Down-regulation of estrogen receptor-α in MCF-7 human breast cancer cells after proteasome inhibition

Biochemical Pharmacology

Volumn 72, Issue 5, 2006, Pages 566-572

  Balan, Kannan V ^a   Wang, Yongbao ^b   Chen, Siming W ^c   Pantazis, Panayotis ^d   Wyche, James H ^d   Han, Zhiyong ^d  

^a CASE WESTERN RESERVE UNIVERSITY   (United States)

^b UNIVERSITY OF MINNESOTA MEDICAL SCHOOL   (United States)

^c WEILL CORNELL MEDICAL COLLEGE   (United States)

^d UNIVERSITY OF OKLAHOMA COLLEGE OF MEDICINE   (United States)

Author keywords

Estrogen; Estrogen receptor down regulation; Inhibitor; Proteasome

Indexed keywords

BENZYLOXYCARBONYLLEUCYLLEUCYLLEUCINAL; CHYMOTRYPSIN; ESTRADIOL; ESTROGEN RECEPTOR; ESTROGEN RECEPTOR ALPHA; PROTEASOME; TAMOXIFEN;

ARTICLE; BREAST CANCER; CANCER CELL CULTURE; CANCER INHIBITION; CELL STRAIN MCF 7; CONTROLLED STUDY; ENZYME ACTIVITY; ESTROGEN ACTIVITY; HUMAN; HUMAN CELL; PRIORITY JOURNAL; PROTEIN SYNTHESIS REGULATION; RECEPTOR DOWN REGULATION; STEADY STATE;

BREAST NEOPLASMS; CELL LINE, TUMOR; DOWN-REGULATION; ESTROGEN RECEPTOR ALPHA; ESTROGENS; HUMANS; PROTEASE INHIBITORS; PROTEASOME ENDOPEPTIDASE COMPLEX; TAMOXIFEN;

EID: 33746664214     PISSN: 00062952     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bcp.2006.05.012     Document Type: Article

References (34)

1. Mhyre A.J., and Dorsa D.M. Estrogen activates rapid signaling in the brain: role of estrogen receptor alpha and estrogen receptor beta in neurons and glia. Neuroscience 138 (2006) 851-858
2. Hisamoto K., and Bender J.R. Vascular cell signaling by membrane estrogen receptors. Steroids 70 (2005) 382-387
3. Christgau S., and Cloos P.A. Sex hormones in the regulation of bone and cartilage metabolism: an old paradigm and a new challenge. Minerva Ginecol 57 (2005) 611-617
4. Chatterton Jr. R.T. Mammary gland: development and secretion. Obstet Gynecol Annu 7 (1978) 303-324
5. Nilsson S., Makela S., Treuter E., Tujague M., Thomsen J., Andersson G., et al. Mechanisms of estrogen action. Physiol Rev 81 (2001) 1535-1565
6. Kong E.H., Pike A.C., and Hubbard R.E. Structure and mechanism of the oestrogen receptor. Biochem Soc Trans 31 (2003) 56-59
7. Ruff M., Gangloff M., Wurtz J.M., and Moras D. Estrogen receptor transcription and transactivation: structure-function relationship in DNA- and ligand-binding domains of estrogen receptors. Breast Cancer Res 2 (2000) 353-359
8. Klinge C.M. Estrogen receptor interaction with co-activators and co-repressors. Steroids 65 (2000) 227-251
9. Osborne C.K., and Schiff R. Estrogen-receptor biology: continuing progress and therapeutic implications. J Clin Oncol 23 (2005) 1616-1622
10. Creasman W.T. Estrogen and cancer. Gynecol Oncol 86 (2002) 1-9
11. Simpson P.T., Reis-Filho J.S., Gale T., and Lakhani S.R. Molecular evolution of breast cancer. J Pathol 205 (2005) 248-254
12. Deroo B.J., and Korach K.S. Estrogen receptors and human disease. J Clin Invest 116 (2006) 561-570
13. Ciechanover A., Orian A., and Schwartz A.L. Ubiquitin-mediated proteolysis: biological regulation via destruction. Bioessays 22 (2000) 442-451
14. Glickman M.H., and Ciechanover A. The ubiquitin-proteasome proteolytic pathway: destruction for the sake of construction. Physiol Rev 82 (2002) 373-428
15. Lee D.H., and Goldberg A.L. Proteasome inhibitors: valuable new tools for cell biologists. Trends Cell Biol 8 (1998) 397-403
16. Kisselev A.F., and Goldberg A.L. Proteasome inhibitors: from research tools to drug candidates. Chem Biol 8 (2001) 739-758
17. Myung J., Kim K.B., and Crews C.M. The ubiquitin-proteasome pathway and proteasome inhibitors. Med Res Rev 21 (2001) 245-273
18. Rock K.L., Gramm C., Rothstein L., Clark K., Stein R., Dick L., et al. Inhibitors of the proteasome block the degradation of most cell proteins and the generation of peptides presented on MHC class I molecules. Cell 78 (1994) 761-771
19. Dick L.R., Cruikshank A.A., Grenier L., Melandri F.D., Nunes S.L., and Stein R.L. Mechanistic studies on the inactivation of the proteasome by lactacystin: a central role for clasto-lactacystin beta-lactone. J Biol Chem 271 (1996) 7273-7276
20. Dick L.R., Cruikshank A.A., Destree A.T., Grenier L., McCormack T.A., Melandri F.D., et al. Mechanistic studies on the inactivation of the proteasome by lactacystin in cultured cells. J Biol Chem 272 (1997) 182-188
21. Meng L., Kwok B.H., Sin N., and Crews C.M. Eponemycin exerts its antitumor effect through the inhibition of proteasome function. Cancer Res 59 (1999) 2798-2801
22. Sin N., Kim K.B., Elofsson M., Meng L., Auth H., Kwok B.H., et al. Total synthesis of the potent proteasome inhibitor epoxomicin: a useful tool for understanding proteasome biology. Bioorg Med Chem Lett 9 (1999) 2283-2288
23. Elofsson M., Splittgerber U., Myung J., Mohan R., and Crews C.M. Towards subunit-specific proteasome inhibitors: synthesis and evaluation of peptide alpha′,beta′-epoxyketones. Chem Biol 6 (1999) 811-822
24. Myung J., Kim K.B., Lindsten K., Dantuma N.P., and Crews C.M. Lack of proteasome active site allostery as revealed by subunit-specific inhibitors. Mol Cell 7 (2001) 411-420
25. Han Z., Pantazis P., Wyche J.H., Kouttab N., Kidd V.J., and Hendrickson E.A. A Fas-associated death domain protein-dependent mechanism mediates the apoptotic action of non-steroidal anti-inflammatory drugs in the human leukemic Jurkat cell line. J Biol Chem 276 (2001) 38748-38754
26. He D.C., Nickerson J.A., and Penman S. Core filaments of the nuclear matrix. J Cell Biol 10 (1990) 569-580
27. Brandeis M., and Hunt T. The proteolysis of mitotic cyclins in mammalian cells persists from the end of mitosis until the onset of S phase. EMBO J 15 (1996) 5280-5289
28. Casanovas O., Jaumot M., Paules A.B., Agell N., and Bachs O. P38SAPK2 phosphorylates cyclin D3 at Thr-283 and targets it for proteasomal degradation. Oncogene 23 (2004) 7537-7544
29. Traenckner E.B., Wilk S., and Baeuerle P.A. A proteasome inhibitor prevents activation of NF-kappa B and stabilizes a newly phosphorylated form of I kappa B-alpha that is still bound to NF-kappa B. EMBO J 13 (1994) 5433-5441
30. Flinn E.M., Busch C.M., and Wright A.P. myc boxes, which are conserved in myc family proteins, are signals for protein degradation via the proteasome. Mol Cell Biol 18 (1998) 5961-5969
31. Wijayaratne A.L., Nagel S.C., Paige L.A., Christensen D.J., Norris J.D., Fowlkes D.M., et al. Comparative analyses of mechanistic differences among antiestrogens. Endocrinology 140 (1999) 5828-5840
32. Wijayaratne A.L., and McDonnell D.P. The human estrogen receptor-alpha is a ubiquitinated protein whose stability is affected differentially by agonists, antagonists, and selective estrogen receptor modulators. J Biol Chem 276 (2001) 35684-35692
33. Preisler-Mashek M.T., Solodin N., Stark B.L., Tyriver M.K., and Alarid E.T. Ligand-specific regulation of proteasome-mediated proteolysis of estrogen receptor-alpha. Am J Physiol Endocrinol Metab 282 (2002) E891-E898
34. Shao W., Keeton E.K., McDonnell D.P., and Brown M. Coactivator AIB1 links estrogen receptor transcriptional activity and stability. Proc Natl Acad Sci USA 101 (2004) 11599-11604