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The Stiffness of Collagen Fibrils Influences Vascular Smooth Muscle Cell Phenotype

Dennis P. McDaniel ^*, Gordon A. Shaw , John T. Elliott ^*, Kiran Bhadriraju , Curt Meuse ^*, Koo-Hyun Chung  and Anne L. Plant ^*

^* Biochemical Science Division and Manufacturing Metrology Division/National Institute of Standards and Technology, Gaithersburg, Maryland 20899; and SAIC, Arlington, Virginia 22203

Correspondence: Address reprint requests to Anne L. Plant, Biochemical Science Division, Chemical Science and Technology Laboratory, National Institute of Standards and Technology, Gaithersburg, MD 20899. Tel.: 301-975-3124; Fax: 301-975-8246; E-mail: anne.plant{at}nist.gov.

Cells receive signals from the extracellular matrix through receptor-dependent interactions, but they are also influenced by the mechanical properties of the matrix. Although bulk properties of substrates have been shown to affect cell behavior, we show here that nanoscale properties of collagen fibrils also play a significant role in determining cell phenotype. Type I collagen fibrils assembled into thin films provide excellent viewing of cells interacting with individual fibrils. Cells can be observed to extensively manipulate the fibrils, and this behavior seems to result in an incompletely spread stellate morphology and a nonproliferative phenotype that is typical of these cells in collagen gels. We show here that thin films of collagen fibrils can be dehydrated, and when seeded on these dehydrated fibrils, smooth muscle cells spread and proliferate extensively. The dehydrated collagen fibrils appear to be similar to the fully hydrated collagen fibrils in topology and in presentation of ß₁ integrin ligation sites, but they are mechanically stiffer. This decrease in compliance of dehydrated fibrils is seen by a failure of cell movement of dehydrated fibrils compared to their ability to rearrange fully hydrated fibrils and from direct measurements by nanoindentation and quantitative atomic force measurements. We suggest that increase in the nanoscale rigidity of collagen fibrils can cause these cells to assume a proliferative phenotype.

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