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A proteomic approach to investigate potential biomarkers directed against membrane‐associated breast cancer proteins
Author(s) -
Canelle Ludovic,
Bousquet Jordane,
Pionneau Cedric,
Hardouin Julie,
ChoquetKastylevsky Genevieve,
JoubertCaron Raymonde,
Caron Michel
Publication year - 2006
Publication title -
electrophoresis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.666
H-Index - 158
eISSN - 1522-2683
pISSN - 0173-0835
DOI - 10.1002/elps.200500712
Subject(s) - membrane protein , transmembrane protein , breast cancer , antigen , proteomics , blot , antibody , chemistry , cell membrane , cancer , cell , biology , cancer research , membrane , biochemistry , medicine , immunology , receptor , gene
The identification of specific protein markers for breast cancer would provide the basis for early diagnosis. Particularly, membrane and membrane‐associated proteins are rich in targets for antibodies that may constitute suitable biomarkers of carcinogenesis. However, membrane proteins separation using 2‐DE remains difficult. In this work, the breast cancer cell line MCF7 was used as source of proteins for the screening of potential cell membrane‐associated antigens recognized by autoantibodies in patients with breast cancer and healthy volunteers. The protein extract obtained using trifluoroethanol (TFE) as cosolvent was compared to a total cell lysate protein extract prepared by a current technique. After 2‐DE separation of the two extracts, their protein patterns clearly differed. About 63% of the proteins identified in the TFE‐extract were predicted to possess at least one transmembrane domain. 2‐D blots probed with sera from cancer patients or from healthy volunteers showed that, as expected, additional antigens were provided in the TFE‐extract. Thus, the method described here appeared well suited for proteomic investigation of potential biomarkers undetected by current techniques.