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Identification of plasma protein markers for the early detection of ovarian cancer
Summary
We seek to identify novel circulating markers of ovarian cancer using proteomics technologies. Ongoing work includes identification and validation studies for development of a screening test to detect early-stage cancers.
Project Description
Ovarian cancer is currently one of the most common causes of cancer-related mortality for women. This is because most ovarian cancer patients have very few recognizable symptoms are diagnosed at a late stage, when the cancer has already spread to other parts of the body.
Survival for patients diagnosed with ovarian cancers diminishes rapidly as the cancer becomes more advanced. Early treatment, while the tumor is still confined to the ovary, provides the best prognosis for a full recovery. Unlike breast or cervical cancer, however, there is currently no suitable way to screen women regularly for ovarian tumors. The currently known molecular markers of ovarian cancer lack suitable sensitivity and specificity to be useful.
Our team, in collaboration with the Ovarian Cancer Research Foundation, is applying new proteomics technologies to identify proteins found in biological fluids that may be useful in the development of an early stage screening test for ovarian cancer. The ultimate goal of our research is a routine diagnostic screening test that is able to detect cancers in their earliest stages. Early detection will significantly increase patient survival from this disease.
Funding
Ovarian Cancer Research Foundation
Victorian Cancer Agency
Outcomes
Developed nanoparticle-based technology for the capture and comparative analysis of very small peptides and proteins
Identified several novel, auto-antigenic proteins in cancer patients that may prove useful in a diagnostic context
Identified a panel of novel potential biomarkers of ovarian cancer for validation
Selected Publications
Adam Rainczuk, Katie Meehan, David L. Steer, Peter G. Stanton, David M. Robertson and Andrew N. Stephens (2009). An Optimized Procedure for the Capture, Fractionation and Proteomic Analysis of Proteins Using Hydrogel Nanoparticles. Proteomics (submitted)
Chen J, Hannan N, Mak Y, Nicholls P, Zhang J, Rainczuk A, Stanton P, Robertson D, Salamonsen L, Stephens AN. (2009). Proteomic Characterization of Mid-Proliferative and Mid-Secretory Human Endometrium. J Proteome Res in press
Hannan NJ, Stoikos CJ, Stephens AN, Salamonsen LA (2009). Depletion of high-abundance serum proteins from human uterine lavages enhances detection of lower-abundance proteins. J Proteome Res. 8(2) pp.1099-1013.
Salamonsen, L.A., Rombauts, L., and Stephens, A.N. (2008) Genomic and proteomic approaches to the study of endometriosis. World Endo. Soc. Journal 10 (3) pp.5-8
Stephens, A.N., Quach, P., Harry, E.J. (2005). A streamlined approach to high throughput proteomics. Expert Rev. Proteomics 2 pp. 173-185
Holland JW, Meehan KL, Redmond SL, Dawkins HJ. Purification of the Keratan Sulfate proteoglycan expressed in prostatic secretory cells and its identification as lumican. The Prostate 2004; 59(3):252-9.
Meehan K, and Sadar, M. Quantitative profiling of LNCaP prostate cancer cells using isotope-coded affinity tags and mass spectrometry. Proteomics 2004; 4(4):1116-34.
Meehan K, Holland J, Dawkins HJ. Identification of differentially expressed proteins in the proteome of normal prostate compared with malignant prostate. The Prostate 2002; 50(1):54-63.