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Quantitative Mass Spectrometric Profiling of Cancer-cell Proteomes Derived From Liquid and Solid Tumors
Published on: February 27, 2015
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Screening protein isoforms predictive for cancer using immunoaffinity capture and fast LC-MS in PRM mode
Antoine Lesur1, Lina Ancheva1, Yeoun Jin Kim1
1Luxembourg Clinical Proteomics Center (LCP), CRP-Santé, Strassen, Luxembourg.
Proteomics. Clinical Applications
|February 7, 2015
Summary
This study introduces an immunocapture method for detecting cancer driver mutations. This approach enhances protein analysis sensitivity and selectivity for improved patient treatment selection.
Area of Science:
- Proteomics
- Cancer Biomarkers
- Mass Spectrometry
Background:
- Analyzing complex biological samples for mutations presents sensitivity and selectivity challenges.
- Existing methods struggle with unfractionated samples, limiting mutation detection.
Purpose of the Study:
- To develop an immunocapture strategy for extracting cancer-specific proteins harboring driver mutations.
- To enable simultaneous assessment of protein mutational status using mass spectrometry (MS).
Main Methods:
- Employed immunoaffinity enrichment to isolate target proteins.
- Utilized fast liquid chromatography (LC) separations with short nanobore columns.
- Coupled LC with a high-resolution quadrupole-orbitrap mass spectrometer for rapid analysis.
Main Results:
- Demonstrated the technical performance of the rapid LC-MS platform.
- Successfully applied the method for quantitative profiling of Ras and EGFR protein isoforms in cells.
- Analyzed serum amyloid A isoforms in plasma samples.
Conclusions:
- Immunoaffinity purification coupled with fast LC-MS facilitates driver mutation detection in tissue and plasma.
- This method aids in identifying cancer biomarkers for personalized therapeutic selection.
- The strategy improves diagnostic accuracy for targeted cancer treatments.
