Label-free proteome analysis of plasma from patients with breast cancer: stage-specific protein expression

ABSTRACT: The breast cancer presents one of the most commonly diagnosed types of cancer among women and its mortality rates remain very high probably due to the diagnosis of this disease is hampered by the lack of an accurate detection method. Since that change of protein expression as well modifications in its glycosylation have been frequently reported in cancer development, the aim of this work was study the differential expression as well modifications of glycosylation of proteins from plasma of women with breast cancer at three different stages of disease. 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. As result, 57,016 peptides and 4,175 proteins among all samples were identified. From this, forty proteins present in unbound (PI – proteins that not interacted 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 breast cancer. Our findings reveal a correlation between alterations in protein glycosylation, lipid metabolism, and the progression of breast cancer.

INSTRUMENT(S): Synapt MS

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Blood Plasma

DISEASE(S): Breast Cancer

SUBMITTER: FREDERICO MORENO  

LAB HEAD: Ana Cristina de Oliveira Monteiro-Moreira

PROVIDER: PXD003106 | Pride | 2017-02-20

REPOSITORIES: Pride