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Related Experiment Video

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Preserving the Phosphoproteome of Clinical Biopsies Using a Quick-Freeze Collection Device.

Jacob J Kennedy1, Amanda Woodcock2, Richard G Ivey1

  • 1Fred Hutchinson Cancer Research Center, Clinical Research Division, Seattle, Washington, USA.

Biopreservation and Biobanking
|October 27, 2022
PubMed
Summary

A new quick-freeze device preserves tissue phosphoproteome without liquid nitrogen, matching gold-standard flash freezing for biomarker discovery in point-of-care settings.

Keywords:
biospecimen preservationdiagnosticsmass spectrometryphosphorylationpreanalyticstissue processing

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Area of Science:

  • Biochemistry
  • Proteomics
  • Biotechnology

Background:

  • Proteomic analysis of tissue biopsies is crucial for understanding disease pathophysiology and identifying biomarkers.
  • Current methods for preserving tissue proteomes, including post-translational modifications, rely on flash freezing in liquid nitrogen (LN2).
  • LN2 availability and trained personnel for rapid processing limit tissue preservation in many clinical settings.

Purpose of the Study:

  • To develop a prototype device for rapid, point-of-care biospecimen freezing without LN2.
  • To evaluate the device's ease of use, shipping compatibility, and cooling performance.
  • To assess the preservation of the phosphoproteome in tissue biospecimens using the prototype compared to LN2 flash freezing.

Main Methods:

  • A proof-of-concept quick-freeze prototype device was developed.
  • Cooling performance was evaluated: <0°C in <60s, <-8°C in <120s, and <0°C for >60min.
  • Murine melanoma xenografts were used; tumors were split and frozen with either LN2 or the prototype.
  • Phosphoproteins were analyzed using liquid chromatography tandem mass spectrometry and targeted multiple reaction monitoring MS.

Main Results:

  • The quick-freeze device successfully preserved the overall phosphoproteome, yielding results comparable to LN2 flash freezing.
  • Cooling performance targets were met, demonstrating rapid and sustained low temperatures.
  • While overall phosphoproteome profiles were equivalent, a subset of phosphopeptides showed increased variability in device-frozen specimens compared to LN2-frozen ones.

Conclusions:

  • The prototype quick-freeze device offers a viable alternative to LN2 for preserving tissue phosphoproteomes at the point-of-care.
  • This technology has the potential to improve tissue biopsy preservation for critical phosphosignaling molecule analysis in diverse clinical environments.
  • Further development could lead to a commercial device enhancing accessibility for proteomic research and diagnostics.