Phosphoproteome analysis of formalin-fixed and paraffin-embedded tissue sections mounted on microscope slides
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Updated: May 4, 2026

Proteomic Sample Preparation from Formalin Fixed and Paraffin Embedded Tissue
Published on: September 2, 2013
Masaki Wakabayashi1, Hiroki Yoshihara, Takeshi Masuda
1Graduate School of Pharmaceutical Sciences, Kyoto University , Sakyo-ku, Kyoto 606-8501, Japan.
Abstract:
Formalin-fixed and paraffin-embedded (FFPE) sections mounted on microscope slides are one of the largest available resources for retrospective research on various diseases, but quantitative phosphoproteome analysis of FFPE sections has never been achieved because of the extreme difficulty of procuring sufficient phosphopeptides from the limited amounts of proteins on the slides. Here, we present the first protocol for quantitative phosphoproteome analysis of FFPE sections by utilizing phase-transfer surfactant-aided extraction/tryptic digestion of FFPE proteins followed by high-recovery phosphopeptide enrichment via lactic acid-modified titania chromatography. We established that FFPE sections retain a similar phosphoproteome to fresh tissue specimens during storage for at least 9 months, confirming the utility of our method for evaluating phosphorylation profiles in various diseases. We also verified that chemical labeling based on reductive dimethylation of amino groups was feasible for quantitative phosphoproteome analysis of FFPE samples on slides. Furthermore, we improved the LC-MS sensitivity by miniaturizing nanoLC columns to 25 μm inner diameter. With this system, we could identify 1090 phosphopeptides from a single FFPE section obtained from a microscope slide, containing 25.2 ± 5.4 μg of proteins. This protocol should be useful for large-scale phosphoproteome analysis of archival FFPE slides, especially scarce samples from patients with rare diseases.
Insights
This study introduces a novel method for quantitative phosphoproteome analysis in formalin-fixed, paraffin-embedded (FFPE) tissue sections. The new protocol enables detailed phosphorylation profiling from archival slides, crucial for retrospective disease research.
Area of Science:
- Proteomics
- Biochemistry
- Pathology
Background:
- Formalin-fixed, paraffin-embedded (FFPE) tissue sections are valuable for retrospective disease research.
- Quantitative phosphoproteome analysis of FFPE sections has been challenging due to limited protein and phosphopeptide yields.
Purpose of the Study:
- To develop the first protocol for quantitative phosphoproteome analysis of FFPE tissue sections.
- To enable comprehensive phosphorylation profiling from archival FFPE slides for disease research.
Main Methods:
- Phase-transfer surfactant-aided extraction and tryptic digestion of FFPE proteins.
- High-recovery phosphopeptide enrichment using lactic acid-modified titania chromatography.
- Chemical labeling via reductive dimethylation and enhanced LC-MS sensitivity with miniaturized nanoLC columns.
Main Results:
- Successfully established a protocol for quantitative phosphoproteome analysis of FFPE sections.
- Demonstrated that FFPE sections maintain a stable phosphoproteome for at least 9 months.
- Identified 1090 phosphopeptides from a single FFPE section using the developed method.
Conclusions:
- The developed protocol is the first to enable quantitative phosphoproteome analysis of FFPE sections.
- This method is suitable for evaluating phosphorylation profiles in various diseases using archival FFPE slides.
- The protocol facilitates large-scale phosphoproteome analysis, particularly for scarce samples like those from rare diseases.
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