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Quantitative MS Workflow for a High-Quality Secretome Analysis by a Quantitative Secretome-Proteome Comparison
Gereon Poschmann1, Nina Prescher1, Kai Stühler2
1Institute of Molecular Medicine I, Proteome Research, University Hospital Düsseldorf, Heinrich Heine University Düsseldorf, Düsseldorf, Germany.
Methods in Molecular Biology (Clifton, N.J.)
|May 5, 2021
Summary
This study introduces a method to accurately identify proteins secreted by cells (secretome). By comparing conditioned medium with cellular proteomes, we minimize contaminants and ensure high-quality secretome data.
Area of Science:
- Cell biology
- Proteomics
- Biochemistry
Background:
- Cells communicate via secreted proteins, forming the secretome.
- Conditioned media analysis can be confounded by serum or dying cell proteins.
- Accurate secretome characterization is crucial for understanding cellular functions.
Purpose of the Study:
- To develop a workflow for high-quality secretome data acquisition.
- To quantitatively compare conditioned medium and cellular proteomes.
- To minimize contaminants in secretome analysis.
Main Methods:
- Cell cultivation and sample preparation.
- Label-free mass spectrometric quantification.
- Comparative analysis of conditioned medium and cellular proteomes.
Main Results:
- A workflow was established for quantitative proteomic comparison.
- Bona fide secreted proteins were detected by minimizing contaminants.
- The method enhances the reliability of secretome profiling.
Conclusions:
- Quantitative proteomic comparison effectively identifies true secreted proteins.
- This approach provides high-quality secretome data.
- Minimizing contaminants is key for accurate secretome analysis.
