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Evaluating integrin activation with time-resolved flow cytometry.

Jesus Sambrano1, Alexandre Chigaev2, Kapil S Nichani1

  • 1New Mexico State University, Department of Chemical and Materials Engineering, Las Cruces, New Mexic, United States.

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|July 12, 2018
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Summary
This summary is machine-generated.

Förster resonance energy transfer (FRET) enables cell-by-cell measurement of protein conformational changes using flow cytometry. This study quantifies leukocyte integrin activation by measuring FRET changes during conformational shifts.

Keywords:
Förster resonance energy transferflow cytometryfluorescence lifetimeintegrin activationphasor analysisprotein conformation

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Area of Science:

  • Biophysics
  • Cell Biology
  • Immunology

Background:

  • Förster resonance energy transfer (FRET) is a biophysical technique used to study molecular interactions and conformational changes in proteins.
  • Flow cytometry offers a high-throughput method for analyzing cellular properties at a single-cell level.

Purpose of the Study:

  • To quantitatively measure the conformational changes of leukocyte α4β1 integrin dimers upon activation using FRET and flow cytometry.
  • To establish a precise cytometric approach for profiling fluorescence donor decay kinetics during integrin conformational changes.

Main Methods:

  • Utilized Förster resonance energy transfer (FRET) coupled with time-resolved flow cytometry to monitor integrin activation.
  • Employed graphical phasor analysis for precise comparative analysis of FRET populations and donor recovery.

Main Results:

  • Observed significant changes in FRET efficiency (37% inactive, 26% active) corresponding to integrin conformational changes.
  • Detected increases in donor emission (up to 17%) and fluorescence lifetime shifts (>1.0 ns) during integrin activation.
  • Demonstrated the utility of phasor analysis for distinguishing between inactive, partially active, and fully active integrin states.

Conclusions:

  • Established a quantitative single-cell cytometric method for profiling FRET kinetics during integrin conformational changes.
  • This approach enables rapid screening and profiling of integrin activation states in leukocytes.
  • The study provides a robust platform for investigating dynamic protein conformational changes in cellular systems.