World J Mens Health.
2022 Oct;40(4):608-617. 10.5534/wjmh.210165.
Comparative Analysis of Proteomes and Phosphoproteomes in Patients with Prostate Cancer Using Different Surgical Conditions
- Affiliations
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- 1Asan Institute for Life Sciences, Asan Medical Center, Seoul, Korea
- 2Convergence Medicine Research Center, Asan Institute for Life Sciences, Seoul, Korea
- 3Department of Biomedical Sciences, University of Ulsan College of Medicine, Asan Medical Center, Seoul, Korea
- 4Department of Pathology, Seegene Medical Foundation, Seoul, Korea
- 5Department of Urology, Dongnam Institute of Radiological & Medical Sciences Cancer Center, Busan, Korea
- 6Department of Urology, College of Medicine, Pusan National University, Busan, Korea
- 7Department of Urology, Inje University Busan Paik Hospital, Inje University College of Medicine, Busan, Korea
- 8Department of Internal Medicine, School of Medicine, Pusan National University, Busan, Korea
- 9Department of Pharmacology, School of Medicine, Pusan National University, Busan, Korea
- 10Digestive Diseases Research Center, University of Ulsan College of Medicine, Seoul, Korea
- 11Bio-Medical Institute of Technology, Asan Medical Center, Seoul, Korea
- 12Biomedical Research Institute, Pusan National University Hospital, Busan, Korea
- KMID: 2537109
- DOI: http://doi.org/10.5534/wjmh.210165
Abstract
- Purpose
To establish the standard of procedure in preparing benign and cancerous prostate tissues and evaluate the quality of proteomics and phosphoproteomics during transurethral resection of the prostate (TUR-P) with different surgical conditions.
Materials and Methods
TUR-P tissue samples from three patients, two diagnosed with prostate cancer and one with benign prostatic hyperplasia, were each analyzed under three different conditions, based on differences in energy values, tissue locations, and surgical techniques. Global- and phosphorylated proteomic profiles of prostate tissues were analyzed by liquid chromatography-tandem mass spectrometry.
Results
A total of 6,019 global proteins and 4,280 phosphorylated peptides were identified in the nine tissues. The quantitative distributions of proteins and phosphorylation in tissues from the same patient were not affected by changes in the surgical conditions, but indirect relative comparisons differed among patients. Phosphorylation levels, especially of proteins involved in the androgen receptor pathway, important in prostate cancer, were preserved in each patient.
Conclusions
Proteomic profiles of prostate tissue collected by TUR-P were not significantly affected by energy levels, tissue location, or surgical technique. In addition, since protein denaturation of samples through TUR-P is rarely confirmed in this study, we think that it will be an important guide for tissue samples in castration resistant prostate cancer patients, where it is difficult to obtain tissue. This result is the first report about proteomic and phosphoproteomic results with TUR-P samples in prostate cancer and will be theoretical basis in protein analysis research with prostate cancer tissues.
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