BTG2 Antiproliferative Gene and Prostate Cancer
Abstract
Levels of the BTG2 tumor suppressor protein diminish during the transition of normal prostate epithelial cells into prostate cancer cells and restoration of BTG2 expression in prostate cancer cells significantly reduces cell proliferation and tumorigenicity. Our working hypothesis being tested is that the tumor suppressive activity of BTG2 is diminished as an early event in prostate carcinogenesis due to increased proteasomal degradation, leading to compromised cell cycle regulation, increased cell invasion and cancer progression. To date we have shown that BTG2 protein expression is lost as a very early event in prostate cancer and that prostate cancer tissue and cells degrade BTG2 at a greater rate than non-cancer tissue and cells. We have also shown that BTG2 has a predominantly nuclear localization consistent with its antiproliferative function, but that BTG2 is transiently sequestered in the nucleolus at 4 hours following growth stimulation of quiescent cells indicating that BTG2 might additionally influence some aspect of ribosome biosynthesis. In the present reporting period we have shown that steady state levels of BTG2 during the cell cycle are influenced by changes in BTG2 ubiquitination (consistent with proteasomal degradation) and not by changes in the level of the deubiquitinating enzyme USP4.
Document Details
- Document Type
- Technical Report
- Publication Date
- Feb 01, 2007
- Accession Number
- ADA470017
Entities
People
- Paul D. Walden
Organizations
- New York University