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Mitigation of reactive human cell adhesion on poly(dimethylsiloxane) by immobilized trypsin.

Abstract
Occlusion or blockage of silicone shunts utilized in the treatment of hydrocephalus is a major challenge that is currently addressed by multiple shunt replacements. Shunt occlusion is caused by the adhesion and proliferation of reactive cells, such as glial and vascular cells, into the lumen of the catheter and on valve components. This in vitro study describes how the adhesive behavior of four human cell types on poly(dimethylsiloxane) (PDMS) surfaces can be suppressed by functionalization with trypsin, a proteolytic enzyme. The covalently conjugated trypsin retained its proteolytic activity and acted in a dose-dependent manner. Trypsin-modified PDMS surfaces supported significantly lower adhesion of normal human astrocytes, human microglia, human dermal fibroblasts, and human umbilical vein endothelial cells compared to unmodified PDMS surfaces (p < 0.0001). Immunofluorescence imaging of cellular fibronectin and quantitative adsorption experiments with serum components indicated that the PDMS surfaces immobilized with trypsin inhibited surface remodeling by all cell types and resisted protein adsorption. The impact of this work lies in the recognition that the well-known proteolytic characteristics of trypsin can be harnessed by covalent surface immobilization to suppress cell adhesion and protein adsorption.
AuthorsAnil Kumar H Achyuta, Kyle D Stephens, Hilton G Pryce Lewis, Shashi K Murthy
JournalLangmuir : the ACS journal of surfaces and colloids (Langmuir) Vol. 26 Issue 6 Pg. 4160-7 (Mar 16 2010) ISSN: 1520-5827 [Electronic] United States
PMID20214394 (Publication Type: Journal Article, Research Support, N.I.H., Extramural)
Chemical References
  • Blood Proteins
  • Dimethylpolysiloxanes
  • Enzymes, Immobilized
  • baysilon
  • Trypsin
Topics
  • Adsorption
  • Blood Proteins (chemistry)
  • Cell Adhesion
  • Cells, Cultured
  • Dimethylpolysiloxanes
  • Enzymes, Immobilized
  • Fluorescent Antibody Technique
  • Humans
  • Trypsin

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