Detection and partial purification of a 30 kDa ovarian carcinoma-associated protein
In an effort to identify novel ovarian tumor markers, we have attempted to detect proteins expressed and secreted from human ovarian cancer cells but not expressed from normal human ovarian epithelial cells. Human ovarian cancer cells and normal ovarian epithelial cells were metabolically radiolabeled in culture with [35S]-methionine. Proteins in the supernatants of the two culture types were visually compared by two-dimensional gel electrophoresis. A 30 kDa protein (p30) with pI ~6.1 was observed to be expressed by all of the cancer cell lines but not by cultured normal ovarian epithelia as detected by denaturing 2D electrophoresis. The p30 was partially purified using a combination of filtration, differential precipitation, gel filtration chromatography, and ion exchange chromatography. Under non-denaturing conditions the p30 protein was purified as a complex at 60 kDa and 90 kDa, suggesting a native structure of homodimers and homotrimers. These studies provide evidence that a p30 protein is differentially expressed and secreted by malignant ovarian epithelia compared to normal ovarian epithelia. This protein deserves further evaluation as a potential tumor marker.
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- Oncology & Carcinogenesis
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Published In
ISSN
Publication Date
Volume
Issue
Start / End Page
Related Subject Headings
- Oncology & Carcinogenesis