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European Journal of Gynaecological Oncology (EJGO) is published by IMR Press from Volume 40 Issue 1 (2019). Previous articles were published by another publisher on a subscription basis, and they are hosted by IMR Press on imrpress.com as a courtesy and upon agreement with S.O.G.
Analysis of protein profiles in human epithelial ovarian cancer tissues by proteomic technology
S. N. Chow1,2a,*, R. J. Chen1, C. H. Chen1, T. C. Chang1, L. C. Chen3, W. J. Lee1, J. Shen4, L. P. Chow5
1 Department of Obstetrics and Gynecology, College of Medicine and National Taiwan University Hospital, National Taiwan University, Taipei (Taiwan)
2 School of Medicine, Fujen Catholic University, Taipei (Taiwan)
2 Gynecologic Oncology Research Center, Department of Obstetrics and Gynecology, Min-Sheng General Hospital, Taoyoun (Taiwan)
3 Division of Research and Development, Digitalgene Biosciences Co., Ltd, Si-Chih, Taipei (Taiwan)
4 Division of Gynecologic Oncology, Department of Obstetrics and Gynecology, California Pacific Medical Center, San Francisco, CA (USA)
5 Department of Biochemistry and Molecular Biology, College of Medicine, National Taiwan University, Taipei (Taiwan)
Eur. J. Gynaecol. Oncol. 2010, 31(1), 55–62;
Published: 10 February 2010
Background: Screening in ovarian cancer is progressively finding out candidate genes and proteins which may work as screening biomarkers and play a role in tumor progression. We examined the protein expression patterns of ovarian cancer tissues using twodimensional gel electrophoresis (2-DE) and matrix-assisted laser desorption/ionization-time of fight mass spectrometry (MALDITOF MS). Methods: Tissues from 36 ovarian cancers and 20 normal ovaries were examined by 2-DE. The images of silver stained gels were analyzed by ImageMaster 2D Elite. The peptide mixtures, after in-gel digestion, were determined by MALDI-TOF MS for fingerprinting. The de-isotope tryptic peptide profiles were matched by using the Mascot search engine based on the entire NCBI and Swiss-Prot protein databases. Western/dot blots were then applied to verify the findings. Results: In ovarian cancer, 12 proteins that showed differential expressions were identified unequivocally. Among these proteins, five proteins (galectin-1, cathepsin B, ubiquitin carboxy-terminal hydrolase L1, HLA class II antigen DRB1-11 and heat shock protein 27) were up-regulated and seven proteins (cellular retinol-binding protein, transthyretin, SH3 binding glutamic-rich-like protein, tubulin-specific chaperone A, DJ-1, gammaactin and tropomyosin 4) were down-regulated. Conclusion: The present study is the first to report the up-regulation of ubiquitin carboxy- terminal hydrolase L1 and the down-regulation of SH3 binding glutamic-rich-like protein, tubulin-specific chaperone A, and tropomyosin 4 in human ovarian cancer tissues. Further cloning and functional analysis of these salient proteins will provide more information on their pathophysiologic roles in ovarian cancer.
Two-dimensional gel electrophoresis
Matrix-assisted laser desorption/ionization-time of fight mass spectrometry