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Single-cell Photoconversion in Living Intact Zebrafish
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Protein fishing from single live cells.

Elaheh Shekaramiz1, Rupak Doshi2,3, H Kumar Wickramasinghe4,5

  • 1Department of Biomedical Engineering, University of California Irvine, Irvine, CA, USA.

Journal of Nanobiotechnology
|September 13, 2018
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Summary
This summary is machine-generated.

Researchers developed a novel biophysical method using a nanoaspirator to extract native proteins from single live mammalian cells for quantitative analysis. This technique avoids cell lysis, enabling live, spatiotemporally-controlled single-cell proteomics.

Keywords:
Live cell protein detectionNanopipetteProteomicsSingle cell analysis

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Area of Science:

  • Biophysics
  • Proteomics
  • Cell Biology

Background:

  • Traditional intracellular protein analysis methods often require cell manipulation that compromises cell viability.
  • Techniques like mass spectrometry and western blotting necessitate cell permeabilization or lysis.
  • There is a need for methods that allow for the study of native proteins in live cells.

Purpose of the Study:

  • To present a novel biophysical method for isolating native proteins from single mammalian cells.
  • To enable quantitative detection of intracellular proteins without compromising cell viability.
  • To facilitate spatiotemporally-controlled, live, single-cell proteomics.

Main Methods:

  • Utilized a nanoaspirator for precise extraction of cytoplasmic or nuclear proteins.
  • Developed a method for ex cellulo quantitative detection of isolated proteins.
  • Maintained single mammalian cell viability throughout the protein extraction process.

Main Results:

  • Successfully extracted native proteins from single mammalian cells using the nanoaspirator.
  • Demonstrated that the method does not compromise cell viability.
  • Enabled quantitative detection of proteins from live, single cells.

Conclusions:

  • The nanoaspirator-based method offers a non-destructive approach to single-cell proteomics.
  • This technique allows for live, quantitative analysis of intracellular proteins.
  • Opens new avenues for spatiotemporally-controlled proteomic studies in live cells.