期刊
WORLD JOURNAL OF MENS HEALTH
卷 40, 期 4, 页码 608-617出版社
KOREAN SOC SEXUAL MEDICINE & ANDROLOGY
DOI: 10.5534/wjmh.210165
关键词
Mass spectrometry; Prostatic hyperplasia; Prostatic neoplasm; Proteme; Transurethral resection of prostate
资金
- National Cancer Center, Korea [NCC-1810861]
- National Research Foundation (NRF) - Korean government (MSIT) [NRF-2019M3E5D3073369]
- Ministry of Education [2021R1A6A1A03040260]
- Pusan National University Hospital [PJ015336012021]
This study establishes the standard procedure for preparing prostate tissues and evaluates the quality of proteomics and phosphoproteomics during transurethral resection of the prostate (TUR-P) with different surgical conditions. The results show that the proteomic profiles of prostate tissue collected by TUR-P are not significantly affected by energy levels, tissue location, or surgical technique. This study provides important guidance for tissue samples in castration resistant prostate cancer patients where it is difficult to obtain tissue.
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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