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.

作者: Shishan Deng , Hongying Zhou , Ruohong Xiong , Youguang Lu , Dazhong Yan

DOI: 10.1007/S10549-006-9393-7

关键词: Molecular biologyCancerGene expressionProteasomeUbiquitin-Protein Ligase E3APSMB5ProteomicsUSP9XUbiquitinBiology

摘要: The ubiquitin-proteasome system facilitates the degradation of damaged proteins and regulators growth stress response. Alterations in this proteolytic are associated with a variety human pathologies. By restriction fragment differential display polymerase chain reaction (RFDD-PCR) 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 ubiquitin specific proteases (USPs), proteasome subuinits (PSs) protein ligase E3A (UBE3A) were analyzed between breast cancer adjacent normal tissues. Some them further verified as over-expression by immunohistochemical stain. Five subunits (PSs), including PSMB5, PSMD1, PSMD2, PSMD8 PSMD11, four USPs, USP9X, USP9Y, USP10 USP25, over-expressed (>3-fold) tissue compared to tissue, (>4-fold) PSMA1 SMT3A observed tissue. PSMD8, PSMD11 UBE3A action obviously enhanced cancer, selectively intervention may be useful method treating cancer.

参考文章(43)
H. D. Ulrich, Natural substrates of the proteasome and their recognition by the ubiquitin system. Current Topics in Microbiology and Immunology. ,vol. 268, pp. 137- 174 ,(2002) , 10.1007/978-3-642-59414-4_6
Christine Doucet, Gustavo J Gutierrez, Catherine Lindon, Thierry Lorca, Gwendaline Lledo, Christian Pinset, Olivier Coux, Multiple phosphorylation events control mitotic degradation of the muscle transcription factor Myf5. BMC Biochemistry. ,vol. 6, pp. 27- 27 ,(2005) , 10.1186/1471-2091-6-27
Mikael Altun, Paul J. Galardy, Reshma Shringarpure, Teru Hideshima, Richard LeBlanc, Kenneth C. Anderson, Hidde L. Ploegh, Benedikt M. Kessler, Effects of PS-341 on the Activity and Composition of Proteasomes in Multiple Myeloma Cells Cancer Research. ,vol. 65, pp. 7896- 7901 ,(2005) , 10.1158/0008-5472.CAN-05-0506
Maria L. Wrang, Flemming Møller, Carsten W. Alsbo, Nils H. Diemer, Changes in gene expression following induction of ischemic tolerance in rat brain: detection and verification. Journal of Neuroscience Research. ,vol. 65, pp. 54- 58 ,(2001) , 10.1002/JNR.1127
Qingxiu Zhang, Ling Tian, Abdel Mansouri, Anita L. Korapati, Terry J. Johnson, Francois X. Claret, Inducible expression of a degradation‐resistant form of p27Kip1 causes growth arrest and apoptosis in breast cancer cells FEBS Letters. ,vol. 579, pp. 3932- 3940 ,(2005) , 10.1016/J.FEBSLET.2005.06.012
Michael Groll, Lars Ditzel, Jan Löwe, Daniela Stock, Matthias Bochtler, Hans D. Bartunik, Robert Huber, Structure of 20S proteasome from yeast at 2.4 A resolution. Nature. ,vol. 386, pp. 463- 471 ,(1997) , 10.1038/386463A0
Sebastian M.B. Nijman, Tony T. Huang, Annette M.G. Dirac, Thijn R. Brummelkamp, Ron M. Kerkhoven, Alan D. D'Andrea, René Bernards, The Deubiquitinating Enzyme USP1 Regulates the Fanconi Anemia Pathway Molecular Cell. ,vol. 17, pp. 331- 339 ,(2005) , 10.1016/J.MOLCEL.2005.01.008
Colin AM Semple, Riken Ger Group, None, The comparative proteomics of ubiquitination in mouse. Genome Research. ,vol. 13, pp. 1389- 1394 ,(2003) , 10.1101/GR.980303