Bcl-2 Family Overexpression and Chemoresistance in Acute Myeloid Leukemia

de Melo Silva, Alex José

doi:10.2478/sjecr-2018-0064

Abstract

The family of Bcl-2 proteins is one of the most responsible for apoptosis pathway, that is a critical process to the maintenance of tissue homeostasis. Bcl-2 is an essential apoptotic regulator belonging to a family of functionally and structurally related proteins known as the Bcl-2 family. Some members of this family act as anti-apoptotic regulators, whereas others act in pro-apoptotic function. The relationship between the pro and anti-apoptotic proteins can regulate whether cells begin the apoptosis or remain its life cycle. Increasing of Bcl-2 expression has been found in some hematologic diseases, such as Acute Myeloid Leukemia (AML) and their effects on responsiveness to anticancer therapy have been recently described. Thus, this review aims to discuss apoptosis and the role of the Bcl-2 family of proteins in chemoresistance when overexpressed in patients committed with Acute Myeloid Leukemia submitted to chemotherapy treatment.

References

1. Abdel-Magid A. F. (2015). Inhibitors of the Antiapoptotic Myeloid Cell Leukemia-1 (Mcl-1) May Provide Effective Treatment for Cancer. ACS Medical Chemistry Letter, 6: 1171–1173. dx.doi.org/10.1021/acsmedchemlett.5b0043810.1021/acsmedchemlett.5b00438
Open DOI Search in Google Scholar Back to article
2. AlBakr R. B, Khojah O. T. (2014). Incidence Trend of the Leukemia Reported Cases in the Kingdom of Saudi Arabia, Observational Descriptive Statistic from Saudi Cancer Registry. International Journal Biomedical Research, 5(8).10.7439/ijbr.v5i8.736
Search in Google Scholar Back to article
3. Anderson M. A, Huang D, Robertsa A. 2014. Targeting BCL2 for the Treatment of Lymphoid Malignancies. Seminar of Hematolology, 51(3), 219–227.10.1053/j.seminhematol.2014.05.008
Search in Google Scholar Back to article
4. Marshall K. D & Baines C. P. 2014. Necroptosis: Is there a role for mitochondria? Frontier of Physiology, 5, 323.10.3389/fphys.2014.00323
Search in Google Scholar Back to article
5. Asif N, Hassan K. 2013. Acute Myeloid Leukemia amongst Adults. Journal of Islamabad Medical & Dentistry College (JIMDC), 2(4), 58-63.
Search in Google Scholar Back to article
6. Zhao H, Jaffer T, Eguchi S, Wang Z, Linkermann A, Ma D. (2015). Role of necroptosis in the pathogenesis of solid organ injury. Cell death and disease, 6, 1-10.10.1038/cddis.2015.316
Search in Google Scholar Back to article
7. Gozuacik D, Kimchi A. (2007). Autophagy and Cell Death. Current topics in developmental biology, 78, 217-245. https://doi.org/10.1016/S0070-2153(06)78006-110.1016/S0070-2153(06)78006-1
Open DOI Search in Google Scholar Back to article
8. Martin S. J, Henry C. M, Cullen S.P. (2012). A perspective on mammalian caspases as positive and negative regulators of inflammation. Molecular, 46(4), 387–397. doi: 10.1016/j.molcel.2012.04.026.2263348710.1016/j.molcel.2012.04.026
Search in Google Scholar Back to article
9. Mohana-Kumaran N, Hill D. S, Allen J. D, Haass N. K. (2014). Targeting the intrinsic apoptosis pathway as a strategy for melanoma therapy. Pigment Cell Melanoma Research, 4, 525-39. doi:10.1111/pcmr. 12242. Epub 2014.10.1111/pcmr.12242.Epub2014
Open DOI Search in Google Scholar Back to article
10. Hajji N. Joseph B. (2010). Epigenetic regulation of cell life and death decisions and deregulation in cancer. Essays in Biochemistry, 48, 121-146.10.1042/bse048012120822491
Search in Google Scholar Back to article
11. Hockenbery D. M. (1994). bcl-2 in cancer, development and apoptosis. Journal of Cell Science, Supplement, 18, 51–55.10.1242/jcs.1994.Supplement_18.77883792
Search in Google Scholar Back to article
12. Yip K. W, Reed J. C. (2008). Bcl-2 family proteins and cancer. Oncogene, 27(50), 6398–6406. https://doi.org/10.1038/onc.2008.30710.1038/onc.2008.30718955968
Open DOI Search in Google Scholar Back to article
13. Frenzel, A., Grespi, F., Chmelewskij, W. & Villunger. A. (2009). Bcl2 family proteins in carcinogenesis and the treatment of cancer. Apoptosis. 14(4); 584–596. doi:10.1007/s10495-008-0300-z.10.1007/s10495-008-0300-z327240119156528
Open DOI Search in Google Scholar Back to article
14. Kelly P, Strasser A. (2011). The role of Bcl-2 and its prosurvival relatives in tumourigenesis and cancer therapy. Cell Death and Different, 18(10), 1414–1424. https://doi.org/10.1038/cdd.2011.1710.1038/cdd.2011.17314974021415859
Search in Google Scholar Back to article
15. Susan F. L, Brad C. T. (2005). Apoptosis, pyroptosis, and necrosis: mechanistic description of dead and dying eukaryotic cells. Infection and immunity, 73(4), 1907-16.10.1128/IAI.73.4.1907-1916.2005
Search in Google Scholar Back to article
16. Doerflinger M, Glab J. A, Puthalakath H. (2015). BH3- only proteins: a 20-year stock-take. FEBS Journal, 282,1006–1016. doi:10.1111/febs.1319010.1111/febs.13190
Search in Google Scholar Back to article
17. Dewson, G, Kluck R. M. (2009). Mechanisms by which Bak and Bax permeabilise mitochondria during apoptosis. Journal of Cell Science, 122, 2801-8.10.1242/jcs.038166
Search in Google Scholar Back to article
18. Ghatage D D, Gosavi S R, Ganvir S. M, Hazarey V. K. (2012). Apoptosis: Molecular mechanism. Journal Orofacial Science, 4 (2).10.4103/0975-8844.106199
Search in Google Scholar Back to article
19. Barak Y, Juven T, Haffner R. (1993). mdm2 expression is induced by wild type p53 activity. EMBO Journal, 12, 461–468.10.1002/j.1460-2075.1993.tb05678.x
Search in Google Scholar Back to article
20. Belizário J, Cordeiro L. V, Enns S. (2015). Necroptotic Cell Death Signaling and Execution Pathway: Lessons from Knockout Mice. Hindawi Publishing Corporation Mediators of Inflammation, 15.10.1155/2015/128076
Search in Google Scholar Back to article
21. Bensi L, Longo R, Vecchi A, Messora C, Garagnani L, Bernardi M. S, Tamassia G, Sacchi S. (1995). BCL-2 Oncoprotein Expression in Acute Myeloid Leukemia. Haematology, 80, 98-102.
Search in Google Scholar Back to article
22. Billard C. (2015). Apoptosis as a Therapeutic Target in Chronic Lymphocytic Leukemia. Lymphocytitc and Chonic Lymphocytic Leukemia, 5, 11–15. doi:10.4137/LCLL.S13718.10.4137/LCLL.S13718
Open DOI Search in Google Scholar Back to article
23. Blau O. (2015). Gene Mutations in Acute Myeloid Leukemia- Incidence, Prognostic Influence, and Association with Other Molecular Markers. INTECH, 75-100.10.5772/60928
Search in Google Scholar Back to article
24. Blatt N. B, Glick G. D. (2001). Signaling pathways and effector mechanisms pre-programmed cell death. Bioorganic and Medical Chemistry, 9(6), 1371-84.10.1016/S0968-0896(01)00041-4
Search in Google Scholar Back to article
25. Fisher A. (1937). The theory of the developmental physiology of malignant tumor. The American journal of cancer, 31(10).
Search in Google Scholar Back to article
26. Breckenridge D. G, Germain M, Mathai J. P, Nguyen M, Shore G. C. (2003) Regulation of apoptosis by endoplasmic reticulum pathways. Oncogene, 22, 8608–8618. doi:10.1038/sj.onc.120710810.1038/sj.onc.120710814634622
Open DOI Search in Google Scholar Back to article
27. Bruin E. C, Medema J. P. (2008). Apoptosis and nonapoptotic deaths in cancer development and treatment response. Cancer Treatment Reviews, 34(8), 737-749. doi: http://dx.doi.org/10.1016/j.ctrv.2008.07.00110.1016/j.ctrv.2008.07.00118722718
Search in Google Scholar Back to article
28. Brunelle J. K, Letai A. (2009). Control of mitochondrial apoptosis by the Bcl-2 family. J Cell Science, 122, 437-441.10.1242/jcs.031682271443119193868
Search in Google Scholar Back to article
29. Chaabane W, User S. D, El-Gazzah M, Jaksik R, Sajjadi E, Rzeszowska-Wolny J, Łos M. J. (2013). Autophagy, Apoptosis, Mitoptosis and Necrosis: Interdependence Between Those Pathways and Effects on Cancer. Archive of Immunology Therapy and Experimental, 61, 43–58, (2013). DOI 10.1007/s00005-012-0205-y10.1007/s00005-012-0205-y23229678
Open DOI Search in Google Scholar Back to article
30. Chipuk J. E. (2015). BCL-2 proteins: melanoma lives on the edge. Oncoscience, 34(7), 857-67.10.18632/oncoscience.193460599726501069
Search in Google Scholar Back to article
31. Chonghaile T. N, Letai A. (2009). Mimicking the BH3 domain to kill cancer cells. Oncogene, 27, 149–157. doi:10.1038/onc.2009.5210.1038/onc.2009.52373326519641500
Open DOI Search in Google Scholar Back to article
32. Thorburn A. (2008). Apoptosis and autophagy: regulatory connections between two supposedly different processes. Apoptosis, 13(1), 1-9. Doi: 10.1007/s10495-007-0154-910.1007/s10495-007-0154-9260159517990121
Open DOI Search in Google Scholar Back to article
33. Kelly P, Strasser A. (2011). The role of Bcl-2 and its prosurvival relatives in tumourigenesis and cancer therapy. Cell Death and Differentiation, 18(10), 1414–1424. https://doi.org/10.1038/cdd.2011.1710.1038/cdd.2011.17314974021415859
Search in Google Scholar Back to article
34. Palai T. K, Mishra S. R. (2015). Caspases: An apoptosis mediator. Journal of Advanced Veerinary and Animal Research, 2(1), 18-22. doi: 10.5455/javar.2015.b5210.5455/javar.2015.b52
Open DOI Search in Google Scholar Back to article
35. Shimizu S, Yoshida T, Tsujioka M, Arakawa S. (2014). Autophagic Cell Death and Cancer. International Journal of Molecular Science, 15, 3145-3153. doi:10.3390/ijms1502314510.3390/ijms15023145395890224566140
Open DOI Search in Google Scholar Back to article
36. Siddiqui W. A, Ahad A, Ahsan H. (2015). The mystery of BCL2 family: Bcl-2 proteins and apoptosis: an update. Archives of Toxicology, 89, 289-317.10.1007/s00204-014-1448-725618543
Search in Google Scholar Back to article
37. Singh L, Pushker N, Saini N, Sen S, Sharma A, Bakhshi S, Chawla B, Kashyap S. (2015). Expression of proapoptotic Bax and anti-apoptotic Bcl-2 proteins in human retinoblastoma. Clinical Experimental Ophthopedic, 43, 259–267. doi: 10.1111/ceo.123910.1111/ceo.1239
Open DOI Search in Google Scholar Back to article
38. Su Z, Yang Z, Xu Y, Chen Y, Qiang Y. Q. (2015). Apoptosis, autophagy, necroptosis, and cancer metastasis. Molecular Cancer, 14(48). Doi:10.1186/s12943-015-0321-510.1186/s12943-015-0321-5
Open DOI Search in Google Scholar Back to article
39. Guicciardi M. E, Gores G. J. (2009). Life and death by death receptors. FASEBJ, 23(6), 1625-37. doi: 10.1096/fj.08-111005.10.1096/fj.08-111005
Open DOI Search in Google Scholar Back to article
40. Marsden V. S, Ekert P. G, Delft M. V, Vaux D. L, Adams J. M, Strasser A. (2004). Bcl-2–regulated apoptosis and cytochrome c release can occur independently of both caspase-2 and caspase- 9. The Journal of Cell Biology, 165(6),775–780. http://www.jcb.org/cgi/doi/10.1083/jcb.20031203010.1083/jcb.200312030
Open DOI Search in Google Scholar Back to article
41. Mason K, Vandenberga C. J, Scotta C. L, Wei A. H, Corya S, Huanga D. (2008). In vivo ef cacy of the Bcl- 2 antagonist ABT-737 against aggressive Myc-driven lymphomas. The Proceedings of the National Academy of Sciences, 105, 17961-17966.10.1073/pnas.0809957105
Search in Google Scholar Back to article
42. Mérino D, Khaw S. L, Glaser S. P, Anderson D. J, Belmont L. D, Wong C. (2012). Bcl-2, Bcl-xL, and Bcl-w are not equivalent targets of ABT-737 and navitoclax (ABT-263 in lymphoid and leukemic cells. Blood, 119, 5807-5816.10.1182/blood-2011-12-400929
Search in Google Scholar Back to article
43. Mehdipour P, Santoro F, Minucci S.(2015). Epigenetic alterations in acute myeloid leukemias. FEBS Journal, 282, 1786–1800. doi:10.1111/febs.1314210.1111/febs.13142
Open DOI Search in Google Scholar Back to article
44. Momand J, Zambetti G. P, Olson D. C. (1991). The mdm-2 oncogene product forms a complex with the p53 protein and inhibits p53-mediated transactivation. Cell, 69, 1237–1245.10.1016/0092-8674(92)90644-R
Search in Google Scholar Back to article
45. Kang M. H, Reynolds C. P. (2009). Bcl-2 Inhibitors: Targeting Mitochondrial Apoptotic Pathways in Cancer Therapy. Clinical Cancer Research, 15(4). doi:10.1158/1078-0432.CCR-08-014410.1158/1078-0432.CCR-08-0144318226819228717
Open DOI Search in Google Scholar Back to article
46. Koff J. L, Ramachandiran S, Bernal-Mizrachi L. (2015). A Time to Kill: Targeting Apoptosis in Cancer. International Journal Molecular Science, 16, 2942-2955. doi:10.3390/ijms1602294210.3390/ijms16022942434687425636036
Open DOI Search in Google Scholar Back to article
47. Kontny U, Lissat A. (2015). Apoptosis and drug resistance in malignant bone tumors. Primary bone tumours. Doi: 10.1016/B978-0-12-416721-6.00036-410.1016/B978-0-12-416721-6.00036-4
Open DOI Search in Google Scholar Back to article
48. Lavrik I. N. (2014). Systems biology of death receptor networks: live and let die. Cell Death and Disease, 5. doi:10.1038/cddis.2014.16010.1038/cddis.2014.160404788124874731
Open DOI Search in Google Scholar Back to article
49. Leber B, Lin J, Andrews D. W. (2010). Still embedded together binding to membranes regulates Bcl-2 protein interactions. Oncogene, 29, 5221-30.10.1038/onc.2010.283645940720639903
Open DOI Search in Google Scholar Back to article
50. Letai A, Sorcinelli M. D, Beard C, Korsmeyer S. J. (2002). Antiapoptotic BCL-2 is required for maintenance of a model leukemia. Cancer Cell, 6, 241–9.10.1016/j.ccr.2004.07.01115380515
Search in Google Scholar Back to article
51. Le´veille F, Papadia S, Fricker M, Bell K. F. S, Soriano F. X, Martel M, Puddifoot C, Habel M, Wyllie D. J, Ikonomidou C, Tolkovsky A. M, Hardingham G. E. (2010). Suppression of the Intrinsic Apoptosis Pathway by Synaptic Activity. The Journal of Neurology, 30(7), 2623–2635.10.1523/JNEUROSCI.5115-09.2010283492720164347
Search in Google Scholar Back to article
52. Liu B, Bhatt D, Oltvai Z. N, Greenberger J. S, Bahar I. (2014). Significance of p53 dynamics in regulating apoptosis in response to ionizing radiation, and polypharmacological strategies. Scientific Reports, 4, 6245. Doi: 10.1038/srep0624510.1038/srep06245415010625175563
Open DOI Search in Google Scholar Back to article
53. Li M. X, Dewson G. (2015). Mitochondria and apoptosis: emerging concepts. F1000Prime Reports, 7(42). doi:10.12703/P7-42.10.12703/P7-42444703226097715
Open DOI Search in Google Scholar Back to article
54. Abramowitz J, Neuman T, Perlman R, Ben-Yehuda D. (2017). Gene and protein analysis reveals that p53 pathway is functionally inactivated in cytogenetically normal Acute Myeloid Leukemia and Acute Promyelocytic Leukemia. BMC Medical Genomics, 10(1),18. https://doi.org/10.1186/s12920-017-0249-210.1186/s12920-017-0249-2542342128340577
Open DOI Search in Google Scholar Back to article
55. Petitjean A, Mathe E, Kato S, Ishioka C, Tavtigian S. V, Hainaut P, Olivier M. (2007). Impact of Mutant p53 Functional Properties on TP53 Mutation Patterns and Tumor Phenotype: Lessons from Recent Developments in the IARC TP53 Database. Human mutation, 28(6), 622-629.10.1002/humu.2049517311302
Search in Google Scholar Back to article
56. Llambi F, Moldoveanu T, Tait Stephen W. G, Bouchier- Hayes L, Temirov J, McCormick L. L, Dillon C. P, Green D. R. (2011). A unified model of mammalian BCL-2 protein family interactions at the mitochondria. Molecular Cell, 44, 517-31.10.1016/j.molcel.2011.10.001322178722036586
Open DOI Search in Google Scholar Back to article
57. Fulda S, Debatin K. M. (2006). Extrinsic versus intrinsic apoptosis pathways in anticancer chemotherapy. Oncogene, 25(34), 4798-811.10.1038/sj.onc.1209608
Search in Google Scholar Back to article
58. Löwenberg B, Rowe J. M. (2015). Introduction to the review series on advances in acute myeloid leukemia (AML). Blood, 127(1). doi:10.1182/blood-2015-10-6626810.1182/blood-2015-10-66268
Open DOI Search in Google Scholar Back to article
59. Mongiat M, Ligresti G, Marastoni S, Lorenzon E, Doliana R, Alfonso C. Regulation of the Extrinsic Apoptotic Pathway by the Extracellular Matrix Glycoprotein EMILIN2. (2007). Molecular Cell Biology, 27(20), 7176–7187. doi:10.1128/MCB.00696-0710.1128/MCB.00696-07
Open DOI Search in Google Scholar Back to article
60. Moore V. D. G, Letai A. (2012). BH3 profiling – measuring integrated function of the mitochondrial apoptotic pathway to predict cell fate decisions. Cancer Letter, 332(2), 202–205. doi:10.1016/j.canlet.2011.12.021.10.1016/j.canlet.2011.12.021
Open DOI Search in Google Scholar Back to article
61. Moore D. G. V, Brown J. R, Certo M. (2007). Chronic lymphocytic leukemia requires BCL2 to sequester prodeath BIM, explaining sensitivity to BCL2 antagonist ABT-737. Journal of Clinical Investiment, 117, 112–21.10.1172/JCI28281
Search in Google Scholar Back to article
62. Naseri H. M, Mahdavi M, Davoodi J, Tackallou S. H, Goudarzvand M, Neishabouri S. H. (2015). Up regulation of Bax and down regulation of Bcl2 during 3-NC mediated apoptosis in human cancer cells. Cancer Cell International, 15(55). Doi: 10.1186/s12935-015-0204-210.1186/s12935-015-0204-2
Open DOI Search in Google Scholar Back to article
63. Ng S. Y, Davids M. S. (2014). Selective Bcl-2 inhibition to treat chronic lymphocytic leukemia and non-Hodgkin lymphoma. Clinical Advanced Hematology Oncology, 12(4), 224-9.
Search in Google Scholar Back to article
64. Noguchi M, Hirata N, Edamura T, Ishigaki S, Suizu F. (2015). Intersection of Apoptosis and Autophagy Cell Death Pathways. Austin Journal of Molecular & Cell Biology, 2(1), 1004.
Search in Google Scholar Back to article
65. Oltersdorf T, Steven W, Elmore S. W, Shoemaker A. R, Armstrong R. C, Augeri D. J, Belli B. A. (2005). An inhibitor of Bcl-2 family proteins induces regression of solid tumours. Nature, 435, 677-681.10.1038/nature03579
Search in Google Scholar Back to article
67. Gibson L, Holmgreen S. P, Huang D. C, Bernard O, Copeland N. G, Jenkins N. A, Sutherland G. R, Baker E, Adams J. M, Cory S. (1996). Bcl-w, a novel member of the bcl-2 family, promotes cell survival. Oncology, 13(4), 665-75.
Search in Google Scholar Back to article
68. Zhong Q, Gao W, Du F, Wang X. (2005). Mule/ARFBP1, a BH3-only E3 ubiquitin ligase, catalyzes the polyubiquiti-nation of Mcl-1 and regulates apoptosis. Cell, 121, 1085–1095.10.1016/j.cell.2005.06.009
Search in Google Scholar Back to article
69. Czabotar P. E, Lee E. F, Delft M. F, Day C. L, Smith B. J, Huang D. C. S, Fairlie W. D, Hinds M. G, Colman P.M. (2007). Structural insights into the degradation of Mcl-1 induced by BH3 domain. Proceedings of the National Academy of Sciences, 104 (15) 6217-6222. DOI:10.1073/pnas.070129710410.1073/pnas.0701297104
Open DOI Search in Google Scholar Back to article
70. Huang D. C. S, Strasser A. (2000). BH3-Only Proteins— Essential Initiators of Apoptotic Cell Death. Cell, 103, 839–842.10.1016/S0092-8674(00)00187-2
Search in Google Scholar Back to article
71. Shamas-Din A, Kale J, Leber B, Andrews D. W. (2013). Mechanisms of Action of Bcl-2 Family Proteins. Cold Spring Harbor Perspective in Biology. doi: 10.1101/cshperspect. a00871410.1101/cshperspect.a008714368389723545417
Open DOI Search in Google Scholar Back to article
72. Belka C, Budach W. (2002). Anti-apoptotic Bcl-2 proteins: structure, function and relevance for radiation biology. International journal of radiation Biology, 78(8), 643-658. Doi: 10.1080/0955300021013768 010.1080/09553000210137680
Search in Google Scholar Back to article
73. Bouillet P, Metcalf D, Huang D. C, Tarlinton D. M, Kay T. W, Kontgen F, Adams J. M, Strasser A. (1999). Proapoptotic Bcl-2 relative Bim required for certain apoptotic responses, leukocyte homeostasis, and to preclude autoimmunity. Science, 286, 1735–1738.10.1126/science.286.5445.173510576740
Search in Google Scholar Back to article
74. Polcic P, Jaká P, Mentel M. (2015). Yeast as a tool for studying proteins of the Bcl-2 family. Microbiology Cell, 2(3), 74-87. doi: 10.15698/mic2015.03.19310.15698/mic2015.03.193534918128357280
Open DOI Search in Google Scholar Back to article
75. Sáez G. A. J. (2012). The secrets of the Bcl-2 family. Cell Death Differentiation, 11, 1733-40. doi: 10.1038/cdd.2012.105.10.1038/cdd.2012.105346906522935609
Open DOI Search in Google Scholar Back to article
76. Scaffidi C, Fulda S, Srinivasan A, Friesen C, Li F, Tomaselli K. J, Debatin K. M, Krammer P. H, Peter M. E. (1998). Two CD95 (APO-1/Fas) signaling pathways. The EMBO Journal, 17(6), 1675–1687.10.1093/emboj/17.6.167511705159501089
Open DOI Search in Google Scholar Back to article
77. Schnerch D, Yalcintepe J, Schmidts A, Becker H, Follo M, Engelhardt M, Wäsch R. (2012). Cell cycle control in acute myeloid leukemia. American Journal of Cancer Research, 2(5), 508-528.
Search in Google Scholar Back to article
78. Scandura J. M, Boccuni P, Cammenga J, Nimer S. D. (2002). Transcription factor fusions in acute leukemia: variations on a theme. Oncogene, 21, 3422-3444. Doi: 10.1038/sj/onc/120531510.1038/sj/onc/1205315
Open DOI Search in Google Scholar Back to article
79. Shimizu S, Yoshida T, Tsujioka M, Arakawa S. (2014). Autophagic Cell Death and Cancer. International Journal of Molecular Science, 15, 3145-3153. doi:10.3390/ijms1502314510.3390/ijms15023145395890224566140
Open DOI Search in Google Scholar Back to article
80. Smaili S. S, Hsu Y. T, Carvalho A. C. P, Rosenstock T. R, Sharpe J. C, Youle, R. J. (2003). Mitochondria, calcium and pro-apoptotic proteins as mediators in cell death signaling. Brazilian Journal of Medical Biology Research. 36(2), 183-190.10.1590/S0100-879X200300020000412563519
Search in Google Scholar Back to article
81. Strasser A. (2005). The role of BH3-only proteins in the immune system. Nature Reviews Immunology, 5, 189-200.doi:10.1038/nri156810.1038/nri156815719025
Open DOI Search in Google Scholar Back to article
82. Sun Z, Cheng Z, Taylor C. A, McConkey B, Thompson J. E. (2010). Apoptosis Induction by eIF5A1 Involves Activation of the Intrinsic Mitochondrial Pathway. Journal of Cell Physiology, 223, 798–809. Doi: 10.1002/jcp.2210010.1002/jcp.2210020232312
Open DOI Search in Google Scholar Back to article
83. Tian K.Y, Liu X. J, Xu J.D, Deng L. J, Wang G. (2015). Propofol inhibits burn injury-induced hyperpermeability through an apoptotic signal pathway in microvascular endothelial cells. Brazilian Journal of Medical Biology Research, 48(5), 401-407. http://dx.doi.org/10.1590/1414-431X2014410710.1590/1414-431X20144107
Open DOI Search in Google Scholar Back to article
84. Trump B. F, Berezesky I. K, Chang, S. H, Phelps P. C. (1997). The Pathways of Cell Death: Oncosis, Apoptosis, and Necrosis. Toxicologic Pathology, 25(1), 82-8. Doi: 10.1177/01926233970250011610.1177/019262339702500116
Search in Google Scholar Back to article
85. Tiwari M, Sharma L. K, Saxena A. K, Godbole M. M. (2015). Interaction Between Mitochondria and Caspases: Apoptotic and Non-Apoptotic Roles. Cell Biology, 3(2), 22-30. doi: 10.11648/j.cb.s.2015030201.1410.11648/j.cb.s.2015030201.14
Open DOI Search in Google Scholar Back to article
86. Tzifi F, Economopoulou C, Gourgiotis D, Ardavanis A, Papageorgiou S, Scorilas A. (2012). The Role of BCL2 Family of Apoptosis Regulator Proteins in Acute and Chronic Leukemias. Hindawi Public Corporation Advanced Hematology, doi:10.1155/2012/524308.10.1155/2012/524308
Open DOI Search in Google Scholar Back to article
87. Vela L, Gonzalo O, Naval J, Marzo I. (2013). Revealed by fluorescence complementation. Journal of Biological Chemistry, doi:10.1074/jbc.M112.42220410.1074/jbc.M112.422204
Open DOI Search in Google Scholar Back to article
88. Verbrugge I, Johnstone R. W, Smyth M. J. (2010). Snap- Shot: Extrinsic Apoptosis Pathways. Cell, 143(7), 1192. DOI 10.1016/j.cell.2010.12.00410.1016/j.cell.2010.12.004
Open DOI Search in Google Scholar Back to article
89. Vo T. T, Ryan J, Carrasco R, Neuberg D, Rossi D. J, Stone R. M, Letai A. (2012). Relative mitochondrial priming of myeloblasts and normal HSCs determines chemotherapeutic success in AML. Cell, 151(2), 344-355.10.1016/j.cell.2012.08.038
Search in Google Scholar Back to article
90. El-Shakankiry N. H, El-Sayed G. M, El-Maghraby S, Moneer M. M. (2009). Bcl-2 protein expression in egyptian acute myeloid leukemia. Journal of Egypt Natural Cancer Institute, 21(1), 71–6.
Search in Google Scholar Back to article
91. Shi Y. (2002). Mechanisms of caspase activation and inhibition during apoptosis. Molecular Cell. https://doi.org/10.1016/S1097-2765(02)00482-310.1016/S1097-2765(02)00482-3
Open DOI Search in Google Scholar Back to article
92. Wang R. A, Li Z. S, Yan Q. Q, Bian X. W, Ding Y. Q, Xiang D. X, Sun B. C, Yun-Tian S. Y. T, Xiang-Hong Zhang X. H. (2014). Resistance to apoptosis should not be taken as a hallmark of cancer. Chinese Journal of Cancer, 33(2).10.5732/cjc.013.10131393500524417874
Search in Google Scholar Back to article
93. Wei A. Teh T. C. (2012). Primed for the kill: occupying Bcl-2 to target death in acute myeloid leukaemia. Bio- Discovery, 6(1). doi:10.7750/BioDiscovery.2012.610.7750/BioDiscovery.2012.6
Open DOI Search in Google Scholar Back to article
94. Weyhenmeyer B, Murphy A. C, Prehn J. H. M, Murphy B. M. (2012). Targeting the anti-apoptotic BCL-2 family members for the treatment of cancer. Experimental Oncology, 34, 192–199.23070004
Search in Google Scholar Back to article
95. Woess C, Tuzlak S, Labi V, Drach M, Bertele D, Schneider P, Villunger A. (2015). Combined loss of the BH3- only proteins Bim and Bmf restores B-cell development and function in TACI-Ig transgenic mice. Cell Death Differentiation, 22, 1477–1488. doi: 10.1038/cdd.2015.810.1038/cdd.2015.8453278425698446
Open DOI Search in Google Scholar Back to article
96. Wu M, Ding H. F, Fisher D. E. Apoptosis: Molecular Mechanisms. Encyclopedia of Life Science 2001.10.1023/A:1011342220621
Open DOI Search in Google Scholar Back to article
97. Yip K. W, Reed J. C. (2008). Bcl-2 family proteins and cancer. Oncology, 27, 6398–6406.10.1038/onc.2008.307
Search in Google Scholar Back to article
98. Yohe S. (2015). Molecular Genetic Markers in Acute Myeloid Leukemia. Journal of Clinical Medicine, 4, 460-478 (2015). doi:10.3390/jcm403046010.3390/jcm4030460447013926239249
Open DOI Search in Google Scholar Back to article
99. Youle R. J, Strasser A. (2005). The BCL-2 protein family: op- posing activities that mediate cell death. Nature Reviews of Molecular and Cell Biology, 9, 47–59.10.1038/nrm2308
Search in Google Scholar Back to article
100. Perez-Stable C, Parrondo R, De Las Pozas A, Reiner T. (2013). ABT-737, a small molecule Bcl-2/Bcl-xL antagonist, increases antimitotic- mediated apoptosis in human prostate cancer cells. Biochemistry, biophysics and molecular biology, https://doi.org/10.7717/peerj.14410.7717/peerj.144377563124058878
Open DOI Search in Google Scholar Back to article
101. Zhao G, Zhu Y, Eno C. O, Liu Y, DeLeeuw L, Joseph A, Burlison J. A, Chaires J. B, Trent J. O, Li C. (2014). Activation of the Proapoptotic Bcl-2 Protein Bax by a Small Molecule Induces Tumor Cell Apoptosis. Molecular Cell Biology, 34(7), 1198–1207. doi:10.1128/MCB.00996-1310.1128/MCB.00996-13399356124421393
Open DOI Search in Google Scholar Back to article
102. Zong W. X, Lindsten T, Ross A. J, MacGregor G. R, Thompson C. B. (2001). BH3-only proteins that bind pro-survival Bcl-2 family members fail to induce apoptosis in the absence of Bax and Bak. Gene & Development, 15, 1481–1486.10.1101/gad.89760131272211410528
Open DOI Search in Google Scholar Back to article

Bcl-2 Family Overexpression and Chemoresistance in Acute Myeloid Leukemia

Abstract

Paradigm

My account