RIP1-HAT1-SIRT Complex Identification and Targeting in Treatment and Prevention of Cancer (245 views)
Clin Cancer Res (ISSN: 1078-0432print, 1078-0432linking), 2018 Jun 15; 24(12): 2886-2900.
Export to BibTeX Export to EndNote
Paper type: Journal Article,
Impact factor: 6.488, 5-year impact factor: 6.646
Url: https://www.scopus.com/inward/record.uri?eid=2-s2.0-85052287980&doi=10.1158%2f1078-0432.CCR-17-3081&partnerID=40&md5=40eb37bac795274af9b9ca4d6a11c13c
Keywords: 12 Dimethylbenz[a]anthracene, Caspase 8, Histone Acetyltransferase, Hydrolase Inhibitor, Mc 2494, Phosphotransferase, Rip1 Kinase, Rip3 Kinase, Sirtuin 1, Unclassified Drug, Animal Experiment, Animal Model, Apoptosis, Article, Breast Cancer, Cancer Model, Cancer Prevention, Cancer Therapy, Cell Death, Complex Formation, Controlled Study, Enzymatic Assay, Ex Vivo Study, Female, Flow Cytometry, Genetic Transfection, Human, Human Cell, Immunoprecipitation, In Vitro Study, In Vivo Study, Infant, Malignant Neoplasm, Mass Spectrometry, Mouse, Mouse Model, Mutagenesis, Nonhuman, Priority Journal, Protein Acetylation, Protein Protein Interaction, Transcriptomics, Tumor Xenograft,
Affiliations:
*** IBB - CNR ***
Dipartimento di Medicina di Precisione, Universita degli Studi della Campania "Luigi Vanvitelli", Napoli, Italy., Dipartimento di Chimica e Tecnologie del Farmaco, "Sapienza" Universita di Roma, Roma, Italy., Dipartimento di Scienze e Tecnologie Ambientali Biologiche e Farmaceutiche, Universita della Campania Luigi Vanvitelli, Caserta, Italy., Biopulse s.r.l., Napoli, Italy., SAFU Department, Regina Elena Cancer Institute, Rome, Italy., Istituto di Biostrutture e Bioimmagini, CNR, and CIRPeB, Napoli, Italy., Center of Excellence on Neurodegenerative Diseases and Department of Pharmacological Sciences, Universita di Milano, Milano, Italy., Department of Molecular Biology, Radboud University, Nijmegen, the Netherlands., Mouse and Animal Pathology Lab, Fondazione Filarete, Milano, Italy., Department of Pathobiology, School of Veterinary Medicine, University of Pennsylvania, Philadelphia, Pennsylvania., CEINGE, Naples, Italy., Dipartimento di Biochimica e Biotecnologie Mediche, Universita Federico II, Napoli, Italy., Pasteur-Fondazione Cenci Bolognetti, Sapienza Universita di Roma, Roma, Italy., Dipartimento di Medicina di Precisione, Universita degli Studi della Campania "Luigi Vanvitelli", Napoli, Italy. lucia.altucci@unicampania.it.,
References:
Galluzzi, L., Kroemer, G., Secondary necrosis: Accidental no more (2017) Trends Cancer, 3, pp. 1-
Galluzzi, L., Bravo-San Pedro, J.M., Vitale, I., Aaronson, S.A., Abrams, J.M., Adam, D., Essential versus accessory aspects of cell death: Recommendations of the NCCD 2015 (2015) Cell Death Differ, 22, pp. 58-73
Galluzzi, L., Baehrecke, E.H., Ballabio, A., Boya, P., Bravo-San Pedro, J.M., Cecconi, F., Molecular definitions of autophagy and related processes (2017) EMBO J, 36, pp. 1811-1836
Galluzzi, L., Kepp, O., Chan, F.K., Kroemer, G., Necroptosis: Mechanisms and relevance to disease (2017) Annu Rev Pathol, 12, pp. 103-130
Vandenabeele, P., Galluzzi, L., Vanden Berghe, T., Kroemer, G., Molecular mechanisms of necroptosis: An ordered cellular explosion (2010) Nat Rev Mol Cell Biol, 11, pp. 700-714
Jouan-Lanhouet, S., Riquet, F., Duprez, L., Vanden Berghe, T., Takahashi, N., Vandenabeele, P., Necroptosis, in vivo detection in experimental disease models (2014) Semin Cell Dev Biol, 35, pp. 2-13
Stanger, B.Z., Leder, P., Lee, T.H., Kim, E., Seed, B., RIP: A novel protein containing a death domain that interacts with Fas/APO-1 (CD95) in yeast and causes cell death (1995) Cell, 81, pp. 513-523
Hsu, H., Huang, J., Shu, H.B., Baichwal, V., Goeddel, D.V., TNF-dependent recruitment of the protein kinase RIP to the TNF receptor-1 signaling complex (1996) Immunity, 4, pp. 387-396
Meylan, E., Burns, K., Hofmann, K., Blancheteau, V., Martinon, F., Kelliher, M., RIP1 is an essential mediator of Toll-like receptor 3-induced NF-kappa B activation (2004) Nat Immunol, 5, pp. 503-507
Sun, L., Wang, H., Wang, Z., He, S., Chen, S., Liao, D., Mixed lineage kinase domain-like protein mediates necrosis signaling downstream of RIP3 kinase (2012) Cell, 148, pp. 213-227
Micheau, O., Tschopp, J., Induction of TNF receptor I-mediated apoptosis via two sequential signaling complexes (2003) Cell, 114, pp. 181-190
Liu, X., Shi, F., Li, Y., Yu, X., Peng, S., Li, W., Post-translational modifications as key regulators of TNF-induced necroptosis (2016) Cell Death Dis, 7, p. e2293
Festjens, N., Vanden Berghe, T., Cornelis, S., Vandenabeele, P., RIP1, a kinase on the crossroads of a cell's decision to live or die (2007) Cell Death Differ, 14, pp. 400-410
Liu, X.Y., Lai, F., Yan, X.G., Jiang, C.C., Guo, S.T., Wang, C.Y., RIP1 kinase is an oncogenic driver in melanoma (2015) Cancer Res, 75, pp. 1736-1748
Lalaoui, N., Brumatti, G., Relevance of necroptosis in cancer (2017) Immunol Cell Biol, 95, pp. 137-145
Nebbioso, A., Clarke, N., Voltz, E., Germain, E., Ambrosino, C., Bontempo, P., Tumor-selective action of HDAC inhibitors involves TRAIL induction in acute myeloid leukemia cells (2005) Nat Med, 11, pp. 77-84
Nebbioso, A., Pereira, R., Khanwalkar, H., Matarese, F., Garcia-Rodriguez, J., Miceli, M., Death receptor pathway activation and increase of ROS production by the triple epigenetic inhibitor UVI5008 (2011) Mol Cancer Ther, 10, pp. 2394-2404
Goeman, F., Manni, I., Artuso, S., Ramachandran, B., Toietta, G., Bossi, G., Molecular imaging of nuclear factor-Y transcriptional activity maps proliferation sites in live animals (2012) Mol Biol Cell, 23, pp. 1467-1474
Ciana, P., Raviscioni, M., Mussi, P., Vegeto, E., Que, I., Parker, M.G., In vivo imaging of transcriptionally active estrogen receptors (2003) Nat Med, 9, pp. 82-86
Spano, D., Heck, C., De Antonellis, P., Christofori, G., Zollo, M., Molecular networks that regulate cancer metastasis (2012) Sem Cancer Biol, 22, pp. 234-249
Wapenaar, H., Dekker, F.J., Histone acetyltransferases: Challenges in targeting bi-substrate enzymes (2016) Clin Epigenet, 8, p. 59
Christofferson, D.E., Yuan, J., Necroptosis as an alternative form of programmed cell death (2010) Curr Opin Cell Biol, 22, pp. 263-268
Cho, Y.S., Challa, S., Moquin, D., Genga, R., Ray, T.D., Guildford, M., Phosphorylation-driven assembly of the RIP1-RIP3 complex regulates programmed necrosis and virus-induced inflammation (2009) Cell, 137, pp. 1112-1123
Narayan, N., Lee, I.H., Borenstein, R., Sun, J., Wong, R., Tong, G., The NAD-dependent deacetylase SIRT2 is required for programmed necrosis (2012) Nature, 492, pp. 199-204
Wegner, K.W., Saleh, D., Degterev, A., Complex pathologic roles of RIPK1 and RIPK3: Moving beyond necroptosis (2017) Trends Pharmacol Sci, 38, pp. 202-225
Outeiro, T.F., Kontopoulos, E., Altmann, S.M., Kufareva, I., Strathearn, K.E., Amore, A.M., Sirtuin 2 inhibitors rescue alpha-synuclein-mediated toxicity in models of Parkinson's disease (2007) Science, 317, pp. 516-519
Trapp, J., Meier, R., Hongwiset, D., Kassack, M.U., Sippl, W., Jung, M., Structure-activity studies on suramin analogues as inhibitors of NAD+-dependent histone deacetylases (sirtuins) (2007) ChemMedChem, 2, pp. 1419-1431
Napper, A.D., Hixon, J., McDonagh, T., Keavey, K., Pons, J.F., Barker, J., Discovery of indoles as potent and selective inhibitors of the deacetylase SIRT1 (2005) J Med Chem, 48, pp. 8045-8054
Jafari, R., Almqvist, H., Axelsson, H., Ignatushchenko, M., Lundback, T., Nordlund, P., The cellular thermal shift assay for evaluating drug target interactions in cells (2014) Nat Protoc, 9, pp. 2100-2122
Linkermann, A., Green, D.R., Necroptosis (2014) N Engl J Med, 370, pp. 455-465
Sun, S.Y., N-acetylcysteine, reactive oxygen species and beyond (2010) Cancer Biol Ther, 9, pp. 109-110
Newton, K., Dugger, D.L., Wickliffe, K.E., Kapoor, N., de Almagro, M.C., Vucic, D., Activity of protein kinase RIPK3 determines whether cells die by necroptosis or apoptosis (2014) Science, 343, pp. 1357-1360
Degterev, A., Hitomi, J., Germscheid, M., Ch'en, I.L., Korkina, O., Teng, X., Identification of RIP1 kinase as a specific cellular target of necrostatins (2008) Nat Chem Biol, 4, pp. 313-321
Bertrand, M.J., Milutinovic, S., Dickson, K.M., Ho, W.C., Boudreault, A., Durkin, J., CIAP1 and cIAP2 facilitate cancer cell survival by functioning as E3 ligases that promote RIP1 ubiquitination (2008) Mol Cell, 30, pp. 689-700
Biton, S., Ashkenazi, A., NEMO and RIP1 control cell fate in response to extensive DNA damage via TNF-alpha feedforward signaling (2011) Cell, 145, pp. 92-103
O'Donnell, M.A., Legarda-Addison, D., Skountzos, P., Yeh, W.C., Ting, A.T., Ubiquitination of RIP1 regulates an NF-kappaB-independent cell-death switch in TNF signaling (2007) Curr Biol, 17, pp. 418-424
O'Donnell, M.A., Hase, H., Legarda, D., Ting, A.T., NEMO inhibits programmed necrosis in an NFkappaB-independent manner by restraining RIP1 (2012) PLoS One, 7
Parthun, M.R., Histone acetyltransferase 1: More than just an enzyme? (2013) Biochim Biophys Acta, 1819, pp. 256-263
Mellini, P., Valente, S., Mai, A., Sirtuin modulators: An updated patent review (2012 - 2014) (2015) Expert Opin Ther Pat, 25, pp. 5-15
Insinga, A., Monestiroli, S., Ronzoni, S., Gelmetti, V., Marchesi, F., Viale, A., Inhibitors of histone deacetylases induce tumor-selective apoptosis through activation of the death receptor pathway (2005) Nat Med, 11, pp. 71-76
Kim, H.B., Kim, M.J., Lee, S.H., Lee, J.W., Bae, J.H., Kim, D.W., Amurensin G, a novel SIRT1 inhibitor, sensitizes TRAIL-resistant human leukemic K562 cells to TRAIL-induced apoptosis (2012) Biochem Pharmacol, 84, pp. 402-410
Lee, M.W., Park, S.C., Kim, J.H., Kim, I.K., Han, K.S., Kim, K.Y., The involvement of oxidative stress in tumor necrosis factor (TNF)-related apoptosis-inducing ligand (TRAIL)-induced apoptosis in HeLa cells (2002) Cancer Lett, 182, pp. 75-82
Parthun, M.R., Hat1: The emerging cellular roles of a type B histone acetyltransferase (2007) Oncogene, 26, pp. 5319-5328
Motta, M.C., Divecha, N., Lemieux, M., Kamel, C., Chen, D., Gu, W., Mammalian SIRT1 represses forkhead transcription factors (2004) Cell, 116, pp. 551-563
Brunet, A., Sweeney, L.B., Sturgill, J.F., Chua, K.F., Greer, P.L., Lin, Y., Stress-dependent regulation of FOXO transcription factors by the SIRT1 deacetylase (2004) Science, 303, pp. 2011-2015
van der Horst, A., Tertoolen, L.G., de Vries-Smits, L.M., Frye, R.A., Medema, R.H., Burgering, B.M., FOXO4 is acetylated upon peroxide stress and deacetylated by the longevity protein hSir2(SIRT1) (2004) J Biol Chem, 279, pp. 28873-28879
Basit, F., Humphreys, R., Fulda, S., RIP1 protein-dependent assembly of a cytosolic cell death complex is required for inhibitor of apoptosis (IAP) inhibitor-mediated sensitization to lexatumumab-induced apoptosis (2012) J Biol Chem, 287, pp. 38767-38777
Carafa, V., Nebbioso, A., Altucci, L., Sirtuins and disease: The road ahead (2012) Front Pharmacol, 3, p. 4
Carafa, V., Rotili, D., Forgione, M., Cuomo, F., Serretiello, E., Hailu, G.S., Sirtuin functions and modulation: From chemistry to the clinic (2016) Clin Epigenetics, 8, p. 61
Clin Cancer Res (ISSN: 1078-0432print, 1078-0432linking), 2018 Jun 15; 24(12): 2886-2900.
Export to BibTeX Export to EndNote
Paper type: Journal Article,
Impact factor: 6.488, 5-year impact factor: 6.646
Url: https://www.scopus.com/inward/record.uri?eid=2-s2.0-85052287980&doi=10.1158%2f1078-0432.CCR-17-3081&partnerID=40&md5=40eb37bac795274af9b9ca4d6a11c13c
Keywords: 12 Dimethylbenz[a]anthracene, Caspase 8, Histone Acetyltransferase, Hydrolase Inhibitor, Mc 2494, Phosphotransferase, Rip1 Kinase, Rip3 Kinase, Sirtuin 1, Unclassified Drug, Animal Experiment, Animal Model, Apoptosis, Article, Breast Cancer, Cancer Model, Cancer Prevention, Cancer Therapy, Cell Death, Complex Formation, Controlled Study, Enzymatic Assay, Ex Vivo Study, Female, Flow Cytometry, Genetic Transfection, Human, Human Cell, Immunoprecipitation, In Vitro Study, In Vivo Study, Infant, Malignant Neoplasm, Mass Spectrometry, Mouse, Mouse Model, Mutagenesis, Nonhuman, Priority Journal, Protein Acetylation, Protein Protein Interaction, Transcriptomics, Tumor Xenograft,
Affiliations:
*** IBB - CNR ***
Dipartimento di Medicina di Precisione, Universita degli Studi della Campania "Luigi Vanvitelli", Napoli, Italy., Dipartimento di Chimica e Tecnologie del Farmaco, "Sapienza" Universita di Roma, Roma, Italy., Dipartimento di Scienze e Tecnologie Ambientali Biologiche e Farmaceutiche, Universita della Campania Luigi Vanvitelli, Caserta, Italy., Biopulse s.r.l., Napoli, Italy., SAFU Department, Regina Elena Cancer Institute, Rome, Italy., Istituto di Biostrutture e Bioimmagini, CNR, and CIRPeB, Napoli, Italy., Center of Excellence on Neurodegenerative Diseases and Department of Pharmacological Sciences, Universita di Milano, Milano, Italy., Department of Molecular Biology, Radboud University, Nijmegen, the Netherlands., Mouse and Animal Pathology Lab, Fondazione Filarete, Milano, Italy., Department of Pathobiology, School of Veterinary Medicine, University of Pennsylvania, Philadelphia, Pennsylvania., CEINGE, Naples, Italy., Dipartimento di Biochimica e Biotecnologie Mediche, Universita Federico II, Napoli, Italy., Pasteur-Fondazione Cenci Bolognetti, Sapienza Universita di Roma, Roma, Italy., Dipartimento di Medicina di Precisione, Universita degli Studi della Campania "Luigi Vanvitelli", Napoli, Italy. lucia.altucci@unicampania.it.,
References:
Galluzzi, L., Kroemer, G., Secondary necrosis: Accidental no more (2017) Trends Cancer, 3, pp. 1-
Galluzzi, L., Bravo-San Pedro, J.M., Vitale, I., Aaronson, S.A., Abrams, J.M., Adam, D., Essential versus accessory aspects of cell death: Recommendations of the NCCD 2015 (2015) Cell Death Differ, 22, pp. 58-73
Galluzzi, L., Baehrecke, E.H., Ballabio, A., Boya, P., Bravo-San Pedro, J.M., Cecconi, F., Molecular definitions of autophagy and related processes (2017) EMBO J, 36, pp. 1811-1836
Galluzzi, L., Kepp, O., Chan, F.K., Kroemer, G., Necroptosis: Mechanisms and relevance to disease (2017) Annu Rev Pathol, 12, pp. 103-130
Vandenabeele, P., Galluzzi, L., Vanden Berghe, T., Kroemer, G., Molecular mechanisms of necroptosis: An ordered cellular explosion (2010) Nat Rev Mol Cell Biol, 11, pp. 700-714
Jouan-Lanhouet, S., Riquet, F., Duprez, L., Vanden Berghe, T., Takahashi, N., Vandenabeele, P., Necroptosis, in vivo detection in experimental disease models (2014) Semin Cell Dev Biol, 35, pp. 2-13
Stanger, B.Z., Leder, P., Lee, T.H., Kim, E., Seed, B., RIP: A novel protein containing a death domain that interacts with Fas/APO-1 (CD95) in yeast and causes cell death (1995) Cell, 81, pp. 513-523
Hsu, H., Huang, J., Shu, H.B., Baichwal, V., Goeddel, D.V., TNF-dependent recruitment of the protein kinase RIP to the TNF receptor-1 signaling complex (1996) Immunity, 4, pp. 387-396
Meylan, E., Burns, K., Hofmann, K., Blancheteau, V., Martinon, F., Kelliher, M., RIP1 is an essential mediator of Toll-like receptor 3-induced NF-kappa B activation (2004) Nat Immunol, 5, pp. 503-507
Sun, L., Wang, H., Wang, Z., He, S., Chen, S., Liao, D., Mixed lineage kinase domain-like protein mediates necrosis signaling downstream of RIP3 kinase (2012) Cell, 148, pp. 213-227
Micheau, O., Tschopp, J., Induction of TNF receptor I-mediated apoptosis via two sequential signaling complexes (2003) Cell, 114, pp. 181-190
Liu, X., Shi, F., Li, Y., Yu, X., Peng, S., Li, W., Post-translational modifications as key regulators of TNF-induced necroptosis (2016) Cell Death Dis, 7, p. e2293
Festjens, N., Vanden Berghe, T., Cornelis, S., Vandenabeele, P., RIP1, a kinase on the crossroads of a cell's decision to live or die (2007) Cell Death Differ, 14, pp. 400-410
Liu, X.Y., Lai, F., Yan, X.G., Jiang, C.C., Guo, S.T., Wang, C.Y., RIP1 kinase is an oncogenic driver in melanoma (2015) Cancer Res, 75, pp. 1736-1748
Lalaoui, N., Brumatti, G., Relevance of necroptosis in cancer (2017) Immunol Cell Biol, 95, pp. 137-145
Nebbioso, A., Clarke, N., Voltz, E., Germain, E., Ambrosino, C., Bontempo, P., Tumor-selective action of HDAC inhibitors involves TRAIL induction in acute myeloid leukemia cells (2005) Nat Med, 11, pp. 77-84
Nebbioso, A., Pereira, R., Khanwalkar, H., Matarese, F., Garcia-Rodriguez, J., Miceli, M., Death receptor pathway activation and increase of ROS production by the triple epigenetic inhibitor UVI5008 (2011) Mol Cancer Ther, 10, pp. 2394-2404
Goeman, F., Manni, I., Artuso, S., Ramachandran, B., Toietta, G., Bossi, G., Molecular imaging of nuclear factor-Y transcriptional activity maps proliferation sites in live animals (2012) Mol Biol Cell, 23, pp. 1467-1474
Ciana, P., Raviscioni, M., Mussi, P., Vegeto, E., Que, I., Parker, M.G., In vivo imaging of transcriptionally active estrogen receptors (2003) Nat Med, 9, pp. 82-86
Spano, D., Heck, C., De Antonellis, P., Christofori, G., Zollo, M., Molecular networks that regulate cancer metastasis (2012) Sem Cancer Biol, 22, pp. 234-249
Wapenaar, H., Dekker, F.J., Histone acetyltransferases: Challenges in targeting bi-substrate enzymes (2016) Clin Epigenet, 8, p. 59
Christofferson, D.E., Yuan, J., Necroptosis as an alternative form of programmed cell death (2010) Curr Opin Cell Biol, 22, pp. 263-268
Cho, Y.S., Challa, S., Moquin, D., Genga, R., Ray, T.D., Guildford, M., Phosphorylation-driven assembly of the RIP1-RIP3 complex regulates programmed necrosis and virus-induced inflammation (2009) Cell, 137, pp. 1112-1123
Narayan, N., Lee, I.H., Borenstein, R., Sun, J., Wong, R., Tong, G., The NAD-dependent deacetylase SIRT2 is required for programmed necrosis (2012) Nature, 492, pp. 199-204
Wegner, K.W., Saleh, D., Degterev, A., Complex pathologic roles of RIPK1 and RIPK3: Moving beyond necroptosis (2017) Trends Pharmacol Sci, 38, pp. 202-225
Outeiro, T.F., Kontopoulos, E., Altmann, S.M., Kufareva, I., Strathearn, K.E., Amore, A.M., Sirtuin 2 inhibitors rescue alpha-synuclein-mediated toxicity in models of Parkinson's disease (2007) Science, 317, pp. 516-519
Trapp, J., Meier, R., Hongwiset, D., Kassack, M.U., Sippl, W., Jung, M., Structure-activity studies on suramin analogues as inhibitors of NAD+-dependent histone deacetylases (sirtuins) (2007) ChemMedChem, 2, pp. 1419-1431
Napper, A.D., Hixon, J., McDonagh, T., Keavey, K., Pons, J.F., Barker, J., Discovery of indoles as potent and selective inhibitors of the deacetylase SIRT1 (2005) J Med Chem, 48, pp. 8045-8054
Jafari, R., Almqvist, H., Axelsson, H., Ignatushchenko, M., Lundback, T., Nordlund, P., The cellular thermal shift assay for evaluating drug target interactions in cells (2014) Nat Protoc, 9, pp. 2100-2122
Linkermann, A., Green, D.R., Necroptosis (2014) N Engl J Med, 370, pp. 455-465
Sun, S.Y., N-acetylcysteine, reactive oxygen species and beyond (2010) Cancer Biol Ther, 9, pp. 109-110
Newton, K., Dugger, D.L., Wickliffe, K.E., Kapoor, N., de Almagro, M.C., Vucic, D., Activity of protein kinase RIPK3 determines whether cells die by necroptosis or apoptosis (2014) Science, 343, pp. 1357-1360
Degterev, A., Hitomi, J., Germscheid, M., Ch'en, I.L., Korkina, O., Teng, X., Identification of RIP1 kinase as a specific cellular target of necrostatins (2008) Nat Chem Biol, 4, pp. 313-321
Bertrand, M.J., Milutinovic, S., Dickson, K.M., Ho, W.C., Boudreault, A., Durkin, J., CIAP1 and cIAP2 facilitate cancer cell survival by functioning as E3 ligases that promote RIP1 ubiquitination (2008) Mol Cell, 30, pp. 689-700
Biton, S., Ashkenazi, A., NEMO and RIP1 control cell fate in response to extensive DNA damage via TNF-alpha feedforward signaling (2011) Cell, 145, pp. 92-103
O'Donnell, M.A., Legarda-Addison, D., Skountzos, P., Yeh, W.C., Ting, A.T., Ubiquitination of RIP1 regulates an NF-kappaB-independent cell-death switch in TNF signaling (2007) Curr Biol, 17, pp. 418-424
O'Donnell, M.A., Hase, H., Legarda, D., Ting, A.T., NEMO inhibits programmed necrosis in an NFkappaB-independent manner by restraining RIP1 (2012) PLoS One, 7
Parthun, M.R., Histone acetyltransferase 1: More than just an enzyme? (2013) Biochim Biophys Acta, 1819, pp. 256-263
Mellini, P., Valente, S., Mai, A., Sirtuin modulators: An updated patent review (2012 - 2014) (2015) Expert Opin Ther Pat, 25, pp. 5-15
Insinga, A., Monestiroli, S., Ronzoni, S., Gelmetti, V., Marchesi, F., Viale, A., Inhibitors of histone deacetylases induce tumor-selective apoptosis through activation of the death receptor pathway (2005) Nat Med, 11, pp. 71-76
Kim, H.B., Kim, M.J., Lee, S.H., Lee, J.W., Bae, J.H., Kim, D.W., Amurensin G, a novel SIRT1 inhibitor, sensitizes TRAIL-resistant human leukemic K562 cells to TRAIL-induced apoptosis (2012) Biochem Pharmacol, 84, pp. 402-410
Lee, M.W., Park, S.C., Kim, J.H., Kim, I.K., Han, K.S., Kim, K.Y., The involvement of oxidative stress in tumor necrosis factor (TNF)-related apoptosis-inducing ligand (TRAIL)-induced apoptosis in HeLa cells (2002) Cancer Lett, 182, pp. 75-82
Parthun, M.R., Hat1: The emerging cellular roles of a type B histone acetyltransferase (2007) Oncogene, 26, pp. 5319-5328
Motta, M.C., Divecha, N., Lemieux, M., Kamel, C., Chen, D., Gu, W., Mammalian SIRT1 represses forkhead transcription factors (2004) Cell, 116, pp. 551-563
Brunet, A., Sweeney, L.B., Sturgill, J.F., Chua, K.F., Greer, P.L., Lin, Y., Stress-dependent regulation of FOXO transcription factors by the SIRT1 deacetylase (2004) Science, 303, pp. 2011-2015
van der Horst, A., Tertoolen, L.G., de Vries-Smits, L.M., Frye, R.A., Medema, R.H., Burgering, B.M., FOXO4 is acetylated upon peroxide stress and deacetylated by the longevity protein hSir2(SIRT1) (2004) J Biol Chem, 279, pp. 28873-28879
Basit, F., Humphreys, R., Fulda, S., RIP1 protein-dependent assembly of a cytosolic cell death complex is required for inhibitor of apoptosis (IAP) inhibitor-mediated sensitization to lexatumumab-induced apoptosis (2012) J Biol Chem, 287, pp. 38767-38777
Carafa, V., Nebbioso, A., Altucci, L., Sirtuins and disease: The road ahead (2012) Front Pharmacol, 3, p. 4
Carafa, V., Rotili, D., Forgione, M., Cuomo, F., Serretiello, E., Hailu, G.S., Sirtuin functions and modulation: From chemistry to the clinic (2016) Clin Epigenetics, 8, p. 61
RIP1-HAT1-SIRT Complex Identification and Targeting in Treatment and Prevention of Cancer
Purpose: Alteration in cell death is a hallmark of cancer. A functional role regulating survival, apoptosis, and necroptosis has been attributed to RIP1/3 complexes. Experimental Design: We have investigated the role of RIP1 and the effects of MC2494 in cell death induction, using different methods as flow cytometry, transcriptome analysis, immunoprecipitation, enzymatic assays, transfections, mutagenesis, and in vivo studies with different mice models. Results: Here, we show that RIP1 is highly expressed in cancer, and we define a novel RIP1/3–SIRT1/2–HAT1/4 complex. Mass spectrometry identified five acetylations in the kinase and death domain of RIP1. The novel characterized pan-SIRT inhibitor, MC2494, increases RIP1 acetylation at two additional sites in the death domain. Mutagenesis of the acetylated lysine decreases RIP1-dependent cell death, suggesting a role for acetylation of the RIP1 complex in cell death modulation. Accordingly, MC2494 displays tumor-selective potential in vitro, in leukemic blasts ex vivo, and in vivo in both xenograft and allograft cancer models. Mechanistically, MC2494 induces bona fide tumor-restricted acetylated RIP1/caspase-8–mediated apoptosis. Excitingly, MC2494 displays tumor-preventive activity by blocking 7,12-dimethylbenz(α)anthracene–induced mammary gland hyperproliferation in vivo. Conclusions: These preventive features might prove useful in patients who may benefit from a recurrence-preventive approach with low toxicity during follow-up phases and in cases of established cancer predisposition. Thus, targeting the newly identified RIP1 complex may represent an attractive novel paradigm in cancer treatment and prevention. ©2018 American Association for Cancer Research.
Purpose: Alteration in cell death is a hallmark of cancer. A functional role regulating survival, apoptosis, and necroptosis has been attributed to RIP1/3 complexes. Experimental Design: We have investigated the role of RIP1 and the effects of MC2494 in cell death induction, using different methods as flow cytometry, transcriptome analysis, immunoprecipitation, enzymatic assays, transfections, mutagenesis, and in vivo studies with different mice models. Results: Here, we show that RIP1 is highly expressed in cancer, and we define a novel RIP1/3–SIRT1/2–HAT1/4 complex. Mass spectrometry identified five acetylations in the kinase and death domain of RIP1. The novel characterized pan-SIRT inhibitor, MC2494, increases RIP1 acetylation at two additional sites in the death domain. Mutagenesis of the acetylated lysine decreases RIP1-dependent cell death, suggesting a role for acetylation of the RIP1 complex in cell death modulation. Accordingly, MC2494 displays tumor-selective potential in vitro, in leukemic blasts ex vivo, and in vivo in both xenograft and allograft cancer models. Mechanistically, MC2494 induces bona fide tumor-restricted acetylated RIP1/caspase-8–mediated apoptosis. Excitingly, MC2494 displays tumor-preventive activity by blocking 7,12-dimethylbenz(α)anthracene–induced mammary gland hyperproliferation in vivo. Conclusions: These preventive features might prove useful in patients who may benefit from a recurrence-preventive approach with low toxicity during follow-up phases and in cases of established cancer predisposition. Thus, targeting the newly identified RIP1 complex may represent an attractive novel paradigm in cancer treatment and prevention. ©2018 American Association for Cancer Research.
RIP1-HAT1-SIRT Complex Identification and Targeting in Treatment and Prevention of Cancer
No results. |
RIP1-HAT1-SIRT Complex Identification and Targeting in Treatment and Prevention of Cancer
Other filter: ([btitle,keywords] "12 Dimethylbenz[a]an ...
Deplano A, Morgillo CM, Demurtas M, Bjorklund E, Cipriano M, Svensson M, Hashemian S, Smaldone G, Pedone E, Luque FJ, Cabiddu MG, Novellino E, Fowler CJ, Catalanotti B, Onnis V
* Novel propanamides as fatty acid amide hydrolase inhibitors (326 views)
Eur J Med Chem (ISSN: 0223-5234, 1768-3254, 0223-5234linking), 2017 Aug 18; 136: 523-542.
Impact Factor: 4.816
View Export to BibTeX Export to EndNote
Milardi D, Pappalardo M
* Molecular dynamics: New advances in drug discovery (433 views)
Eur J Med Chem (ISSN: 0223-5234, 1768-3254, 0223-5234linking), 2015; 91: 1-3.
Impact Factor: 3.902
View Export to BibTeX Export to EndNote
Dynkevich Y, Rother KI, Whitford I, Qureshi S, Galiveeti S, Szulc AL, Danoff A, Breen TL, Kaviani N, Shanik MH, LeRoith D, Vigneri R, Koch CA, Roth J
* Tumors, IGF-2, and Hypoglycemia: Insights From the Clinic, the Laboratory, and the Historical Archive (2014 views)
Endocrine Reviews (ISSN: 0163-769x), 2013 Dec; 34(6): 798-826.
Impact Factor: 19.358
View Export to BibTeX Export to EndNote
Rosa R, Marciano R, Malapelle U, Formisano L, Nappi L, D'Amato C, D'Amato V, Damiano V, Marf G, Del Vecchio S, Zannetti A, Greco A, De Stefano A, Carlomagno C, Veneziani BM, Troncone G, De Placido S, Bianco R
* Sphingosine Kinase 1 Overexpression Contributes to Cetuximab Resistance in Human Colorectal Cancer Models (673 views)
Clin Cancer Res (ISSN: 1078-0432, 1078-0432linking, 1078-0432print), 2013 Jan 1; 19(1): 138-147.
Impact Factor: 8.193
View Export to BibTeX Export to EndNote
Milite C, Castellano S, Benedetti R, Tosco A, Ciliberti C, Vicidomini C, Boully L, Franci G, Altucci L, Mai A, Sbardella G
* Modulation of the activity of histone acetyltransferases by long chain alkylidenemalonates (LoCAMs) (362 views)
Bioorg Med Chem (ISSN: 0968-0896, 1464-3391, 1464-3391electronic), 2011 Jun 15; 19(12): 3690-3701.
Impact Factor: 2.921
View Export to BibTeX Export to EndNote
Marasco D, Perretta G, Sabatella M, Ruvo M
* Past and Future Perspectives of Synthetic Peptide Libraries (562 views)
Curr Protein Pept Sci (ISSN: 1389-2037, 1389-2037linking), 2008 Oct; 9(5): 447-467.
Impact Factor: 3.011
View Export to BibTeX Export to EndNote
Sbardella G, Castellano S, Vicidomini C, Rotili D, Nebbioso A, Miceli M, Altucci L, Mai A
* Identification of long chain alkylidenemalonates as novel small molecule modulators of histone acetyltransferases (313 views)
Bioorganic & Medicinal Chemistry Letters (ISSN: 0960-894x), 2008 May 1; 18(9): 2788-2792.
Impact Factor: 2.531
View Export to BibTeX Export to EndNote
Mai A, Rotili D, Tarantino D, Ornaghi P, Tosi F, Vicidomini C, Sbardella G, Nebbioso A, Miceli M, Altucci L, Filetici P
* Small-molecule inhibitors of histone acetyltransferase activity: Identification and biological properties (604 views)
J Med Chem (ISSN: 0022-2623, 1520-4804, 0022-2623print), 2006 Nov 16; 49(23): 6897-6907.
Impact Factor: 5.115
View Export to BibTeX Export to EndNote
Mai A, Rotili D, Ornaghi P, Tosi F, Vicidomini C, Sardella G, Nebbioso A, Altucci L, Filatici P
* Identification of small molecules inhibitors of GCN5 histone acetyltransferase activity (280 views)
Arkivoc (ISSN: 1424-6376), 2006; 6(VIII): 24-37.
Impact Factor: 0.8
View Export to BibTeX Export to EndNote
* Novel propanamides as fatty acid amide hydrolase inhibitors (326 views)
Eur J Med Chem (ISSN: 0223-5234, 1768-3254, 0223-5234linking), 2017 Aug 18; 136: 523-542.
Impact Factor: 4.816
View Export to BibTeX Export to EndNote
Milardi D, Pappalardo M
* Molecular dynamics: New advances in drug discovery (433 views)
Eur J Med Chem (ISSN: 0223-5234, 1768-3254, 0223-5234linking), 2015; 91: 1-3.
Impact Factor: 3.902
View Export to BibTeX Export to EndNote
Dynkevich Y, Rother KI, Whitford I, Qureshi S, Galiveeti S, Szulc AL, Danoff A, Breen TL, Kaviani N, Shanik MH, LeRoith D, Vigneri R, Koch CA, Roth J
* Tumors, IGF-2, and Hypoglycemia: Insights From the Clinic, the Laboratory, and the Historical Archive (2014 views)
Endocrine Reviews (ISSN: 0163-769x), 2013 Dec; 34(6): 798-826.
Impact Factor: 19.358
View Export to BibTeX Export to EndNote
Rosa R, Marciano R, Malapelle U, Formisano L, Nappi L, D'Amato C, D'Amato V, Damiano V, Marf G, Del Vecchio S, Zannetti A, Greco A, De Stefano A, Carlomagno C, Veneziani BM, Troncone G, De Placido S, Bianco R
* Sphingosine Kinase 1 Overexpression Contributes to Cetuximab Resistance in Human Colorectal Cancer Models (673 views)
Clin Cancer Res (ISSN: 1078-0432, 1078-0432linking, 1078-0432print), 2013 Jan 1; 19(1): 138-147.
Impact Factor: 8.193
View Export to BibTeX Export to EndNote
Milite C, Castellano S, Benedetti R, Tosco A, Ciliberti C, Vicidomini C, Boully L, Franci G, Altucci L, Mai A, Sbardella G
* Modulation of the activity of histone acetyltransferases by long chain alkylidenemalonates (LoCAMs) (362 views)
Bioorg Med Chem (ISSN: 0968-0896, 1464-3391, 1464-3391electronic), 2011 Jun 15; 19(12): 3690-3701.
Impact Factor: 2.921
View Export to BibTeX Export to EndNote
Marasco D, Perretta G, Sabatella M, Ruvo M
* Past and Future Perspectives of Synthetic Peptide Libraries (562 views)
Curr Protein Pept Sci (ISSN: 1389-2037, 1389-2037linking), 2008 Oct; 9(5): 447-467.
Impact Factor: 3.011
View Export to BibTeX Export to EndNote
Sbardella G, Castellano S, Vicidomini C, Rotili D, Nebbioso A, Miceli M, Altucci L, Mai A
* Identification of long chain alkylidenemalonates as novel small molecule modulators of histone acetyltransferases (313 views)
Bioorganic & Medicinal Chemistry Letters (ISSN: 0960-894x), 2008 May 1; 18(9): 2788-2792.
Impact Factor: 2.531
View Export to BibTeX Export to EndNote
Mai A, Rotili D, Tarantino D, Ornaghi P, Tosi F, Vicidomini C, Sbardella G, Nebbioso A, Miceli M, Altucci L, Filetici P
* Small-molecule inhibitors of histone acetyltransferase activity: Identification and biological properties (604 views)
J Med Chem (ISSN: 0022-2623, 1520-4804, 0022-2623print), 2006 Nov 16; 49(23): 6897-6907.
Impact Factor: 5.115
View Export to BibTeX Export to EndNote
Mai A, Rotili D, Ornaghi P, Tosi F, Vicidomini C, Sardella G, Nebbioso A, Altucci L, Filatici P
* Identification of small molecules inhibitors of GCN5 histone acetyltransferase activity (280 views)
Arkivoc (ISSN: 1424-6376), 2006; 6(VIII): 24-37.
Impact Factor: 0.8
View Export to BibTeX Export to EndNote
9 Records (9 excluding Abstracts).
Total impact factor: 50.647 (50.647 excluding Abstracts).
Total 5 year impact factor: 56.584 (56.584 excluding Abstracts).
Total impact factor: 50.647 (50.647 excluding Abstracts).
Total 5 year impact factor: 56.584 (56.584 excluding Abstracts).
245 views. Last view on Monday 24 April 2023, 14:20:57
ibb.cnr.it
