Abstract |
Endometrial carcinoma is a common malignancy in women, being exceeded in incidence only by that of breast, lung, and colorectal cancers. At present, no serum tumor markers are available for the monitoring of endometrial carcinoma patients, and patients with recurrent disease are detected only following the development of symptoms or abnormalities in imaging assessments. Similarly, no screening tools are available for endometrial carcinoma. Protein profiling by matrix-assisted laser desorption/ionization-time-of-flight mass spectrometry (MALDI-TOF MS) has proven to be a sensitive and fast method of analysis for small proteins or peptides to yield specific biomarkers. In this study, a variety of normal and malignant endometrial tissue samples were fractionated and analyzed by SELDI-TOF MS (SELDI is a version of MALDI utilizing protein "chips"). A number of proteins displayed differential expression in malignant endometrial tissues. One of the prominent proteins fractionated by weak cation exchange chromatography and displaying enhanced expression in these malignant tissues was identified as chaperonin 10. The increased expression of chaperonin 10 in malignant endometrial tissues was further confirmed by parallel Western blot and immunohistochemistry analyses.
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Authors | Eric C C Yang, Jingzhong Guo, Georg Diehl, Leroi DeSouza, Mary Joe Rodrigues, Alexander D Romaschin, Terence J Colgan, K W Michael Siu |
Journal | Journal of proteome research
(J Proteome Res)
2004 May-Jun
Vol. 3
Issue 3
Pg. 636-43
ISSN: 1535-3893 [Print] United States |
PMID | 15253447
(Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
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Chemical References |
- Biomarkers, Tumor
- Chaperonin 10
- Proteome
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Topics |
- Biomarkers, Tumor
(blood, chemistry)
- Chaperonin 10
(metabolism)
- Endometrial Neoplasms
(metabolism)
- Female
- Gene Expression Regulation, Neoplastic
(genetics)
- Humans
- Immunohistochemistry
- Proteome
- Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
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