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A Versatile Method of Patterning Proteins and Cells
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Tuning cell-surface affinity to direct cell specific responses to patterned proteins.

Sébastien G Ricoult1, Greta Thompson-Steckel, James P Correia

  • 1McGill Program in NeuroEngineering, Department of Biomedical Engineering, McGill University, 740 Dr. Penfield Avenue, Montreal, Quebec H3A 0G1, Canada; Genome Quebec Innovation Centre, McGill University, Montréal, Quebec H3A 0G1, Canada; McGill Program in NeuroEngineering, Department of Neurology and Neurosurgery, Montreal Neurological Institute, McGill University, 3801 University Ave., Montreal, Quebec H3A 2B4, Canada.

Biomaterials
|October 23, 2013
PubMed
Summary
This summary is machine-generated.

Cell migration is guided by extracellular cues. Researchers developed a method to control cell response to protein cues by tuning the reference surface (RS), demonstrating that RS affinity can override specific protein interactions.

Keywords:
Cell–surface affinityFibronectinMicrocontact printingPDLPDMSPLL-g-PEGPoly(ethylene glycol)PolylysineReference surfacepoly-d-lysinepoly-l-lysine-grafted-polyethylene glycolpolydimethylsiloxane

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Area of Science:

  • Cell Biology
  • Biophysics
  • Materials Science

Background:

  • Cell migration is crucial for development and disease.
  • Extracellular matrix (ECM) proteins act as cues influencing cell behavior.
  • Understanding cell response to patterned cues requires controlled experimental conditions.

Purpose of the Study:

  • To define and investigate the role of a reference surface (RS) in modulating cell responses to patterned protein cues.
  • To develop a method for systematically tuning the RS affinity.
  • To reveal specific cell-type and protein-dependent response curves.

Main Methods:

  • Microcontact printing was used to pattern ECM proteins (fibronectin, netrin-1).
  • A series of reference surfaces (RS) with varying poly-D-lysine (PDL) and polyethylene glycol (PEG) ratios were created.
  • Cell distribution and response were quantified on substrates with different RS affinities.

Main Results:

  • The affinity of the RS significantly influenced cell response, overriding specific protein interactions.
  • High-affinity RS led to no response to patterned proteins, while low-affinity RS induced preference for patterned proteins.
  • Specific, quantitative response curves unique to cell type-protein pairs were observed, especially with intermediate RS affinities.

Conclusions:

  • Cellular choices in response to surface-bound cues are context-dependent and must be interpreted relative to the RS.
  • Tuning RS affinity offers a powerful method to control and study cell-surface interactions.
  • This approach provides new insights into cell signaling pathways and quantitative analysis of cell behavior.