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Protein adsorption and cell attachment to patterned surfaces.

C D McFarland1, C H Thomas, C DeFilippis

  • 1CSIRO Molecular Science, Sydney Laboratory, P.O. Box 184, North Ryde, NSW 1670, Australia.

Journal of Biomedical Materials Research
|November 26, 1999
PubMed
Summary

Human bone-derived cells (HBDC) preferentially attach to specific surface chemistries on biomaterials, mediated by vitronectin adsorption. This cell attachment mechanism influences cell spreading and may impact tissue development.

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Area of Science:

  • Biomaterials Science
  • Cell Biology
  • Tissue Engineering

Background:

  • Understanding cell attachment to biomaterials is crucial for designing functional tissue architectures.
  • Patterned surface chemistry on biomaterials can direct cell behavior.
  • The role of specific adhesive proteins in cell localization on patterned surfaces requires elucidation.

Purpose of the Study:

  • To investigate the mechanism of human bone-derived cell (HBDC) attachment to surfaces with patterned chemistry.
  • To determine the role of serum adhesive glycoproteins in mediating HBDC spatial organization.
  • To assess the impact of surface chemistry and protein adsorption on cell morphology and adhesion formation.

Main Methods:

  • Photolithography was used to create alternating domains of N-(2-aminoethyl)-3-aminopropyl-trimethoxysilane (EDS) and dimethyldichlorosilane (DMS).

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  • HBDC were seeded onto patterned surfaces, and their localization was analyzed.
  • Serum depleted of adhesive glycoproteins was used to identify mediating proteins.
  • Immunostaining confirmed protein adsorption and cell adhesion receptor distribution.

    • Main Results:

    • HBDC preferentially localized to EDS domains within 90 minutes of seeding.
    • Vitronectin (Vn) adsorption to EDS domains mediated this spatial organization.
    • Fibronectin (Fn) adsorption was inhibited by competing serum components.
    • Both Vn and Fn adsorbed to EDS and DMS regions from pure solution, mediating cell adhesion.
    • Cell spreading was constrained on EDS domains, with limited integrin receptor clustering and focal adhesion formation.

    Conclusions:

    • Vitronectin mediates preferential attachment of HBDC to specific patterned surface chemistries.
    • The competitive adsorption of serum proteins significantly influences cell localization on biomaterials.
    • Constrained cell spreading on certain domains may affect subsequent differentiated cell functions.