Label-Free Proteome Analysis of Plasma from Patients with Breast Cancer: Stage-Specific Protein Expression.

{"sci_version": "1.2", "schema": "https://corpus.bntrg.co.uk/sci/1.0/sci.schema.json", "id": "pmid:28210565", "kind": "science-record", "revision": 6, "content_hash": "sha256:2313da2c3716cb303d85451d9be7afb07638535a5c53fb3305c1b25738f4fdaf", "created_at": "2026-11-01T15:40:22Z", "updated_at": "2026-11-01T21:20:48Z", "generator": {"name": "corpus-assay-engine", "run_id": "reading-sci-2026-11-01"}, "paper": {"state": "complete", "title": "Label-Free Proteome Analysis of Plasma from Patients with Breast Cancer: Stage-Specific Protein Expression.", "doi": "10.3389/fonc.2017.00014", "pmid": "28210565", "authors": ["Marina Duarte Pinto Lobo", "Frederico Bruno Mendes Batista Moreno", "Gustavo Henrique Martins Ferreira Souza", "Sara Maria Moreira Lima Verde", "Renato de Azevedo Moreira", "Ana Cristina de Oliveira Monteiro-Moreira"], "journal": "Frontiers in oncology", "year": 2017, "abstract": "Breast cancer is one of the most commonly diagnosed types of cancer among women. Breast cancer mortality rates remain high probably because its diagnosis is hampered by inaccurate detection methods. Since changes in protein expression as well as modifications in protein glycosylation have been frequently reported in cancer development, the aim of this work was to study the differential expression as well as modifications of glycosylation of proteins from plasma of women with breast cancer at different stages of disease (n = 30) compared to healthy women (n = 10). A proteomics approach was used that depleted albumin and IgG from plasma followed by glycoprotein enrichment using immobilized Moraceae lectin (frutalin)-affinity chromatography and data-independent label-free mass spectrometric analysis. Data are available via ProteomeXchange with identifier PXD003106. As result, 57,016 peptides and 4,175 proteins among all samples were identified. From this, 40 proteins present in unbound (PI-proteins that did not interact with lectin) and bound (PII-proteins that interacted with lectin) fractions were differentially expressed. High levels of apolipoprotein A-II were detected here that were elevated significantly in the early and advanced stages of the disease. Apolipoprotein C-III was detected in both fractions, and its level was increased slightly in the PI fraction of patients with early-stage breast cancer and expressed at higher levels in the PII fraction of patients with early and intermediate stages. Clusterin was present at higher levels in both fractions of patients with early and intermediate stages of breast cancer. Our findings reveal a correlation between alterations in protein glycosylation, lipid metabolism, and the progression of breast cancer.", "claims": [{"id": "claim-method", "statement": "The average quantitative values of all samples were calculated, and the p value (p < 0.05) calculated using ExpressionE software to refer to the differences between biological replicates.", "kind": "methodological", "target": null, "evidence": [{"asset": "source:pmid:28210565", "locator": "sections[10] \"Data Processing, Protein Identification, and Quantification\" paragraph 2", "quote": "The average quantitative values of all samples were calculated, and the p value (p < 0.05) calculated using ExpressionE software to refer to the differences between biological replicates."}], "state": "complete"}, {"id": "claim-data-access", "statement": "Data are available via ProteomeXchange with identifier PXD003106.", "kind": "methodological", "target": null, "evidence": [{"asset": "source:pmid:28210565", "locator": "sections[0] \"Abstract\" paragraph 1", "quote": "Data are available via ProteomeXchange with identifier PXD003106."}], "state": "complete"}, {"id": "claim-target-result", "statement": "The study used data-independent label-free mass spectrometry after albumin/IgG depletion and frutalin-affinity enrichment of plasma; the proteomics data were available via ProteomeXchange with identifier PXD003106. The headline finding was identification of 57,016 peptides and 4,175 proteins, with 40 proteins differentially expressed across the unbound-PI and bound-PII fractions.", "kind": "qualitative", "target": null, "evidence": [{"asset": "source:pmid:28210565", "locator": "sections[0] \"Abstract\" paragraph 1", "quote": "A proteomics approach was used that depleted albumin and IgG from plasma followed by glycoprotein enrichment using immobilized Moraceae lectin (frutalin)-affinity chromatography and data-independent label-free mass spectrometric analysis."}, {"asset": "source:pmid:28210565", "locator": "sections[0] \"Abstract\" paragraph 1", "quote": "Data are available via ProteomeXchange with identifier PXD003106."}, {"asset": "source:pmid:28210565", "locator": "sections[0] \"Abstract\" paragraph 1", "quote": "As result, 57,016 peptides and 4,175 proteins among all samples were identified."}, {"asset": "source:pmid:28210565", "locator": "sections[0] \"Abstract\" paragraph 1", "quote": "From this, 40 proteins present in unbound (PI—proteins that did not interact with lectin) and bound (PII—proteins that interacted with lectin) fractions were differentially expressed."}], "state": "complete"}], "gaps": []}, "experiment": {"state": "complete", "objective": "The study used data-independent label-free mass spectrometry after albumin/IgG depletion and frutalin-affinity enrichment of plasma; the proteomics data were available via ProteomeXchange with identifier PXD003106. 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