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Proteomics Study of Human Breast Milk for Breast Cancer Biomarkers Discovery
Author(s) -
Aslebagh Roshanak,
Ngounou Armand,
Channaveerappa Devika,
Arcaro Kathleen,
Darie Costel
Publication year - 2015
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.29.1_supplement.567.26
Subject(s) - breast cancer , proteomics , coomassie brilliant blue , mammography , cancer , medicine , biomarker discovery , mass spectrometry , oncology , pathology , chemistry , chromatography , staining , biochemistry , gene
Breast cancer as one of the major causes of mortality in US is a challenging subject to study. Based on recent National Cancer Institute's statistics, it is the second common cancer in US. Detection and treatment of breast cancer at the very early stages and diagnosis of breast cancer risk before it happens is a challenging subject of study. Mammography has greatly increased the early detection of breast cancer, but has known limitations, especially in younger women with dense breasts. Breast milk is an appropriate cancer microenvironment for identifying breast cancer biomarkers that consists of epithelial cells and the proteins which are provided from breast tissue. Mass spectrometry‐based proteomics on human breast milk may offer a novel way to identify young women at increased risk of developing breast cancer. In this study, breast milk samples were separated by SDS‐PAGE and stained by Coomassie for qualitative and quantitative analysis and direct comparison of the samples. The gel lanes of cancerous and healthy samples (as the control) were cut into several bands which were digested with trypsin and then analyzed by nanoliquid chromatography‐tandem mass spectrometry (nanoLC‐MS/MS) using a nanoAcquity UPLC coupled with QTOF Micro mass spectrometer. Data processing and analysis were performed using MassLynx (version 4.1), ProteinLynx Global Served (PLGS 2.4), Mascot and Scaffold 4.0. In the Coomassie‐stained SDS‐PAGE, although the overall protein patterns of most of the major bands are similar, sample specific‐bands are also present which make the differences between cancerous and healthy samples. These outcomes are currently being investigated.