High molecular mass proteome of androgen independent prostate cancer

• Kuruma Hidetoshi

  Department of Urology, Kitasato University School of Medicine

• Egawa Shin

  Department of Urology, Kitasato University School of Medicine

• Oh-Ishi Masamichi

  Department of Physics, Kitasato University School of Science

• Kodera Yoshio

  Department of Physics, Kitasato University School of Science

• Satoh Mamoru

  Department of Physics, Kitasato University School of Science

• Chen Weigiang

  Department of Urology, Kitasato University School of Medicine

• Baba Shiro

  Department of Urology, Kitasato University School of Medicine

• Maeda Tadakazu

  Department of Physics, Kitasato University School of Science

Bibliographic Information

Other Title

• アンドロゲン非依存性前立腺癌の高分子量プロテオーム

Abstract

We studied comprehensive protein expression in human prostate cancer cells, LNCaP, borne in male nude mice by using an agarose 2-DE method followed by LC-MS/MS. The agarose 2-DE being good at separating high molecular mass (HMM) proteins and alkaline ones, we successfully revealed differences between proteomes of androgen dependent and independent cancers especially in HMM regions larger than 80 kDa. About 500 of proteins separated by the 2-DE method were visualized in a Coomassie-stained 2-DE gel, and the staining intensities of respective protein spots enabled us to infer contents of the proteins in the tumors. We successfully identified 295 proteins (91.0%) out of 324 spots excised in total. Sixty-two among the 295 proteins being redundant, we obtained a non-redundant set of 233 proteins, among which eight were mouse proteins. Excluding these eight mouse-derived proteins, we considered remaining 225 proteins to be related to the cancer. We divided the 225 cancer-related proteins into HMM and LMM (low molecular mass) groups by their molecular mass above or below 80 kDa, the former group contained 84 HMM proteins and the latter 141 LMM ones. Functional classification of the proteins in these two groups showed clear differences between the two: More than half (54.8%) of the HMM proteins but less than one-third (29.1%) of the LMM ones were classified among transcription/translation related proteins. The biggest fraction (29.8%) of the LMM group was metabolism related proteins. Eighteen proteins changed in content when the tumor progressed from androgen dependent to independent states. Five of these proteins had a function to protect cells against oxidant stress induced apoptosis. In conclusion, HMM proteome of androgen independent prostate cancer provided critical information to understand its progression. Besides, some of identified proteins would be candidates for new biomarkers or therapeutic targets.

Journal

• Abstracts for Annual Meeting of Japanese Proteomics Society

  Abstracts for Annual Meeting of Japanese Proteomics Society 2004 (0), 115-115, 2004

  Japanese Proteomics Society (Japan Human Proteome Organisation)

Keywords

• high molecular mass proteome
• prostate cancer
• androgen independent
• agarose two-dimensional electrophoresis
• oxidative stress

Details

• CRID: 1390282680610406656
• NII Article ID: 130006995824
• DOI: 10.14889/jhupo.2004.0.115.0
• Data Source:
  • JaLC
  • CiNii Articles
• Abstract License Flag: Disallowed