Interplay of protein misfolding pathway and unfolded-protein response in acute promyelocytic leukemia

Expert Review of Proteomics

Volumn 7, Issue 4, 2010, Pages 591-600

  Khan, Matiullah ^a  

^a Dept Medicine Endocrinol Diabet   (Singapore)

Author keywords

acute promyelocytic leukemia; genistein; molecular target; nuclear receptor corepressor; promyelocytic leukemia retinoic acid receptor; protein misfolding

Indexed keywords

NUCLEAR RECEPTOR COREPRESSOR; RETINOIC ACID RECEPTOR;

HUMAN; LOSS OF FUNCTION MUTATION; MALIGNANT NEOPLASTIC DISEASE; PATHOGENESIS; PROMYELOCYTIC LEUKEMIA; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN FUNCTION; QUALITY CONTROL; REVIEW;

ANIMALS; HUMANS; LEUKEMIA, PROMYELOCYTIC, ACUTE; NUCLEAR RECEPTOR CO-REPRESSOR 1; ONCOGENE PROTEINS, FUSION; PROTEIN FOLDING;

EID: 77955002491     PISSN: 14789450     EISSN: 17448387     Source Type: Journal    
DOI: 10.1586/epr.10.38     Document Type: Review

References (47)

1. Gregersen N, Bross P, Vang S et al. Protein misfolding and human diseases. Annu. Rev. Genomics Hum. Genet. 7, 103-124 (2006).
2. Jahn TR, Radford SE. The yin and yang of protein folding. FEBS J. 272, 5962-5970 (2005).
3. Kakizuka A, Miller WH, Umesono K et al. Chromosomal translocation t(15;17) in human acute promyelocytic leukemia fuses RAR a with a novel putative transcription factor, PML. Cell 66, 663-674 (1991).
4. de The H, Lavau C, Marchio A et al. The PML-RAR a fusion mRNA generated by the t(15;17) translocation in acute promyelocytic leukemia encodes a functionally altered RAR. Cell 66, 675-684 (1991).
5. Dyck JA, Maul GG, Miller WH et al. A novel macromolecular structure is a target of the promyelocyte-retinoic acid receptor oncoprotein. Cell 76, 333-343 (1994).
6. Weis K, Rambaud S, Lavau C et al. Retinoic acid regulates aberrant nuclear localization of PML-RAR a in acute promyelocytic leukemia cells. Cell 76, 345-356 (1994).
7. Lehming N, Le Saux A, Schüller J et al. Chromatin components as part of a putative transcriptional repressing complex. Proc. Natl Acad. Sci. USA 95, 7322-7326 (1998).
8. Boisvert FM, Hendzel MJ, Bazett-Jones DP et al. Promyelocytic leukemia (PML) nuclear bodies are protein structures that do not accumulate RNA. J. Cell Biol. 148, 283-292 (2000).
9. Khan MM, Nomura T, Kim H et al. Role of PML and PML-RARa in Mad-mediated transcriptional repression. Mol. Cell 6, 1233-1243 (2001).
10. Lin RJ, Nagy L, Inoue S et al. Role of the histone deacetylase complex in acute promyelocytic leukaemia. Nature 391, 811-814 (1998).
11. Grignani F, De Matteis S, Nervi C et al. Fusion proteins of the retinoic acid receptor-a recruit histone deacetylase in promyelocytic leukaemia. Nature 391, 815-818 (1998).
12. Degos L, Dombret H, Chomienne C et al. Alltrans retinoic acid as a differentiating agent in the treatment of acute promyelocytic leukemia. Blood 85, 2643-2653 (1995).
13. Degos L, Wang ZY. All trans retinoic acid in acute promyelocytic leukemia. Oncogene 20, 7140-7145 (2001).
14. Kopf E, Plassat JL, Vivat V et al. Dimerization with retinoid X receptors and phosphorylation modulate the retinoic acid-induced degradation of retinoic acid receptors a and g through the ubiquitin-proteasome pathway. J. Biol. Chem. 275, 33280-33288 (2000).
15. Zhu J, Gianni M, Kopf E et al. Retinoic acid induces proteasome-dependent degradation of retinoic acid receptor a (RAR a) and oncogenic RAR a fusion proteins. Proc. Natl Acad. Sci. USA 96, 14807-14812 (1999).
16. Rosenbauer F, Tenen DG. Transcription factors in myeloid development: balancing differentiation with transformation. Nat. Rev. Immunol. 7, 105-117 (2007).
17. Florence CG, Meritxell AJ, Hideyo H et al. Identification of a myeloid committed progenitor as the cancer-initiating cell in acute promyelocytic leukemia. Blood 114, 5415-5425 (2009).
18. Wojiski S, Guibal FC, Kindler T et al. PML-RAR initiates leukemia by conferring properties of self-renewal to committed promyelocytic progenitors. Leukemia 23, 1462-1471 (2009).
19. Ng PPA, Howe FJ, Nin DS et al. Cleavage of mis-folded nuclear receptor co-repressor confers resistance to unfolded protein response-induced apoptosis. Cancer Res. 66, 9903-9912 (2006).
20. Hörlein AJ, Näär AM, Heinzel T et al. Ligand-independent repression by the thyroid hormone receptormediated by a nuclear receptor corepressor. Nature 377, 397-404 (1995).
21. Heinzel TRM, Lavinsky TM, Mullen M et al. A complex containing N-CoR, mSin3, and histone deacetylase mediates transcriptional repression. Nature 387, 43-48 (1997).
22. Perissi V, Jepsen K, Glass CK et al. Deconstructing repression: evolving models of co-repressor action Nat. Rev. Genet. 11, 109-123 (2010).
23. Battaglia S, Maguire O, Campbell MJ et al. Transcription factor co-repressors in cancer biology; roles and targeting. Int. J. Cancer 126, 2511-2529 (2010).
24. Jepsen K, Hermanson O, Onami TM et al. Combinatorial roles of the nuclear receptor co-repressor in transcription and development. Cell 102, 753-763 (2000)
25. Khan MM, Nomura T, Kim H et al. Role of PML and PML-RARa in Mad-mediated transcriptional repression. Mol. Cell 6, 1233-1243 (2001).
26. Nomura T, Khan M M, Kual SC et al. Ski is a component of the histone deacetylase complex required for transcriptional repression mediated by Mad and thyroid hormone receptor. Genes Dev. 13, 412-423 (1999).
27. Zada AA, Pulikkan JA, Bararia D et al. Proteomic discovery of Max as a novel interacting partner of C/EBPa: a Myc/Max/Mad link. Leukemia 20, 2137-2146 (2006).
28. Zhang D, Ellen CE, Wong J et al. A critical role for the co-repressor N-CoR in erythroid differentiation and heme synthesis. Cell Res. 17, 804-814 (2007).
29. Khan MM, Nomura T, Chiba T et al. The fusion onco-protein PML-RAR induces endoplasmic reticulum associated degradation of N-CoR and ER stress. J. Biol. Chem. 279, 11814-11824 (2004).
30. Zhong S, Delva L, Rachez C et al. A RA-dependent tumor-growth suppressive transcription complex is the target of the PML/RARa and T18 oncoproteins. Nat. Genet. 23, 287-295 (1999).
31. Ferrucci PR, Grignani F, Pearson M et al. Cell death induction by the acute promyelocytic leukemia-specific PML-RAR fusion protein. Proc. Natl Acad. Sci. USA 94, 10901-10916 (1997).
32. Grisolano JL, Wesselschmidt RL, Pelicci PG et al. Altered myeloid development and acute leukemia in transgenic mice expressing PML-RAR under control of cathepsin G regulatory sequences. Blood 89, 376-387 (1997).
33. He LZ, Tribioli C, Rivi R et al. Acute leukemia promyelocytic features in PML-RAR transgenic mice. Proc. Natl Acad. Sci. USA 94, 5302-5307 (1997).
34. Westervelt P, Lane AA, Pollock JL et al. High penetrance mouse model of acute promyelocyticleukemia with very low levels of PML-RAR expression. Blood 102, 1857-1865 (2003).
35. Early EMA, Moore A, Kakizuka K et al. Transgenic expression of PML/RAR impairs myelopoiesis. Proc. Natl. Acad. Sci. USA 93, 7900-7904 (1996).
36. Minucci SS, Monestiroli S, Giavara et al. PML-RAR induces promyelocytic leukemia with high efficiency following retroviral gene transfer into purified murine hematopoietic progenitors. Blood 100, 2989-2995 (2002).
37. Lane AA, Ley TJ. Neutrophil elastase cleaves PML-RARa and is important for the development of acute promyelocytic leukemia in mice. Cell 115, 305-318 (2003).
38. Lane AA, Ley TJ. Neutrophil elastase is important for PML-retinoic acid receptor activities in early myeloid cells. Mol. Cell. Biol. 25, 23-33 (2005).
39. Yanjun M, Hendershot LM. The role of the unfolded protein response in tumor development: friend or foe? Nat. Rev. Cancer 4, 966-977 (2004).
40. Kaufman RJ. Orchestrating the unfolded protein responses in health and diseases. J. Clin. Invest. 110, 1389-1398 (2002).
41. Ng PPA, Nin DS, Howe FJ et al. Therapeutic targeting of nuclear receptor co-repressor (N-CoR) mis-folding in acute promyelocytic leukemia (APL) cells with genistein. Mol. Cancer Ther. 6, 2240-2248 (2007).
42. Zhou Y, Lee AS. Mechanism for the suppression of the mammalian stress response by genstein, an anticancer phytoestrogen from soy. J. Natl Cancer Inst. 90, 381-388 (1998).
43. Akiyama T, Ishida J, Nakagawa S et al. Genistein, a specific inhibitor of tyrosine specific protein kinase. J. Biol. Chem. 262, 5592-5595 (1987).
44. Green NS, Foss TR, Kelly JW et al. Genistein, a natural product from soy, is a potent inhibitor of transthyretin amyloidosis. Proc. Natl Acad. Sci. USA 102, 14545-14550 (2005).
45. Carrel RW, Lomas DA. a1-antitrypsin deficiency: a model for conformational disease. N. Engl. J. Med. 346, 45-53 (2002).
46. Zylicz M, King FW, Wawrzynow A et al. HSP70 interaction with the p53 tumour suppressor protein. EMBO J. 20, 4634-4638 (2001).
47. Williams RS, Chasman DI, Hau DD et al. Detection of protein folding defects caused by BRCA1-BRCT truncation and missense mutations. J. Biol. Chem. 278, 53007-53016 (2003).