Bcl-2 (B-ćelijski limfom 2) je član Bcl-2 familije proteinskih regulatora apoptoze. On je kodiran BCL2genom.[1][2] Bcl-2 je drugi član niza proteina koji su inicijalno bili opisani u kontekstu hromozomske translokacijehromozoma 14 i 18 kod folikularnih limfoma. Bcl-2 ortolozi[3] postoje kod mnogobrojnih sisara. Dve izoforme Bcl-2, Izoforma 1, takođe poznata kao 1G5M, i Izoforma 2, poznata kao 1G5O/1GJH, imaju sličnu prostornu strukturu. Međutim, one se razlikuju u njihovoj sposobnosti vezivanja BAD u BAK proteina, kao i po strukturnoj topologiji i elektrostatičkom potencijalu vezujućeg žljeba. Iz toga sledi da Bcl-2 izoforme imaju različite antiapoptotičke aktivnosti.[4]
^Tsujimoto Y, Finger LR, Yunis J, Nowell PC, Croce CM (1984). „Cloning of the chromosome breakpoint of neoplastic B cells with the t(14;18) chromosome translocation”. Science. 226 (4678): 1097—99. PMID6093263. doi:10.1126/science.6093263.
^Cleary ML, Smith SD, Sklar J (1986). „Cloning and structural analysis of cDNAs for bcl-2 and a hybrid bcl-2/immunoglobulin transcript resulting from the t(14;18) translocation”. Cell. 47 (1): 19—28. PMID2875799. doi:10.1016/0092-8674(86)90362-4.
^ абKomatsu K, Miyashita T, Hang H, Hopkins KM, Zheng W, Cuddeback S, Yamada M, Lieberman HB, Wang HG (2000). „Human homologue of S. pombe Rad9 interacts with BCL-2/BCL-xL and promotes apoptosis”. Nat. Cell Biol. ENGLAND. 2 (1): 1—6. ISSN1465-7392. PMID10620799. doi:10.1038/71316.
^ абвгLin, Bingzhen; Kolluri Siva Kumar; Lin Feng (2004). Liu Wen, Han Young-Hoon, Cao Xihua, Dawson Marcia I, Reed John C, Zhang Xiao-kun. „Conversion of Bcl-2 from protector to killer by interaction with nuclear orphan receptor Nur77/TR3”. Cell. United States. 116 (4): 527—40. ISSN0092-8674. PMID14980220. doi:10.1016/S0092-8674(04)00162-X.
^Enyedy IJ, Ling Y, Nacro K, Tomita Y, Wu X, Cao Y, Guo R, Li B, Zhu X, Huang Y, Long YQ, Roller PP, Yang D, Wang S (2001). „Discovery of small-molecule inhibitors of Bcl-2 through structure-based computer screening”. J. Med. Chem. United States. 44 (25): 4313—24. ISSN0022-2623. PMID11728179. doi:10.1021/jm010016f.
^Tagami S, Eguchi Y, Kinoshita M, Takeda M, Tsujimoto Y (2000). „A novel protein, RTN-XS, interacts with both Bcl-XL and Bcl-2 on endoplasmic reticulum and reduces their anti-apoptotic activity”. Oncogene. England. 19 (50): 5736—46. ISSN0950-9232. PMID11126360. doi:10.1038/sj.onc.1203948.
^Oltvai, Z N; Milliman C L; Korsmeyer S J (1993). „Bcl-2 heterodimerizes in vivo with a conserved homolog, Bax, that accelerates programmed cell death”. Cell. UNITED STATES. 74 (4): 609—19. ISSN0092-8674. PMID8358790. doi:10.1016/0092-8674(93)90509-O.
^Poulaki V, Mitsiades N, Romero ME, Tsokos M (2001). „Fas-mediated apoptosis in neuroblastoma requires mitochondrial activation and is inhibited by FLICE inhibitor protein and Bcl-2”. Cancer Res. United States. 61 (12): 4864—72. ISSN0008-5472. PMID11406564.
^Guo, Yin; Srinivasula Srinivasa M; Druilhe Anne; Fernandes-Alnemri Teresa; Alnemri Emad S (2002). „Caspase-2 induces apoptosis by releasing proapoptotic proteins from mitochondria”. J. Biol. Chem. United States. 277 (16): 13430—7. ISSN0021-9258. PMID11832478. doi:10.1074/jbc.M108029200.
^Pasinelli, Piera; Belford Mary Elizabeth; Lennon Niall; Bacskai Brian J; Hyman Bradley T; Trotti Davide; Brown Robert H (2004). „Amyotrophic lateral sclerosis-associated SOD1 mutant proteins bind and aggregate with Bcl-2 in spinal cord mitochondria”. Neuron. United States. 43 (1): 19—30. ISSN0896-6273. PMID15233914. doi:10.1016/j.neuron.2004.06.021.
^ абвгдђChen L, Willis SN, Wei A, Smith BJ, Fletcher JI, Hinds MG, Colman PM, Day CL, Adams JM, Huang DC (2005). „Differential targeting of prosurvival Bcl-2 proteins by their BH3-only ligands allows complementary apoptotic function”. Mol. Cell. United States. 17 (3): 393—403. ISSN1097-2765. PMID15694340. doi:10.1016/j.molcel.2004.12.030.
^Real, Pedro Jose; Cao Yeyu; Wang Renxiao; Nikolovska-Coleska Zaneta (2004). Sanz-Ortiz Jaime, Wang Shaomeng, Fernandez-Luna Jose Luis. „Breast cancer cells can evade apoptosis-mediated selective killing by a novel small molecule inhibitor of Bcl-2”. Cancer Res. United States. 64 (21): 7947—53. ISSN0008-5472. PMID15520201. doi:10.1158/0008-5472.CAN-04-0945.
^Fernandez-Sarabia, M J; Bischoff J R (1993). „Bcl-2 associates with the ras-related protein R-ras p23”. Nature. ENGLAND. 366 (6452): 274—5. ISSN0028-0836. PMID8232588. doi:10.1038/366274a0.
^Hsu, S Y; Lin P; Hsueh A J (1998). „BOD (Bcl-2-related ovarian death gene) is an ovarian BH3 domain-containing proapoptotic Bcl-2 protein capable of dimerization with diverse antiapoptotic Bcl-2 members”. Mol. Endocrinol. UNITED STATES. 12 (9): 1432—40. ISSN0888-8809. PMID9731710. doi:10.1210/me.12.9.1432.
^ абQin, Wenxin; Hu Jian; Guo Minglei; Xu Jian (2003). Li Jinjun, Yao Genfu, Zhou Xiaomei, Jiang Huiqiu, Zhang Pingping, Shen Li, Wan Dafang, Gu Jianren. „BNIPL-2, a novel homologue of BNIP-2, interacts with Bcl-2 and Cdc42GAP in apoptosis”. Biochem. Biophys. Res. Commun. United States. 308 (2): 379—85. ISSN0006-291X. PMID12901880. doi:10.1016/S0006-291X(03)01387-1.
^Yasuda, M; Han J W; Dionne C A; Boyd J M; Chinnadurai G (1999). „BNIP3alpha: a human homolog of mitochondrial proapoptotic protein BNIP3”. Cancer Res. UNITED STATES. 59 (3): 533—7. ISSN0008-5472. PMID9973195.
^Alberici A, Moratto D, Benussi L, Gasparini L, Ghidoni R, Gatta LB, Finazzi D, Frisoni GB, Trabucchi M, Growdon JH, Nitsch RM, Binetti G (1999). „Presenilin 1 protein directly interacts with Bcl-2”. J. Biol. Chem. UNITED STATES. 274 (43): 30764—9. ISSN0021-9258. PMID10521466. doi:10.1074/jbc.274.43.30764.
^Puthalakath H, Villunger A, O'Reilly LA, Beaumont JG, Coultas L, Cheney RE, Huang DC, Strasser A (2001). „Bmf: a proapoptotic BH3-only protein regulated by interaction with the myosin V actin motor complex, activated by anoikis”. Science. United States. 293 (5536): 1829—32. ISSN0036-8075. PMID11546872. doi:10.1126/science.1062257.
^ абBoyd JM, Malstrom S, Subramanian T, Venkatesh LK, Schaeper U, Elangovan B, D'Sa-Eipper C, Chinnadurai G (1994). „Adenovirus E1B 19 kDa and Bcl-2 proteins interact with a common set of cellular proteins”. Cell. UNITED STATES. 79 (2): 341—51. ISSN0092-8674. PMID7954800. doi:10.1016/0092-8674(94)90202-X.
^Ray R, Chen G, Vande VC, Cizeau J, Park JH, Reed JC, Gietz RD, Greenberg AH (2000). „BNIP3 heterodimerizes with Bcl-2/Bcl-X(L) and induces cell death independent of a Bcl-2 homology 3 (BH3) domain at both mitochondrial and nonmitochondrial sites”. J. Biol. Chem. UNITED STATES. 275 (2): 1439—48. ISSN0021-9258. PMID10625696. doi:10.1074/jbc.275.2.1439.
^Zhang, Haichao; Nimmer Paul; Rosenberg Saul H; Ng Shi-Chung; Joseph Mary (2002). „Development of a high-throughput fluorescence polarization assay for Bcl-x(L)”. Anal. Biochem. United States. 307 (1): 70—5. ISSN0003-2697. PMID12137781. doi:10.1016/S0003-2697(02)00028-3.
^Jin, Zhaohui; Gao Fengqin; Flagg Tammy; Deng Xingming (2004). „Tobacco-specific nitrosamine 4-(methylnitrosamino)-1-(3-pyridyl)-1-butanone promotes functional cooperation of Bcl2 and c-Myc through phosphorylation in regulating cell survival and proliferation”. J. Biol. Chem. United States. 279 (38): 40209—19. ISSN0021-9258. PMID15210690. doi:10.1074/jbc.M404056200.
^Iwahashi H, Eguchi Y, Yasuhara N, Hanafusa T, Matsuzawa Y, Tsujimoto Y (1997). „Synergistic anti-apoptotic activity between Bcl-2 and SMN implicated in spinal muscular atrophy”. Nature. ENGLAND. 390 (6658): 413—7. ISSN0028-0836. PMID9389483. doi:10.1038/37144.
^Gil-Parrado, Shirley; Fernández-Montalván Amaury; Assfalg-Machleidt Irmgard; Popp Oliver; Bestvater Felix (2002). Holloschi Andreas, Knoch Tobias A, Auerswald Ennes A, Welsh Katherine, Reed John C, Fritz Hans, Fuentes-Prior Pablo, Spiess Eberhard, Salvesen Guy S, Machleidt Werner. „Ionomycin-activated calpain triggers apoptosis. A probable role for Bcl-2 family members”. J. Biol. Chem. United States. 277 (30): 27217—26. ISSN0021-9258. PMID12000759. doi:10.1074/jbc.M202945200.
^Deng X, Ito T, Carr B, Mumby M, May WS (1998). „Reversible phosphorylation of Bcl2 following interleukin 3 or bryostatin 1 is mediated by direct interaction with protein phosphatase 2A”. J. Biol. Chem. UNITED STATES. 273 (51): 34157—63. ISSN0021-9258. PMID9852076. doi:10.1074/jbc.273.51.34157.
^Oda E, Ohki R, Murasawa H, Nemoto J, Shibue T, Yamashita T, Tokino T, Taniguchi T, Tanaka N (2000). „Noxa, a BH3-only member of the Bcl-2 family and candidate mediator of p53-induced apoptosis”. Science. UNITED STATES. 288 (5468): 1053—8. ISSN0036-8075. PMID10807576. doi:10.1126/science.288.5468.1053.