The differential regulation of cell motile activity through matrix stiffness and porosity in three dimensional collagen matrices

Miguel Miron-Mendoza, Joachim Seemann, Frederick Grinnell

Research output: Contribution to journalArticle

148 Scopus citations

Abstract

In three dimensional collagen matrices, cell motile activity results in collagen translocation, cell spreading and cell migration. Cells can penetrate into the matrix as well as spread and migrate along its surface. In the current studies, we quantitatively characterize collagen translocation, cell spreading and cell migration in relationship to collagen matrix stiffness and porosity. Collagen matrices prepared with 1-4mg/ml collagen exhibited matrix stiffness (storage modulus measured by oscillating rheometry) increasing from 4 to 60Pa and matrix porosity (measured by scanning electron microscopy) decreasing from 4 to 1 μm2. Over this collagen concentration range, the consequences of cell motile activity changed markedly. As collagen concentration increased, cells no longer were able to cause translocation of collagen fibrils. Cell migration increased and cell spreading changed from dendritic to more flattened and polarized morphology depending on location of cells within or on the surface of the matrix. Collagen translocation appeared to depend primarily on matrix stiffness, whereas cell spreading and migration were less dependent on matrix stiffness and more dependent on collagen matrix porosity.

Original languageEnglish (US)
Pages (from-to)6425-6435
Number of pages11
JournalBiomaterials
Volume31
Issue number25
DOIs
StatePublished - Sep 1 2010

Keywords

  • Cell migration
  • Cell spreading
  • Collagen translocation
  • Extracellular matrix
  • Mechanoregulation

ASJC Scopus subject areas

  • Bioengineering
  • Ceramics and Composites
  • Biophysics
  • Biomaterials
  • Mechanics of Materials

Fingerprint Dive into the research topics of 'The differential regulation of cell motile activity through matrix stiffness and porosity in three dimensional collagen matrices'. Together they form a unique fingerprint.

  • Cite this