Proteomics-based approach identified differentially expressed proteins with potential roles in endometrial carcinoma.
BACKGROUND
We used proteomic approaches to identify altered expressed proteins in endometrial carcinoma, with the aim of discovering potential biomarkers or therapeutic targets for endometrial carcinoma.


METHODS
The global proteins extracted from endometrial carcinoma and normal endometrial tissues were separated by 2-dimensional electrophoresis and analyzed with PDQuest (Bio-Rad, Hercules, Calif) software. The differentially expressed spots were identified by mass spectrometry and searched against NCBInr protein database. Those proteins with potential roles were confirmed by Western blotting and immunohistochemical assays.


RESULTS
Ninety-nine proteins were identified by mass spectrometry, and a cluster diagram analysis indicated that these proteins were involved in metabolism, cell transformation, protein folding, translation and modification, proliferation and apoptosis, signal transduction, cytoskeleton, and so on. In confirmatory immunoblotting and immunohistochemical analyses, overexpressions of epidermal fatty acid-binding protein, calcyphosine, and cyclophilin A were also observed in endometrial carcinoma tissues, which were consistent with the proteomic results.


CONCLUSIONS
Our results suggested that these identified proteins, including epidermal fatty acid-binding protein, calcyphosine, and cyclophilin A, might be of potential values in the studies of endometrial carcinogenesis or investigations of diagnostic biomarkers or treatment targets for endometrial carcinoma.
Li
Zhengyu
Z
Department of Gynecology and Obstetrics, West China Second Hospital, Sichuan University, Chengdu 610041, China.
Min
Wenjiao
W
Huang
Canhua
C
Bai
Shujun
S
Tang
Minghai
M
Zhao
Xia
X
D000230:Adenocarcinoma / Q000209:etiology / Q000378:metabolism*; D000328:Adult; D016000:Cluster Analysis; D016889:Endometrial Neoplasms / Q000209:etiology / Q000378:metabolism*; D005260:Female; D006801:Humans; D016555:Matched-Pair Analysis; D008875:Middle Aged; D009363:Neoplasm Proteins / Q000032:analysis / Q000302:isolation & purification* / Q000378:metabolism / Q000502:physiology; D020543:Proteome / Q000032:analysis; D040901:Proteomics / Q000379:methods; D053719:Tandem Mass Spectrometry
D009363:Neoplasm Proteins; D020543:Proteome