell spreading and motility on collagen requires local matrix stiffening, which can be achieved via cell-mediated fiber remodeling or by chemically crosslinking the fibers. These findings provide new mechanistic insights into the regulatory function of agarose and bear general implications for cell adhesion and motility in fibrous ECMs. © 2011 Elsevier Ltd.
URI
http://hdl.handle.net/20.500.11750/13416
DOI
10.1016/j.biomaterials.2011.04.045
Publisher
ELSEVIER SCI LTD
Related Researcher
  • Author Moon, Dae Won NanoBio Imaging Laboratory
  • Research Interests Coherent Raman Scattering; Surface Plasmon Resonance Imaging Ellipsometry; Imaging Mass Spectrometry; Time-of-flight Medium Energy Ion Scattering
Files:
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Collection:
Department of New BiologyNanoBio Imaging Laboratory1. Journal Articles


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