Evaluation of Protein Purification Techniques and Effects of Storage Duration on LC-MS/MS Analysis of Archived FFPE Human CRC Tissues.

{"sci_version": "1.2", "schema": "https://corpus.bntrg.co.uk/sci/1.0/sci.schema.json", "id": "pmid:34257588", "kind": "science-record", "revision": 8, "content_hash": "sha256:ef0fbb7a3c655c75d341e38a9b7db0676033ad4718566d74a44ab1fec3932a47", "created_at": "2026-11-01T15:41:43Z", "updated_at": "2026-11-01T22:47:05Z", "generator": {"name": "corpus-assay-engine", "run_id": "reading-sci-2026-11-01"}, "paper": {"state": "complete", "title": "Evaluation of Protein Purification Techniques and Effects of Storage Duration on LC-MS/MS Analysis of Archived FFPE Human CRC Tissues.", "doi": "10.3389/pore.2021.622855", "pmid": "34257588", "authors": ["Sophia C Rossouw", "Hocine Bendou", "Renette J Blignaut", "Liam Bell", "Jonathan Rigby", "Alan Christoffels"], "journal": "Pathology oncology research : POR", "year": 2021, "abstract": "To elucidate cancer pathogenesis and its mechanisms at the molecular level, the collecting and characterization of large individual patient tissue cohorts are required. Since most pathology institutes routinely preserve biopsy tissues by standardized methods of formalin fixation and paraffin embedment, these archived FFPE tissues are important collections of pathology material that include patient metadata, such as medical history and treatments. FFPE blocks can be stored under ambient conditions for decades, while retaining cellular morphology, due to modifications induced by formalin. However, the effect of long-term storage, at resource-limited institutions in developing countries, on extractable protein quantity/quality has not yet been investigated. In addition, the optimal sample preparation techniques required for accurate and reproducible results from label-free LC-MS/MS analysis across block ages remains unclear. This study investigated protein extraction efficiency of 1, 5, and 10-year old human colorectal carcinoma resection tissue and assessed three different gel-free protein purification methods for label-free LC-MS/MS analysis. A sample size of n = 17 patients per experimental group (with experiment power = 0.7 and α = 0.05, resulting in 70% confidence level) was selected. Data were evaluated in terms of protein concentration extracted, peptide/protein identifications, method reproducibility and efficiency, sample proteome integrity (due to storage time), as well as protein/peptide distribution according to biological processes, cellular components, and physicochemical properties. Data are available via ProteomeXchange with identifier PXD017198. The results indicate that the amount of protein extracted is significantly dependent on block age (p < 0.0001), with older blocks yielding less protein than newer blocks. Detergent removal plates were the most efficient and overall reproducible protein purification method with regard to number of peptide and protein identifications, followed by the MagReSyn® SP3/HILIC method (with on-bead enzymatic digestion), and lastly the acetone precipitation and formic acid resolubilization method. Overall, the results indicate that long-term storage of FFPE tissues (as measured by methionine oxidation) does not considerably interfere with retrospective proteomic analysis (p > 0.1). Block age mainly affects initial protein extraction yields and does not extensively impact on subsequent label-free LC-MS/MS analysis results.", "claims": [{"id": "claim-method", "statement": "One-way ANOVA or Kruskal–Wallis tests were conducted (results and conclusions are listed in Supplementary Table S2) to determine if the number of identified peptides and proteins were significantly different between block ages, as well as for each protein purification method.", "kind": "methodological", "target": null, "evidence": [{"asset": "source:pmid:34257588", "locator": "sections[16] \"The Effect of Block Age and Protein Purification Methods on Peptide and Protein Identification\" paragraph 6", "quote": "One-way ANOVA or Kruskal–Wallis tests were conducted (results and conclusions are listed in Supplementary Table S2) to determine if the number of identified peptides and proteins were significantly different between block ages, as well as for each protein purification method."}], "state": "complete"}, {"id": "claim-data-access", "statement": "The mass spectrometry proteomics data [41] generated and analyzed for this study can be found in the PRIDE [43] repository (http://www.ebi.ac.uk/pride/archive/) with the dataset identifier PXD017198 and DOI: 10.6019/PXD017198.", "kind": "methodological", "target": null, "evidence": [{"asset": "source:pmid:34257588", "locator": "sections[26] \"Data Availability Statement\" paragraph 2", "quote": "The mass spectrometry proteomics data [41] generated and analyzed for this study can be found in the PRIDE [43] repository (http://www.ebi.ac.uk/pride/archive/) with the dataset identifier PXD017198 and DOI: 10.6019/PXD017198."}], "state": "complete"}], "gaps": []}, "experiment": {"state": "complete", "objective": null, "steps": [{"id": "read_published_estimate", "order": 1, "name": "Read the published estimate from the source", "kind": "other", "state": "complete", "blocked_on": null, "description": "The claim, method and evidence span published with the source article.", "duration_hours": null, "parameters": {}, "inputs": ["source:pmid:34257588"], "outputs": ["the published estimate and its evidence"], "instruments": [], "reagents": []}, {"id": "obtain_source_data", "order": 2, "name": "Obtain the source data from the named repository", "kind": "data-preparation", "state": "complete", "blocked_on": null, "description": "The GEO series accession resolves and its sample accessions are listed. 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