posted on 2014-02-07, 00:00authored byMasaki Wakabayashi, Hiroki Yoshihara, Takeshi Masuda, Mai Tsukahara, Naoyuki Sugiyama, Yasushi Ishihama
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.