Fluorizoline-induced apoptosis requires prohibitins in nematodes and human cells.


Journal

Apoptosis : an international journal on programmed cell death
ISSN: 1573-675X
Titre abrégé: Apoptosis
Pays: Netherlands
ID NLM: 9712129

Informations de publication

Date de publication:
02 2021
Historique:
accepted: 11 12 2020
pubmed: 3 1 2021
medline: 23 11 2021
entrez: 2 1 2021
Statut: ppublish

Résumé

We previously showed that fluorizoline, a fluorinated thiazoline compound, binds to both subunits of the mitochondrial prohibitin (PHB) complex, PHB1 and PHB2, being the expression of these proteins required for fluorizoline-induced apoptosis in mouse embryonic fibroblasts. To investigate the conservation of this apoptotic mechanism, we studied the effect of PHB downregulation on fluorizoline activity on two human cell lines, HEK293T and U2OS. Then, we asked whether PHBs mediate the effect of fluorizoline in a multicellular organism. Interestingly, reduced levels of PHBs in the human cells impaired the induction of apoptosis by fluorizoline. We observed that fluorizoline has a detrimental dose-dependent effect on the development and survival of the nematode model Caenorhabditis elegans. Besides, such effects of fluorizoline treatment in living nematodes were absent in PHB mutants. Finally, we further explored the apoptotic pathway triggered by fluorizoline in human cell lines. We found that the BH3-only proteins NOXA, BIM and PUMA participate in fluorizoline-induced apoptosis and that the induction of NOXA and PUMA is dependent on PHB expression.

Identifiants

pubmed: 33387147
doi: 10.1007/s10495-020-01651-z
pii: 10.1007/s10495-020-01651-z
doi:

Substances chimiques

Caenorhabditis elegans Proteins 0
PHB protein, human 0
PHB2 protein, human 0
Phb2 protein, mouse 0
Prohibitins 0
Repressor Proteins 0
Thiazolidines 0
prohibitin 2, C elegans 0

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

83-95

Références

Hanahan D, Weinberg RA (2011) Hallmarks of cancer: the next generation. Cell 144:646–674. https://doi.org/10.1016/j.cell.2011.02.013
doi: 10.1016/j.cell.2011.02.013
Muller PAJ, Vousden KH (2013) P53 mutations in cancer. Nat Cell Biol 15:2–8
doi: 10.1038/ncb2641
Pérez-Perarnau A, Preciado S, Palmeri CM et al (2014) A trifluorinated thiazoline scaffold leading to pro-apoptotic agents targeting prohibitins. Angew Chem Int Ed 53:10150–10154. https://doi.org/10.1002/anie.201405758
doi: 10.1002/anie.201405758
Pomares H, Palmeri CM, Iglesias-Serret D et al (2016) Targeting prohibitins induces apoptosis in acute myeloid leukemia cells. Oncotarget 7:64987–65000. https://doi.org/10.18632/oncotarget.11333
doi: 10.18632/oncotarget.11333 pubmed: 27542247 pmcid: 5323132
Cosialls AM, Pomares H, Iglesias-Serret D et al (2017) The prohibitin-binding compound fluorizoline induces apoptosis in chronic lymphocytic leukemia cells through the upregulation of NOXA and synergizes with ibrutinib, 5-aminoimidazole-4-carboxamide riboside or venetoclax. Haematologica 102:1587–1593. https://doi.org/10.3324/haematol.2016.162958
doi: 10.3324/haematol.2016.162958 pubmed: 28619845 pmcid: 5685241
Wierz M, Pierson S, Chouha N et al (2018) The prohibitin-binding compound fluorizoline induces apoptosis in chronic lymphocytic leukemia cells ex vivo but fails to prevent leukemia development in a murine model. Haematologica 103:e154–e157
doi: 10.3324/haematol.2017.175349
Moncunill-Massaguer C, Saura-Esteller J, Pérez-Perarnau A et al (2015) A novel prohibitin-binding compound induces the mitochondrial apoptotic pathway through NOXA and BIM upregulation. Oncotarget 6:41750–41765. https://doi.org/10.18632/oncotarget.6154
doi: 10.18632/oncotarget.6154 pubmed: 26497683 pmcid: 4747186
Wang D, Tabti R, Elderwish S et al (2020) Prohibitin ligands: a growing armamentarium to tackle cancers, osteoporosis, inflammatory, cardiac and neurological diseases. Cell Mol Life Sci. https://doi.org/10.1007/s00018-020-03475-1
doi: 10.1007/s00018-020-03475-1 pubmed: 33226440 pmcid: 7588389
Thuaud F, Ribeiro N, Nebigil CG, Désaubry L (2013) Prohibitin ligands in cell death and survival: mode of action and therapeutic potential. Chem Biol 20:316–331
doi: 10.1016/j.chembiol.2013.02.006
Yang J, Li B, He QY (2018) Significance of prohibitin domain family in tumorigenesis and its implication in cancer diagnosis and treatment review-article. Cell Death Dis 9:580
doi: 10.1038/s41419-018-0661-3
Signorile A, Sgaramella G, Bellomo F, De Rasmo D (2019) Prohibitins: a critical role in mitochondrial functions and implication in diseases. Cells 8:71. https://doi.org/10.3390/cells8010071
doi: 10.3390/cells8010071 pmcid: 6356732
Peng Y-T, Chen P, Ouyang R-Y, Song L (2015) Multifaceted role of prohibitin in cell survival and apoptosis. Apoptosis 20:1135–1149. https://doi.org/10.1007/s10495-015-1143-z
doi: 10.1007/s10495-015-1143-z pubmed: 26091791 pmcid: 4531144
Wei Y, Chiang W-C, Sumpter R et al (2017) Prohibitin 2 is an inner mitochondrial membrane mitophagy receptor. Cell 168:224-238.e10. https://doi.org/10.1016/j.cell.2016.11.042
doi: 10.1016/j.cell.2016.11.042 pubmed: 28017329
Hernando-Rodríguez B, Artal-Sanz M (2018) Mitochondrial quality control mechanisms and the PHB (Prohibitin). Complex Cells 7:238. https://doi.org/10.3390/cells7120238
doi: 10.3390/cells7120238
Nijtmans LGJ, Artal Sanz M, Grivell LA, Coates PJ (2002) The mitochondrial PHB complex: roles in mitochondrial respiratory complex assembly, ageing and degenerative disease. Cell Mol Life Sci 59:143–155
doi: 10.1007/s00018-002-8411-0
Chowdhury I, Thompson WE, Welch C et al (2013) Prohibitin (PHB) inhibits apoptosis in rat granulosa cells (GCs) through the extracellular signal-regulated kinase 1/2 (ERK1/2) and the Bcl family of proteins. Apoptosis 18:1513–1525. https://doi.org/10.1007/s10495-013-0901-z
doi: 10.1007/s10495-013-0901-z pubmed: 24096434 pmcid: 3825582
McClung JK, Danner DB, Stewart DA et al (1989) Isolation of a cDNA that hybrid selects antiproliferative mRNA from rat liver. Biochem Biophys Res Commun 164:1316–1322. https://doi.org/10.1016/0006-291X(89)91813-5
doi: 10.1016/0006-291X(89)91813-5 pubmed: 2480116
Liu P, Xu Y, Zhang W et al (2017) Prohibitin promotes androgen receptor activation in ER-positive breast cancer. Cell Cycle 16:776–784. https://doi.org/10.1080/15384101.2017.1295193
doi: 10.1080/15384101.2017.1295193 pubmed: 28272969 pmcid: 5405713
Cao Y, Liang H, Zhang F et al (2016) Prohibitin overexpression predicts poor prognosis and promotes cell proliferation and invasion through ERK pathway activation in gallbladder cancer. J Exp Clin Cancer Res. https://doi.org/10.1186/s13046-016-0346-7
doi: 10.1186/s13046-016-0346-7 pubmed: 27596051 pmcid: 5011911
Fu P, Yang Z, Bach LA (2013) Prohibitin-2 binding modulates insulin-like growth factor-binding protein-6 (IGFBP-6)-induced rhabdomyosarcoma cell migration. J Biol Chem 288:29890–29900. https://doi.org/10.1074/jbc.M113.510826
doi: 10.1074/jbc.M113.510826 pubmed: 24003225 pmcid: 3795287
Chiu CF, Ho MY, Peng JM et al (2013) Raf activation by Ras and promotion of cellular metastasis require phosphorylation of prohibitin in the raft domain of the plasma membrane. Oncogene 32:777–787. https://doi.org/10.1038/onc.2012.86
doi: 10.1038/onc.2012.86 pubmed: 22410782
Merkwirth C, Dargazanli S, Tatsuta T et al (2008) Prohibitins control cell proliferation and apoptosis by regulating OPA1-dependent cristae morphogenesis in mitochondria. Genes Dev 22:476–488. https://doi.org/10.1101/gad.460708
doi: 10.1101/gad.460708 pubmed: 18281461 pmcid: 2238669
Sanz MA, Tsang WY, Willems EM et al (2003) The mitochondrial prohibitin complex is essential for embryonic viability and germline function in Caenorhabditis elegans. J Biol Chem 278:32091–32099. https://doi.org/10.1074/jbc.M304877200
doi: 10.1074/jbc.M304877200 pubmed: 12794069
Ran FA, Hsu PD, Wright J et al (2013) Genome engineering using the CRISPR-Cas9 system. Nat Protoc 8:2281–2308. https://doi.org/10.1038/nprot.2013.143
doi: 10.1038/nprot.2013.143 pubmed: 24157548 pmcid: 3969860
Brenner S (1974) The genetics of Caenorabditis elegans. Genetics. https://doi.org/10.1016/S0047-2484(78)80101-8
doi: 10.1016/S0047-2484(78)80101-8 pubmed: 4858229 pmcid: 1213121
Porta-de-la-Riva M, Fontrodona L, Villanueva A, Cerón J (2012) Basic Caenorhabditis elegans methods: synchronization and observation. J Vis Exp. https://doi.org/10.3791/4019
doi: 10.3791/4019 pubmed: 22710399 pmcid: 3607348
Hernando-Rodríguez B, Erinjeri AP, Rodríguez-Palero MJ et al (2018) Combined flow cytometry and high-throughput image analysis for the study of essential genes in Caenorhabditis elegans. BMC Biol 16:36. https://doi.org/10.1186/s12915-018-0496-5
doi: 10.1186/s12915-018-0496-5 pubmed: 29598825 pmcid: 5875015
Artal-Sanz M, Tavernarakis N (2009) Prohibitin couples diapause signalling to mitochondrial metabolism during ageing in C. elegans. Nature 461:793–797. https://doi.org/10.1038/nature08466
doi: 10.1038/nature08466 pubmed: 19812672
Zubovych I, Doundoulakis T, Harran PG, Roth MG (2006) A missense mutation in Caenorhabditis elegans prohibitin 2 confers an atypical multidrug resistance. Proc Natl Acad Sci USA 103:15523–15528. https://doi.org/10.1073/pnas.0607338103
doi: 10.1073/pnas.0607338103 pubmed: 17032754
Zubovych IO, Straud S, Roth MG (2010) Mitochondrial dysfunction confers resistance to multiple drugs in Caenorhabditis elegans. Mol Biol Cell 21:956–969. https://doi.org/10.1091/mbc.E09-08-0673
doi: 10.1091/mbc.E09-08-0673 pubmed: 20089839 pmcid: 2836976
Birkinshaw RW, Czabotar PE (2017) The BCL-2 family of proteins and mitochondrial outer membrane permeabilisation. Semin Cell Dev Biol 72:152–162
doi: 10.1016/j.semcdb.2017.04.001

Auteurs

José Saura-Esteller (J)

Departament de Ciències Fisiològiques, Facultat de Medicina i Ciències de la Salut, Universitat de Barcelona-IDIBELL (Institut d'Investigació Biomèdica de Bellvitge), L'Hospitalet de Llobregat, Barcelona, Spain.

Ismael Sánchez-Vera (I)

Departament de Ciències Fisiològiques, Facultat de Medicina i Ciències de la Salut, Universitat de Barcelona-IDIBELL (Institut d'Investigació Biomèdica de Bellvitge), L'Hospitalet de Llobregat, Barcelona, Spain.

Sonia Núñez-Vázquez (S)

Departament de Ciències Fisiològiques, Facultat de Medicina i Ciències de la Salut, Universitat de Barcelona-IDIBELL (Institut d'Investigació Biomèdica de Bellvitge), L'Hospitalet de Llobregat, Barcelona, Spain.

Judith Jabalquinto-Carrasco (J)

Departament de Ciències Fisiològiques, Facultat de Medicina i Ciències de la Salut, Universitat de Barcelona-IDIBELL (Institut d'Investigació Biomèdica de Bellvitge), L'Hospitalet de Llobregat, Barcelona, Spain.

Ana M Cosialls (AM)

Departament de Ciències Fisiològiques, Facultat de Medicina i Ciències de la Salut, Universitat de Barcelona-IDIBELL (Institut d'Investigació Biomèdica de Bellvitge), L'Hospitalet de Llobregat, Barcelona, Spain.

Lorena Mendive-Tapia (L)

Laboratory of Medical Chemistry, Faculty of Pharmacy and Food Sciences, Institute of Medicine (IBUB), University of Barcelona, Barcelona, Spain.

Dmytro Kukhtar (D)

Modeling Human Diseases in C. Elegans Group. Genes, Disease and Therapy Program, IDIBELL (Institut d'Investigació Biomèdica de Bellvitge), L'Hospitalet de Llobregat, Barcelona, Spain.

Manuel D Martínez-Bueno (MD)

Andalusian Center for Developmental Biology, Consejo Superior de Investigaciones Científicas/Junta de Andalucía, Universidad Pablo de Olavide, Seville, Spain.
Department of Molecular Biology and Biochemical Engineering, Universidad Pablo de Olavide, Seville, Spain.

Rodolfo Lavilla (R)

Laboratory of Medical Chemistry, Faculty of Pharmacy and Food Sciences, Institute of Medicine (IBUB), University of Barcelona, Barcelona, Spain.

Julián Cerón (J)

Modeling Human Diseases in C. Elegans Group. Genes, Disease and Therapy Program, IDIBELL (Institut d'Investigació Biomèdica de Bellvitge), L'Hospitalet de Llobregat, Barcelona, Spain.

Marta Artal-Sanz (M)

Andalusian Center for Developmental Biology, Consejo Superior de Investigaciones Científicas/Junta de Andalucía, Universidad Pablo de Olavide, Seville, Spain.
Department of Molecular Biology and Biochemical Engineering, Universidad Pablo de Olavide, Seville, Spain.

Gabriel Pons (G)

Departament de Ciències Fisiològiques, Facultat de Medicina i Ciències de la Salut, Universitat de Barcelona-IDIBELL (Institut d'Investigació Biomèdica de Bellvitge), L'Hospitalet de Llobregat, Barcelona, Spain.

Daniel Iglesias-Serret (D)

Departament de Ciències Fisiològiques, Facultat de Medicina i Ciències de la Salut, Universitat de Barcelona-IDIBELL (Institut d'Investigació Biomèdica de Bellvitge), L'Hospitalet de Llobregat, Barcelona, Spain.
Facultat de Medicina, Universitat de Vic-Universitat Central de Catalunya (UVic-UCC), Vic, Barcelona, Spain.

Joan Gil (J)

Departament de Ciències Fisiològiques, Facultat de Medicina i Ciències de la Salut, Universitat de Barcelona-IDIBELL (Institut d'Investigació Biomèdica de Bellvitge), L'Hospitalet de Llobregat, Barcelona, Spain. jgil@ub.edu.

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