Over-expression of genes and proteins of ubiquitin specific peptidases (USPs) and proteasome subunits (PSs) in breast cancer tissue observed by the methods of RFDD-PCR and proteomics
- 27 September 2006
- journal article
- Published by Springer Nature in Breast Cancer Research and Treatment
- Vol. 104 (1) , 21-30
- https://doi.org/10.1007/s10549-006-9393-7
Abstract
The ubiquitin–proteasome system facilitates the degradation of damaged proteins and regulators of growth and stress response. Alterations in this proteolytic system are associated with a variety of human pathologies. By restriction fragment differential display polymerase chain reaction (RFDD-PCR) and matrix-assisted laser desorption/ionization tandem time-of-flight mass spectrometry (MALDI-TOF-TOF MS) based on two-dimensional polyacrylamide gel electrophoresis (2-DE), differentially expressed genes and proteins of ubiquitin specific proteases (USPs), proteasome subuinits (PSs) and ubiquitin protein ligase E3A (UBE3A) were analyzed between breast cancer and adjacent normal tissues. Some of them were further verified as over-expression by immunohistochemical stain. Five genes of proteasome subunits (PSs), including PSMB5, PSMD1, PSMD2, PSMD8 and PSMD11, four genes of USPs, including USP9X, USP9Y, USP10 and USP25, and ubiquitin protein ligase E3A (UBE3A) were over-expressed (>3-fold) in breast cancer tissue compared to adjacent normal tissue, and over-expression (>4-fold) of proteins of PSMA1 and SMT3A were observed in breast cancer tissue. PSMD8, PSMD11 and UBE3A were further verified as over-expression by immunohistochemical stain. The action of ubiquitin–proteasome system were obviously enhanced in breast cancer, and selectively intervention in action of ubiquitin–proteasome system may be a useful method of treating human breast cancer.Keywords
This publication has 39 references indexed in Scilit:
- Genomic and functional profiling of duplicated chromosome 15 cell lines reveal regulatory alterations in UBE3A-associated ubiquitin–proteasome pathway processesHuman Molecular Genetics, 2006
- The Processivity of Multiubiquitination by the APC Determines the Order of Substrate DegradationCell, 2006
- Intracellular Protein Degradation: From a Vague Idea, through the Lysosome and the Ubiquitin–Proteasome System, and onto Human Diseases and Drug Targeting (Nobel Lecture)Angewandte Chemie International Edition in English, 2005
- Inducible expression of a degradation-resistant form of p27Kip1 causes growth arrest and apoptosis in breast cancer cellsFEBS Letters, 2005
- The Deubiquitinating Enzyme USP1 Regulates the Fanconi Anemia PathwayMolecular Cell, 2005
- COP1, the Negative Regulator of p53, Is Overexpressed in Breast and Ovarian AdenocarcinomasCancer Research, 2004
- The Comparative Proteomics of Ubiquitination in MouseGenome Research, 2003
- Ras–GAP SH3 domain binding protein (G3BP) is a modulator of USP10, a novel human ubiquitin specific proteaseOncogene, 2001
- USP25, a Novel Gene Encoding a Deubiquitinating Enzyme, Is Located in the Gene-Poor Region 21q11.2Genomics, 1999
- Structure of 20S proteasome from yeast at 2.4Å resolutionNature, 1997