Hücre Ölüm Yolakları
Özet
Hücre ölümü, organizmanın gelişimi ve homeostazının sürdürülmesi için kritik bir mekanizmadır. Programlanmış hücre ölümü olarak adlandırılan süreç, hücrelerin kontrollü bir şekilde yok olmasına olanak tanır ve genellikle apoptoz, otofaji, nekroz ve ferroptoz gibi farklı yollarla gerçekleştirilir. Apoptoz, hücrenin kendi kendini yok etme süreci olup, genetik materyalin ve hücresel yapıların parçalanmasıyla sonlanır. Diğer yandan, otofaji, hücrenin bozulmuş veya hasar görmüş bileşenlerini lizozomal bir yolla sindirdiği bir süreçtir ve hücresel homeostazın korunmasında önemli bir rol oynar. Nekroz ise, çoğunlukla hücre hasarı sonucunda gerçekleşen düzensiz bir hücre ölümü şeklidir, ancak son yıllarda nekroptoz adı verilen programlanmış bir nekroz tipi keşfedilmiştir. Ferroptoz, demir bağımlı lipid peroksidasyonu ile gerçekleşen yeni bir hücre ölüm yolu olarak öne çıkmaktadır. Bu farklı hücre ölüm yolakları, organizmada hayatta kalmayı sağlayan ve aynı zamanda hastalıkların gelişimine yol açan karmaşık biyolojik süreçleri temsil eder. Apoptoz ve otofaji, genellikle fizyolojik durumlarla ilişkilendirilse de kanser gibi patolojik durumlar bu süreçlerin kontrolsüz işlemesi ile karakterizedir. Nekrozun da çeşitli hastalıkların etiyolojisinde rol oynadığı, özellikle enflamasyonla ilişkilendirildiği bilinmektedir. Ayrıca, ferroptoz gibi atipik hücre ölüm yollarının keşfi, bu süreçlerin daha iyi anlaşılmasını ve tedavi stratejilerinin geliştirilmesini sağlamaktadır. Bu bağlamda, hücre ölümü mekanizmalarının derinlemesine incelenmesi, yeni terapötik yaklaşımlar için temel oluşturmaktadır.
Cell death is a critical mechanism for the development and maintenance of homeostasis in multicellular organisms. The process known as programmed cell death enables the controlled elimination of cells and typically occurs through distinct pathways such as apoptosis, autophagy, necrosis, and ferroptosis. Apoptosis is a self-destructive cellular process characterized by the fragmentation of genetic material and cellular components. In contrast, autophagy involves the lysosome-mediated degradation of damaged or dysfunctional cellular components and plays a vital role in maintaining cellular homeostasis. Necrosis is generally considered a disordered form of cell death resulting from cellular injury; however, a regulated form of necrosis known as necroptosis has been identified in recent years. Ferroptosis, a newly recognized form of cell death, is driven by iron-dependent lipid peroxidation. These diverse cell death pathways represent complex biological processes that contribute both to organismal survival and the pathogenesis of various diseases. While apoptosis and autophagy are commonly associated with physiological conditions, their dysregulation is a hallmark of pathological states such as cancer. Necrosis is also implicated in the etiology of several diseases, particularly due to its association with inflammation. Moreover, the discovery of atypical forms of cell death such as ferroptosis has expanded our understanding of these processes and facilitated the development of novel therapeutic strategies. In this context, an in-depth investigation of cell death mechanisms forms the foundation for innovative treatment approaches.
Referanslar
Hanahan D, Weinberg RA. The hallmarks of cancer. Cell. 2000 Jan 7;100(1):57-70. doi: 10.1016/s0092-8674(00)81683-9. PMID: 10647931.
Lockshin RA, Williams CM. Programmed Cell Death--I. Cytology of Degeneration in The Intersegmental Muscles of The Pernyi Silkmoth. J Insect Physiol. 1965 Feb; 11:123-33. doi: 10.1016/0022-1910(65)90099-5. PMID: 14287218.
Lockshin RA. Programmed cell death 50 (and beyond). Cell Death Differ. 2016 Jan;23(1):10-7. doi: 10.1038/cdd.2015.126. Epub 2015 Nov 13. PMID: 26564398; PMCID: PMC4815967.
Yuan J, Ofengeim D. A guide to cell death pathways. Nat Rev Mol Cell Biol. 2024 May;25(5):379-395. doi: 10.1038/s41580-023-00689-6. Epub 2023 Dec 18. PMID: 38110635.
Newton K, Strasser A, Kayagaki N, et al. Cell death. Cell. 2024 Jan 18;187(2):235-256. doi: 10.1016/j.cell.2023.11.044. PMID: 38242081.
Johnson AG, Wein T, Mayer ML, et al. Bacterial gasdermins reveal an ancient mechanism of cell death. Science. 2022 Jan 14;375(6577):221-225. doi: 10.1126/science.abj8432. Epub 2022 Jan 13. PMID: 35025633; PMCID: PMC9134750.
Kerr JF, Wyllie AH, Currie AR. Apoptosis: a basic biological phenomenon with wide-ranging implications in tissue kinetics. Br J Cancer. 1972 Aug;26(4):239-57. doi: 10.1038/bjc.1972.33. PMID: 4561027; PMCID: PMC2008650.
Sulston JE. Post-embryonic development in the ventral cord of Caenorhabditis elegans. Philos Trans R Soc Lond B Biol Sci. 1976 Aug 10;275(938):287-97. doi: 10.1098/rstb.1976.0084. PMID: 8804.
Gilbert, SF. Developmental biology, 2000, ISBN-10: 0-87893-243-7
Li K, van Delft MF, Dewson G. Too much death can kill you: inhibiting intrinsic apoptosis to treat disease. EMBO J. 2021 Jul 15;40(14):e107341. doi: 10.15252/embj.2020107341. Epub 2021 May 26. PMID: 34037273; PMCID: PMC8280825.
Bertheloot D, Latz E, Franklin BS. Necroptosis, pyroptosis and apoptosis: an intricate game of cell death. Cell Mol Immunol. 2021 May;18(5):1106-1121. doi: 10.1038/s41423-020-00630-3. Epub 2021 Mar 30. PMID: 33785842; PMCID: PMC8008022.
Nicholson DW, Thornberry NA. Caspases: killer proteases. Trends Biochem Sci. 1997 Aug;22(8):299-306. doi: 10.1016/s0968-0004(97)01085-2. PMID: 9270303.
Nicholson DW, Thornberry NA. Caspases: killer proteases. Trends Biochem Sci. 1997 Aug;22(8):299-306. doi: 10.1016/s0968-0004(97)01085-2. PMID: 9270303.
Kuwana T, Mackey MR, Perkins G, et al. Bid, Bax, and lipids cooperate to form supramolecular openings in the outer mitochondrial membrane. Cell. 2002 Nov 1;111(3):331-42. doi: 10.1016/s0092-8674(02)01036-x. PMID: 12419244.
Letai A, Bassik MC, Walensky LD, et al. Distinct BH3 domains either sensitize or activate mitochondrial apoptosis, serving as prototype cancer therapeutics. Cancer Cell. 2002 Sep;2(3):183-92. doi: 10.1016/s1535-6108(02)00127-7. PMID: 12242151.
Cheng EH, Wei MC, Weiler S, et al. BCL-2, BCL-X(L) sequester BH3 domain-only molecules preventing BAX- and BAK-mediated mitochondrial apoptosis. Mol Cell. 2001 Sep;8(3):705-11. doi: 10.1016/s1097-2765(01)00320-3. PMID: 11583631.
Nakano K, Vousden KH. PUMA, a novel proapoptotic gene, is induced by p53. Mol Cell. 2001 Mar;7(3):683-94. doi: 10.1016/s1097-2765(01)00214-3. PMID: 11463392.
Inuzuka H, Shaik S, Onoyama I, et al. SCF(FBW7) regulates cellular apoptosis by targeting MCL1 for ubiquitylation and destruction. Nature. 2011 Mar 3;471(7336):104-9. doi: 10.1038/nature09732. PMID: 21368833; PMCID: PMC3076007.
Edlich F, Banerjee S, Suzuki M, et al. Bcl-x(L) retrotranslocates Bax from the mitochondria into the cytosol. Cell. 2011 Apr 1;145(1):104-16. doi: 10.1016/j.cell.2011.02.034. PMID: 21458670; PMCID: PMC3070914.
Kour S, Rana S, Contreras JI, et al. CDK5 Inhibitor Downregulates Mcl-1 and Sensitizes Pancreatic Cancer Cell Lines to Navitoclax. Mol Pharmacol. 2019 Oct;96(4):419-429. doi: 10.1124/mol.119.116855. PMID: 31467029; PMCID: PMC6726458.
Miyashita T, Reed JC. Tumor suppressor p53 is a direct transcriptional activator of the human bax gene. Cell. 1995 Jan 27;80(2):293-9. doi: 10.1016/0092-8674(95)90412-3. PMID: 7834749.
Cain K, Brown DG, Langlais C, et al. Caspase activation involves the formation of the aposome, a large (approximately 700 kDa) caspase-activating complex. J Biol Chem. 1999 Aug 6;274(32):22686-92. doi: 10.1074/jbc.274.32.22686. PMID: 10428850.
Li P, Nijhawan D, Budihardjo I, et al. Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade. Cell. 1997 Nov 14;91(4):479-89. doi: 10.1016/s0092-8674(00)80434-1. PMID: 9390557.
Bratton SB, Walker G, Srinivasula SM, et al. Recruitment, activation and retention of caspases-9 and -3 by Apaf-1 apoptosome and associated XIAP complexes. EMBO J. 2001 Mar 1;20(5):998-1009. doi: 10.1093/emboj/20.5.998. PMID: 11230124; PMCID: PMC145489.
Srinivasula SM, Hegde R, Saleh A, et al. A conserved XIAP-interaction motif in caspase-9 and Smac/DIABLO regulates caspase activity and apoptosis. Nature. 2001 Mar 1;410(6824):112-6. doi: 10.1038/35065125. Erratum in: Nature 2001 Jun 28;411(6841):1081. PMID: 11242052.
Slee EA, Harte MT, Kluck RM, et al. Ordering the cytochrome c-initiated caspase cascade: hierarchical activation of caspases-2, -3, -6, -7, -8, and -10 in a caspase-9-dependent manner. J Cell Biol. 1999 Jan 25;144(2):281-92. doi: 10.1083/jcb.144.2.281. PMID: 9922454; PMCID: PMC2132895.
Gon S, Gatanaga T, Sendo F. Involvement of two types of TNF receptor in TNF-alpha induced neutrophil apoptosis. Microbiol Immunol. 1996;40(6):463-5. doi: 10.1111/j.1348-0421.1996.tb01095.x. PMID: 8839434.
Itoh N, Yonehara S, Ishii A, et al. The polypeptide encoded by the cDNA for human cell surface antigen Fas can mediate apoptosis. Cell. 1991 Jul 26;66(2):233-43. doi: 10.1016/0092-8674(91)90614-5. PMID: 1713127.
Suliman A, Lam A, Datta R, et al. Intracellular mechanisms of TRAIL: apoptosis through mitochondrial-dependent and -independent pathways. Oncogene. 2001 Apr 19;20(17):2122-33. doi: 10.1038/sj.onc.1204282. PMID: 11360196.
Vanden Berghe T, van Loo G, Saelens X, et al. Differential signaling to apoptotic and necrotic cell death by Fas-associated death domain protein FADD. J Biol Chem. 2004 Feb 27;279(9):7925-33. doi: 10.1074/jbc.M307807200. Epub 2003 Dec 10. PMID: 14668343.
Irmler M, Thome M, Hahne M, et al. Inhibition of death receptor signals by cellular FLIP. Nature. 1997 Jul 10;388(6638):190-5. doi: 10.1038/40657. PMID: 9217161.
Micheau O, Tschopp J. Induction of TNF receptor I-mediated apoptosis via two sequential signaling complexes. Cell. 2003 Jul 25;114(2):181-90. doi: 10.1016/s0092-8674(03)00521-x. PMID: 12887920.
Wang L, Du F, Wang X. TNF-alpha induces two distinct caspase-8 activation pathways. Cell. 2008 May 16;133(4):693-703. doi: 10.1016/j.cell.2008.03.036. PMID: 18485876.
Medema JP, Scaffidi C, Kischkel FC, et al. FLICE is activated by association with the CD95 death-inducing signaling complex (DISC). EMBO J. 1997 May 15;16(10):2794-804. doi: 10.1093/emboj/16.10.2794. PMID: 9184224; PMCID: PMC1169888.
Srinivasula SM, Ahmad M, Fernandes-Alnemri T, et al. Molecular ordering of the Fas-apoptotic pathway: the Fas/APO-1 protease Mch5 is a CrmA-inhibitable protease that activates multiple Ced-3/ICE-like cysteine proteases. Proc Natl Acad Sci U S A. 1996 Dec 10;93(25):14486-91. doi: 10.1073/pnas.93.25.14486. PMID: 8962078; PMCID: PMC26159.
Luo X, Budihardjo I, Zou H, et al. Bid, a Bcl2 interacting protein, mediates cytochrome c release from mitochondria in response to activation of cell surface death receptors. Cell. 1998 Aug 21;94(4):481-90. doi: 10.1016/s0092-8674(00)81589-5. PMID: 9727491.
Kaiser WJ, Daley-Bauer LP, Thapa RJ, et al. RIP1 suppresses innate immune necrotic as well as apoptotic cell death during mammalian parturition. Proc Natl Acad Sci U S A. 2014 May 27;111(21):7753-8. doi: 10.1073/pnas.1401857111. Epub 2014 May 12. PMID: 24821786; PMCID: PMC4040608.
Muzio M, Chinnaiyan AM, Kischkel FC, et al. FLICE, a novel FADD-homologous ICE/CED-3-like protease, is recruited to the CD95 (Fas/APO-1) death--inducing signaling complex. Cell. 1996 Jun 14;85(6):817-27. doi: 10.1016/s0092-8674(00)81266-0. PMID: 8681377.
Blomgran R, Zheng L, Stendahl O. Cathepsin-cleaved Bid promotes apoptosis in human neutrophils via oxidative stress-induced lysosomal membrane permeabilization. J Leukoc Biol. 2007 May;81(5):1213-23. doi: 10.1189/jlb.0506359. Epub 2007 Jan 30. PMID: 17264306.
Chen M, He H, Zhan S, et al. Bid is cleaved by calpain to an active fragment in vitro and during myocardial ischemia/reperfusion. J Biol Chem. 2001 Aug 17;276(33):30724-8. doi: 10.1074/jbc.M103701200. Epub 2001 Jun 12. PMID: 11404357.
Reiners JJ Jr, Caruso JA, Mathieu P, et al. Release of cytochrome c and activation of pro-caspase-9 following lysosomal photodamage involves Bid cleavage. Cell Death Differ. 2002 Sep;9(9):934-44. doi: 10.1038/sj.cdd.4401048. PMID: 12181744; PMCID: PMC4569095.
Fulda S. Promises and Challenges of Smac Mimetics as Cancer Therapeutics. Clin Cancer Res. 2015 Nov 15;21(22):5030-6. doi: 10.1158/1078-0432.CCR-15-0365. PMID: 26567362.
Carneiro BA, El-Deiry WS. Targeting apoptosis in cancer therapy. Nat Rev Clin Oncol. 2020 Jul;17(7):395-417. doi: 10.1038/s41571-020-0341-y. Epub 2020 Mar 23. PMID: 32203277; PMCID: PMC8211386.
Abedini MR, Muller EJ, Brun J, et al. Cisplatin induces p53-dependent FLICE-like inhibitory protein ubiquitination in ovarian cancer cells. Cancer Res. 2008 Jun 15;68(12):4511-7. doi: 10.1158/0008-5472.CAN-08-0673. PMID: 18559494.
Boice A, Bouchier-Hayes L. Targeting apoptotic caspases in cancer. Biochim Biophys Acta Mol Cell Res. 2020 Jun;1867(6):118688. doi: 10.1016/j.bbamcr.2020.118688. Epub 2020 Feb 19. PMID: 32087180; PMCID: PMC7155770.
Thome M, Schneider P, Hofmann K, et al. Viral FLICE-inhibitory proteins (FLIPs) prevent apoptosis induced by death receptors. Nature. 1997 Apr 3;386(6624):517-21. doi: 10.1038/386517a0. PMID: 9087414.
Goldmacher VS, Bartle LM, Skaletskaya A, et al. A cytomegalovirus-encoded mitochondria-localized inhibitor of apoptosis structurally unrelated to Bcl-2. Proc Natl Acad Sci U S A. 1999 Oct 26;96(22):12536-41. doi: 10.1073/pnas.96.22.12536. PMID: 10535957; PMCID: PMC22976.
Schweichel JU, Merker HJ. The morphology of various types of cell death in prenatal tissues. Teratology. 1973 Jun;7(3):253-66. doi: 10.1002/tera.1420070306. PMID: 4807128.
Kist M, Vucic D. Cell death pathways: intricate connections and disease implications. EMBO J. 2021 Mar 1;40(5):e106700. doi: 10.15252/embj.2020106700. Epub 2021 Jan 13. PMID: 33439509; PMCID: PMC7917554.
Kuma A, Komatsu M, Mizushima N. Autophagy-monitoring and autophagy-deficient mice. Autophagy. 2017 Oct 3;13(10):1619-1628. doi: 10.1080/15548627.2017.1343770. Epub 2017 Aug 18. PMID: 28820286; PMCID: PMC5640176.
Zachari M, Ganley IG. The mammalian ULK1 complex and autophagy initiation. Essays Biochem. 2017 Dec 12;61(6):585-596. doi: 10.1042/EBC20170021. PMID: 29233870; PMCID: PMC5869855.
Galluzzi L, Green DR. Autophagy-Independent Functions of the Autophagy Machinery. Cell. 2019 Jun 13;177(7):1682-1699. doi: 10.1016/j.cell.2019.05.026. PMID: 31199916; PMCID: PMC7173070.
Galluzzi L, Vitale I, Aaronson SA, et al. Molecular mechanisms of cell death: recommendations of the Nomenclature Committee on Cell Death 2018. Cell Death Differ. 2018 Mar;25(3):486-541. doi: 10.1038/s41418-017-0012-4. Epub 2018 Jan 23. PMID: 29362479; PMCID: PMC5864239.
Dasari SK, Bialik S, Levin-Zaidman S, et al. Signalome-wide RNAi screen identifies GBA1 as a positive mediator of autophagic cell death. Cell Death Differ. 2017 Jul;24(7):1288-1302. doi: 10.1038/cdd.2017.80. Epub 2017 Jun 2. PMID: 28574511; PMCID: PMC5520177.
Liu Y, Shoji-Kawata S, Sumpter RM Jr, et al. Autosis is a Na+,K+-ATPase-regulated form of cell death triggered by autophagy-inducing peptides, starvation, and hypoxia-ischemia. Proc Natl Acad Sci U S A. 2013 Dec 17;110(51):20364-71. doi: 10.1073/pnas.1319661110. Epub 2013 Nov 25. PMID: 24277826; PMCID: PMC3870705.
Bialik S, Dasari SK, Kimchi A. Autophagy-dependent cell death - where, how and why a cell eats itself to death. J Cell Sci. 2018 Sep 20;131(18):jcs215152. doi: 10.1242/jcs.215152. PMID: 30237248.
Denton D, Kumar S. Autophagy-dependent cell death. Cell Death Differ. 2019 Mar;26(4):605-616. doi: 10.1038/s41418-018-0252-y. Epub 2018 Dec 19. PMID: 30568239; PMCID: PMC6460387.
White E. Autophagic cell death unraveled: Pharmacological inhibition of apoptosis and autophagy enables necrosis. Autophagy. 2008 May;4(4):399-401. doi: 10.4161/auto.5907. Epub 2008 Mar 13. PMID: 18367872; PMCID: PMC2696931.
Degterev A, Huang Z, Boyce M, et al. Chemical inhibitor of nonapoptotic cell death with therapeutic potential for ischemic brain injury. Nat Chem Biol. 2005 Jul;1(2):112-9. doi: 10.1038/nchembio711. Epub 2005 May 29. Erratum in: Nat Chem Biol. 2005 Sep;1(4):234. PMID: 16408008.
Fleming A, Bourdenx M, Fujimaki M, et al. The different autophagy degradation pathways and neurodegeneration. Neuron. 2022 Mar 16;110(6):935-966. doi: 10.1016/j.neuron.2022.01.017. Epub 2022 Feb 7. PMID: 35134347; PMCID: PMC8930707.
Aits S, Jäättelä M. Lysosomal cell death at a glance. J Cell Sci. 2013 May 1;126(Pt 9):1905-12. doi: 10.1242/jcs.091181. PMID: 23720375.
Xie Z, Zhao M, Yan C, et al. Cathepsin B in programmed cell death machinery: mechanisms of execution and regulatory pathways. Cell Death Dis. 2023 Apr 8;14(4):255. doi: 10.1038/s41419-023-05786-0. PMID: 37031185; PMCID: PMC10082344.
Pan C, Banerjee K, Lehmann GL, et al. Lipofuscin causes atypical necroptosis through lysosomal membrane permeabilization. Proc Natl Acad Sci U S A. 2021 Nov 23;118(47):e2100122118. doi: 10.1073/pnas.2100122118. PMID: 34782457; PMCID: PMC8617501.
Ryckman AE, Brockhausen I, Walia JS. Metabolism of Glycosphingolipids and Their Role in the Pathophysiology of Lysosomal Storage Disorders. Int J Mol Sci. 2020 Sep 19;21(18):6881. doi: 10.3390/ijms21186881. PMID: 32961778; PMCID: PMC7555265.
Degterev A, Hitomi J, Germscheid M, et al. Identification of RIP1 kinase as a specific cellular target of necrostatins. Nat Chem Biol. 2008 May;4(5):313-21. doi: 10.1038/nchembio.83. PMID: 18408713; PMCID: PMC5434866.
Degterev A, Maki JL, Yuan J. Activity and specificity of necrostatin-1, small-molecule inhibitor of RIP1 kinase. Cell Death Differ. 2013 Feb;20(2):366. doi: 10.1038/cdd.2012.133. Epub 2012 Nov 30. PMID: 23197295; PMCID: PMC3554332.
Bertrand MJ, Milutinovic S, Dickson KM, et al. cIAP1 and cIAP2 facilitate cancer cell survival by functioning as E3 ligases that promote RIP1 ubiquitination. Mol Cell. 2008 Jun 20;30(6):689-700. doi: 10.1016/j.molcel.2008.05.014. PMID: 18570872.
Geng J, Ito Y, Shi L, et al. Regulation of RIPK1 activation by TAK1-mediated phosphorylation dictates apoptosis and necroptosis. Nat Commun. 2017 Aug 25;8(1):359. doi: 10.1038/s41467-017-00406-w. PMID: 28842570; PMCID: PMC5572456.
Zhao J, Jitkaew S, Cai Z, et al. Mixed lineage kinase domain-like is a key receptor interacting protein 3 downstream component of TNF-induced necrosis. Proc Natl Acad Sci U S A. 2012 Apr 3;109(14):5322-7. doi: 10.1073/pnas.1200012109. Epub 2012 Mar 15. PMID: 22421439; PMCID: PMC3325682.
Kaiser WJ, Sridharan H, Huang C, et al. Toll-like receptor 3-mediated necrosis via TRIF, RIP3, and MLKL. J Biol Chem. 2013 Oct 25;288(43):31268-79. doi: 10.1074/jbc.M113.462341. Epub 2013 Sep 9. PMID: 24019532; PMCID: PMC3829437.
Vandenabeele P, Galluzzi L, Vanden Berghe T, Kroemer G. Molecular mechanisms of necroptosis: an ordered cellular explosion. Nat Rev Mol Cell Biol. 2010 Oct;11(10):700-14. doi: 10.1038/nrm2970. Epub 2010 Sep 8. PMID: 20823910.
Upton JW, Kaiser WJ, Mocarski ES. DAI/ZBP1/DLM-1 Complexes with RIP3 to Mediate Virus-Induced Programmed Necrosis that Is Targeted by Murine Cytomegalovirus vIRA. Cell Host Microbe. 2019 Oct 9;26(4):564. doi: 10.1016/j.chom.2019.09.004. PMID: 31600504.
Negroni A, Colantoni E, Cucchiara S, et al. Necroptosis in Intestinal Inflammation and Cancer: New Concepts and Therapeutic Perspectives. Biomolecules. 2020 Oct 10;10(10):1431. doi: 10.3390/biom10101431. PMID: 33050394; PMCID: PMC7599789.
Sun L, Wang H, Wang Z, et al. Mixed lineage kinase domain-like protein mediates necrosis signaling downstream of RIP3 kinase. Cell. 2012 Jan 20;148(1-2):213-27. doi: 10.1016/j.cell.2011.11.031. PMID: 22265413.
Miller DR, Cramer SD, Thorburn A. The interplay of autophagy and non-apoptotic cell death pathways. Int Rev Cell Mol Biol. 2020;352:159-187. doi: 10.1016/bs.ircmb.2019.12.004. Epub 2020 Jan 13. PMID: 32334815; PMCID: PMC8185908.
Gong Y, Fan Z, Luo G, et al. The role of necroptosis in cancer biology and therapy. Mol Cancer. 2019 May 23;18(1):100. doi: 10.1186/s12943-019-1029-8. PMID: 31122251; PMCID: PMC6532150.
Newton K, Manning G. Necroptosis and Inflammation. Annu Rev Biochem. 2016 Jun 2;85:743-63. doi: 10.1146/annurev-biochem-060815-014830. Epub 2016 Feb 8. PMID: 26865533.
Murphy JM, Czabotar PE, Hildebrand JM, et al. The pseudokinase MLKL mediates necroptosis via a molecular switch mechanism. Immunity. 2013 Sep 19;39(3):443-53. doi: 10.1016/j.immuni.2013.06.018. Epub 2013 Sep 5. PMID: 24012422.
Cai Z, Jitkaew S, Zhao J, et al. Plasma membrane translocation of trimerized MLKL protein is required for TNF-induced necroptosis. Nat Cell Biol. 2014 Jan;16(1):55-65. doi: 10.1038/ncb2883. Epub 2013 Dec 8. Erratum in: Nat Cell Biol. 2014 Feb;16(2):200. PMID: 24316671; PMCID: PMC8369836.
Chen X, Li W, Ren J, et al. Translocation of mixed lineage kinase domain-like protein to plasma membrane leads to necrotic cell death. Cell Res. 2014 Jan;24(1):105-21. doi: 10.1038/cr.2013.171. Epub 2013 Dec 24. PMID: 24366341; PMCID: PMC3879712.
Overholtzer M, Mailleux AA, Mouneimne G, et al. A nonapoptotic cell death process, entosis, that occurs by cell-in-cell invasion. Cell. 2007 Nov 30;131(5):966-79. doi: 10.1016/j.cell.2007.10.040. PMID: 18045538.
Zeng C, Zeng B, Dong C, et al. Rho-ROCK signaling mediates entotic cell death in tumor. Cell Death Discov. 2020 Jan 23;6:4. doi: 10.1038/s41420-020-0238-7. PMID: 32123580; PMCID: PMC7026421.
Hamann JC, Surcel A, Chen R, et al. Entosis Is Induced by Glucose Starvation. Cell Rep. 2017 Jul 5;20(1):201-210. doi: 10.1016/j.celrep.2017.06.037. PMID: 28683313; PMCID: PMC5559205.
Bozkurt E, Düssmann H, Salvucci M, et al. TRAIL signaling promotes entosis in colorectal cancer. J Cell Biol. 2021 Nov 1;220(11):e202010030. doi: 10.1083/jcb.202010030. Epub 2021 Sep 21. PMID: 34546352; PMCID: PMC8563286.
Dixon SJ, Lemberg KM, Lamprecht MR, et al. Ferroptosis: an iron-dependent form of nonapoptotic cell death. Cell. 2012 May 25;149(5):1060-72. doi: 10.1016/j.cell.2012.03.042. PMID: 22632970; PMCID: PMC3367386.
Trachootham D, Lu W, Ogasawara MA, et al. Redox regulation of cell survival. Antioxid Redox Signal. 2008 Aug;10(8):1343-74. doi: 10.1089/ars.2007.1957. PMID: 18522489; PMCID: PMC2932530.
Sato M, Kusumi R, Hamashima S, et al. The ferroptosis inducer erastin irreversibly inhibits system xc- and synergizes with cisplatin to increase cisplatin's cytotoxicity in cancer cells. Sci Rep. 2018 Jan 17;8(1):968. doi: 10.1038/s41598-018-19213-4. PMID: 29343855; PMCID: PMC5772355.
Ayala A, Muñoz MF, Argüelles S. Lipid peroxidation: production, metabolism, and signaling mechanisms of malondialdehyde and 4-hydroxy-2-nonenal. Oxid Med Cell Longev. 2014;360438. doi: 10.1155/2014/360438. Epub 2014 May 8. PMID: 24999379; PMCID: PMC4066722.
Zhang H, Morgan TE, Forman HJ. Age-related alteration in HNE elimination enzymes. Arch Biochem Biophys. 2021 Mar 15;699:108749. doi: 10.1016/j.abb.2020.108749. Epub 2021 Jan 5. PMID: 33417945.
Zheng H, Jiang L, Tsuduki T, et al. Embryonal erythropoiesis and aging exploit ferroptosis. Redox Biol. 2021 Oct 30;48:102175. doi: 10.1016/j.redox.2021.102175. Epub ahead of print. PMID: 34736120; PMCID: PMC8577445.
Coyle JT, Puttfarcken P. Oxidative stress, glutamate, and neurodegenerative disorders. Science. 1993 Oct 29;262(5134):689-95. doi: 10.1126/science.7901908. PMID: 7901908.
Dmitriev LF, Titov VN. Lipid peroxidation in relation to ageing and the role of endogenous aldehydes in diabetes and other age-related diseases. Ageing Res Rev. 2010 Apr;9(2):200-10. doi: 10.1016/j.arr.2009.09.004. Epub 2009 Oct 1. PMID: 19800421.
Matak P, Matak A, Moustafa S, et al. Disrupted iron homeostasis causes dopaminergic neurodegeneration in mice. Proc Natl Acad Sci U S A. 2016 Mar 29;113(13):3428-35. doi: 10.1073/pnas.1519473113. Epub 2016 Feb 29. PMID: 26929359; PMCID: PMC4822577.
Cozzi A, Rovelli E, Frizzale G, et al. Oxidative stress and cell death in cells expressing L-ferritin variants causing neuroferritinopathy. Neurobiol Dis. 2010 Jan;37(1):77-85. doi: 10.1016/j.nbd.2009.09.009. Epub 2009 Sep 23. PMID: 19781644.
Ryan SK, Zelic M, Han Y, et al. Microglia ferroptosis is regulated by SEC24B and contributes to neurodegeneration. Nat Neurosci. 2023 Jan;26(1):12-26. doi: 10.1038/s41593-022-01221-3. Epub 2022 Dec 19. PMID: 36536241; PMCID: PMC9829540.
Tsvetkov P, Coy S, Petrova B, et al. Copper induces cell death by targeting lipoylated TCA cycle proteins. Science. 2022 Mar 18;375(6586):1254-1261. doi: 10.1126/science.abf0529. Epub 2022 Mar 17. Erratum in: Science. 2022 Apr 22;376(6591):eabq4855. doi: 10.1126/science.abq4855. PMID: 35298263; PMCID: PMC9273333.
Ge EJ, Bush AI, Casini A, et al. Connecting copper and cancer: from transition metal signalling to metalloplasia. Nat Rev Cancer. 2022 Feb;22(2):102-113. doi: 10.1038/s41568-021-00417-2. Epub 2021 Nov 11. PMID: 34764459; PMCID: PMC8810673.
Tsvetkov P, Detappe A, Cai K, et al. Mitochondrial metabolism promotes adaptation to proteotoxic stress. Nat Chem Biol. 2019 Jul;15(7):681-689. doi: 10.1038/s41589-019-0291-9. Epub 2019 May 27. Erratum in: Nat Chem Biol. 2019 Jul;15(7):757. doi: 10.1038/s41589-019-0315-5. PMID: 31133756; PMCID: PMC8183600.
Gao W, Huang Z, Duan J, et al. Elesclomol induces copper-dependent ferroptosis in colorectal cancer cells via degradation of ATP7A. Mol Oncol. 2021 Dec;15(12):3527-3544. doi: 10.1002/1878-0261.13079. Epub 2021 Sep 15. PMID: 34390123; PMCID: PMC8637554.
Tong X, Tang R, Xiao M, et al. Targeting cell death pathways for cancer therapy: recent developments in necroptosis, pyroptosis, ferroptosis, and cuproptosis research. J Hematol Oncol. 2022 Dec 8;15(1):174. doi: 10.1186/s13045-022-01392-3. PMID: 36482419; PMCID: PMC9733270.
Degterev A, Boyce M, Yuan J. A decade of caspases. Oncogene. 2003 Nov 24;22(53):8543-67. doi: 10.1038/sj.onc.1207107. PMID: 14634618.
Yuan J, Najafov A, Py BF. Roles of Caspases in Necrotic Cell Death. Cell. 2016 Dec 15;167(7):1693-1704. doi: 10.1016/j.cell.2016.11.047. PMID: 27984721; PMCID: PMC5381727.
Wang S, Miura M, Jung YK, et al. Murine caspase-11, an ICE-interacting protease, is essential for the activation of ICE. Cell. 1998 Feb 20;92(4):501-9. doi: 10.1016/s0092-8674(00)80943-5. PMID: 9491891.
Kang SJ, Wang S, Hara H, et al. Dual role of caspase-11 in mediating activation of caspase-1 and caspase-3 under pathological conditions. J Cell Biol. 2000 May 1;149(3):613-22. doi: 10.1083/jcb.149.3.613. PMID: 10791975; PMCID: PMC2174843.
Kang SJ, Wang S, Hara H, et al. Dual role of caspase-11 in mediating activation of caspase-1 and caspase-3 under pathological conditions. J Cell Biol. 2000 May 1;149(3):613-22. doi: 10.1083/jcb.149.3.613. PMID: 10791975; PMCID: PMC2174843.
Broz P, Pelegrín P, Shao F. The gasdermins, a protein family executing cell death and inflammation. Nat Rev Immunol. 2020 Mar;20(3):143-157. doi: 10.1038/s41577-019-0228-2. Epub 2019 Nov 5. PMID: 31690840.
Ding J, Wang K, Liu W, et al. Pore-forming activity and structural autoinhibition of the gasdermin family. Nature. 2016 Jul 7;535(7610):111-6. doi: 10.1038/nature18590. Epub 2016 Jun 8. Erratum in: Nature. 2016 Dec 1;540(7631):150. doi: 10.1038/nature20106. PMID: 27281216.
Liu X, Zhang Z, Ruan J, et al. Inflammasome-activated gasdermin D causes pyroptosis by forming membrane pores. Nature. 2016 Jul 7;535(7610):153-8. doi: 10.1038/nature18629. PMID: 27383986; PMCID: PMC5539988.
Xia S, Zhang Z, Magupalli VG, et al. Gasdermin D pore structure reveals preferential release of mature interleukin-1. Nature. 2021 May;593(7860):607-611. doi: 10.1038/s41586-021-03478-3. Epub 2021 Apr 21. PMID: 33883744; PMCID: PMC8588876.
He WT, Wan H, Hu L, et al. Gasdermin D is an executor of pyroptosis and required for interleukin-1β secretion. Cell Res. 2015 Dec;25(12):1285-98. doi: 10.1038/cr.2015.139. Epub 2015 Nov 27. PMID: 26611636; PMCID: PMC4670995.
Moonen S, Koper MJ, Van Schoor E, et al. Pyroptosis in Alzheimer's disease: cell type-specific activation in microglia, astrocytes and neurons. Acta Neuropathol. 2023 Feb;145(2):175-195. doi: 10.1007/s00401-022-02528-y. Epub 2022 Dec 9. Erratum in: Acta Neuropathol. 2024 Dec 23;149(1):3. doi: 10.1007/s00401-024-02841-8. PMID: 36481964.
Boucher D, Monteleone M, Coll RC, et al.Caspase-1 self-cleavage is an intrinsic mechanism to terminate inflammasome activity. J Exp Med. 2018 Mar 5;215(3):827-840. doi: 10.1084/jem.20172222. Epub 2018 Feb 6. PMID: 29432122; PMCID: PMC5839769.
Aglietti RA, Estevez A, Gupta A, et al. GsdmD p30 elicited by caspase-11 during pyroptosis forms pores in membranes. Proc Natl Acad Sci U S A. 2016 Jul 12;113(28):7858-63. doi: 10.1073/pnas.1607769113. Epub 2016 Jun 23. PMID: 27339137; PMCID: PMC4948338.
Kayagaki N, Stowe IB, Lee BL, et al. Caspase-11 cleaves gasdermin D for non-canonical inflammasome signalling. Nature. 2015 Oct 29;526(7575):666-71. doi: 10.1038/nature15541. Epub 2015 Sep 16. PMID: 26375259.
Shi J, Zhao Y, Wang K, et al. Cleavage of GSDMD by inflammatory caspases determines pyroptotic cell death. Nature. 2015 Oct 29;526(7575):660-5. doi: 10.1038/nature15514. Epub 2015 Sep 16. PMID: 26375003.
Shi J, Zhao Y, Wang K, et al. Cleavage of GSDMD by inflammatory caspases determines pyroptotic cell death. Nature. 2015 Oct 29;526(7575):660-5. doi: 10.1038/nature15514. Epub 2015 Sep 16. PMID: 26375003.
Santos JC, Dick MS, Lagrange B, et al. LPS targets host guanylate-binding proteins to the bacterial outer membrane for non-canonical inflammasome activation. EMBO J. 2018 Mar 15;37(6):e98089. doi: 10.15252/embj.201798089. Epub 2018 Feb 19. PMID: 29459437; PMCID: PMC5852652.
Franklin BS, Bossaller L, De Nardo D, et al. The adaptor ASC has extracellular and 'prionoid' activities that propagate inflammation. Nat Immunol. 2014 Aug;15(8):727-37. doi: 10.1038/ni.2913. Epub 2014 Jun 22. PMID: 24952505; PMCID: PMC4116676.
Baroja-Mazo A, Martín-Sánchez F, Gomez AI, Martínez CM, et al. The NLRP3 inflammasome is released as a particulate danger signal that amplifies the inflammatory response. Nat Immunol. 2014 Aug;15(8):738-48. doi: 10.1038/ni.2919. Epub 2014 Jun 22. PMID: 24952504.
Heneka MT, Kummer MP, Stutz A, et al. NLRP3 is activated in Alzheimer's disease and contributes to pathology in APP/PS1 mice. Nature. 2013 Jan 31;493(7434):674-8. doi: 10.1038/nature11729. Epub 2012 Dec 19. PMID: 23254930; PMCID: PMC3812809.