Necrostatin-1 analogues: Critical issues on the specificity, activity and in vivo use in experimental disease models

Cell Death and Disease

Volumn 3, Issue 11, 2012, Pages

  Takahashi, N ^a   Duprez, L ^a   Grootjans, S ^a   Cauwels, A ^a   Nerinckx, W ^a   Duhadaway, J B ^b   Goossens, V ^a   Roelandt, R ^a   Van Hauwermeiren, F ^a   Libert, C ^a   Declercq, W ^a   Callewaert, N ^a   Prendergast, G C ^b,c,d   Degterev, A ^e   Yuan, J ^f   Vandenabeele, P ^a  

^a GHENT UNIVERSITY   (Belgium)

^b LANKENAU INSTITUTE FOR MEDICAL RESEARCH   (United States)

^c THOMAS JEFFERSON UNIVERSITY   (United States)

^d THOMAS JEFFERSON UNIVERSITY   (United States)

^e TUFTS UNIVERSITY SCHOOL OF MEDICINE   (United States)

^f HARVARD MEDICAL SCHOOL   (United States)

Author keywords

IDO; Necroptosis; Necrostatin; RIPK1; Sepsis; SIRS

Indexed keywords

HYDANTOIN DERIVATIVE; INACTIVE NECROSTATIN 1; INDOLEAMINE 2,3 DIOXYGENASE INHIBITOR; METHYL THIOHYDANTOIN TRYPTOPHAN; NECROSTATIN 1; PROTEIN KINASE; PROTEIN KINASE INHIBITOR; RECEPTOR INTERACTING PROTEIN KINASE 1; STABLE NECROSTATIN 1; TRYPTOPHAN DERIVATIVE; TUMOR NECROSIS FACTOR; UNCLASSIFIED DRUG;

ANIMAL CELL; ANIMAL EXPERIMENT; ARTICLE; CONTROLLED STUDY; DISEASE MODEL; DRUG ACTIVITY; DRUG MEGADOSE; DRUG SPECIFICITY; ENZYME ACTIVITY; IN VITRO STUDY; IN VIVO STUDY; LOW DRUG DOSE; MOLECULAR MODEL; MORTALITY; MOUSE; NECROPTOSIS; NONHUMAN; PRIORITY JOURNAL;

ANIMALS; APOPTOSIS; CELL LINE, TUMOR; DISEASE MODELS, ANIMAL; DRUG THERAPY; ENZYME INHIBITORS; FEMALE; HUMANS; IMIDAZOLES; INDOLEAMINE-PYRROLE 2,3,-DIOXYGENASE; INDOLES; MICE; MICE, INBRED C57BL; MODELS, MOLECULAR; MOLECULAR STRUCTURE; RECEPTOR-INTERACTING PROTEIN SERINE-THREONINE KINASES; SPECIES SPECIFICITY; SYSTEMIC INFLAMMATORY RESPONSE SYNDROME;

MUS;

EID: 84870570760     PISSN: None     EISSN: 20414889     Source Type: Journal    
DOI: 10.1038/cddis.2012.176     Document Type: Article

References (52)

1. Cho YS, Challa S, Moquin D, Genga R, Ray TD, Guildford M et al. Phosphorylation-driven assembly of the RIP1-RIP3 complex regulates programmed necrosis and virus-induced inflammation. Cell 2009; 137: 1112-1123.
2. Declercq W, Vanden Berghe T, Vandenabeele P. RIP kinases at the crossroads of cell death and survival. Cell 2009; 138: 229-232.
3. He S, Wang L, Miao L, Wang T, Du F, Zhao L et al. Receptor interacting protein kinase-3 determines cellular necrotic response to TNF-alpha. Cell 2009; 137: 1100-1111.
4. Vandenabeele P, Galluzzi L, Vanden Berghe T, Kroemer G. Molecular mechanisms of necroptosis: an ordered cellular explosion. Nat Rev Mol Cell Biol 2010; 11: 700-714.
5. Zhang DW, Shao J, Lin J, Zhang N, Lu BJ, Lin SC et al. RIP3, an energy metabolism regulator that switches TNF-induced cell death from apoptosis to necrosis. Science 2009; 325: 332-336.
6. Bertrand MJ, Vandenabeele P. The ripoptosome: death decision in the cytosol. Mol Cell 2011; 43: 323-325.
7. Feoktistova M, Geserick P, Kellert B, Dimitrova DP, Langlais C, Hupe M et al. cIAPs block ripoptosome formation, a RIP1/caspase-8 containing intracellular cell death complex differentially regulated by cFLIP isoforms. Mol Cell 2011; 43: 449-463.
8. Tenev T, Bianchi K, Darding M, Broemer M, Langlais C, Wallberg F et al. The Ripoptosome, a signaling platform that assembles in response to genotoxic stress and loss of IAPs. Mol Cell 2011; 43: 432-448.
9. Degterev A, Huang Z, Boyce M, Li Y, Jagtap P, Mizushima N et al. Chemical inhibitor of nonapoptotic cell death with therapeutic potential for ischemic brain injury. Nat Chem Biol 2005; 1: 112-119.
10. Degterev A, Hitomi J, Germscheid M, Ch'en IL, Korkina O, Teng X et al. Identification of RIP1 kinase as a specific cellular target of necrostatins. Nat Chem Biol 2008; 4: 313-321.
11. Lee TH, Shank J, Cusson N, Kelliher MA. The kinase activity of Rip1 is not required for tumor necrosis factor-alpha-induced IkappaB kinase or p38 MAP kinase activation or for the ubiquitination of Rip1 by Traf2. J Biol Chem 2004; 279: 33185-33191.
12. Oliver AW, Knapp S, Pearl LH. Activation segment exchange: a common mechanism of kinase autophosphorylation? Trends Biochem Sci 2007; 32: 351-356.
13. Kelliher MA, Grimm S, Ishida Y, Kuo F, Stanger BZ, Leder P. The death domain kinase RIP mediates the TNF-induced NF-kappaB signal. Immunity 1998; 8: 297-303.
14. Lee TH, Huang Q, Oikemus S, Shank J, Ventura JJ, Cusson N et al. The death domain kinase RIP1 is essential for tumor necrosis factor alpha signaling to p38 mitogen-activated protein kinase. Mol Cell Biol 2003; 23: 8377-8385.
15. Lim SY, Davidson SM, Mocanu MM, Yellon DM, Smith CC. The cardioprotective effect of necrostatin requires the cyclophilin-D component of the mitochondrial permeability transition pore. Cardiovasc Drugs Ther 2007; 21: 467-469.
16. Northington FJ, Chavez-Valdez R, Graham EM, Razdan S, Gauda EB, Martin LJ. Necrostatin decreases oxidative damage, inflammation, and injury after neonatal HI. J Cereb Blood Flow Metab 2011; 31: 178-189.
17. Smith CC, Davidson SM, Lim SY, Simpkin JC, Hothersall JS, Yellon DM. Necrostatin: a potentially novel cardioprotective agent? Cardiovasc Drugs Ther 2007; 21: 227-233.
18. You Z, Savitz SI, Yang J, Degterev A, Yuan J, Cuny GD et al. Necrostatin-1 reduces histopathology and improves functional outcome after controlled cortical impact in mice. J Cereb Blood Flow Metab 2008; 28: 1564-1573.
19. Trichonas G, Murakami Y, Thanos A, Morizane Y, Kayama M, Debouck CM et al. Receptor interacting protein kinases mediate retinal detachment-induced photoreceptor necrosis and compensate for inhibition of apoptosis. Proc Natl Acad Sci USA 2010; 107: 21695-21700.
20. Linkermann A, Brasen JH, Himmerkus N, Liu S, Huber TB, Kunzendorf U et al. Rip1 (receptor-interacting protein kinase 1) mediates necroptosis and contributes to renal ischemia/reperfusion injury. Kidney Int 2012; 81: 751-761.
21. Duprez L, Takahashi N, Van Hauwermeiren F, Vandendriessche B, Goossens V, Vanden Berghe T et al. RIP kinase-dependent necrosis drives lethal systemic inflammatory response syndrome. Immunity 2011; 35: 908-918.
22. Biton S, Ashkenazi A. NEMO and RIP1 control cell fate in response to extensive DNA damage via TNF-alpha feedforward signaling. Cell 2011; 145: 92-103.
23. Cho Y, McQuade T, Zhang H, Zhang J, Chan FK. RIP1-dependent and independent effects of necrostatin-1 in necrosis and T cell activation. PLoS One 2011; 6: e23209.
24. Christofferson DE, Li Y, Hitomi J, Zhou W, Upperman C, Zhu H et al. A novel role for RIP1 kinase in mediating TNFalpha production. Cell Death Dis 2012; 3: e320.
25. Vanlangenakker N, Vanden Berghe T, Bogaert P, Laukens B, Zobel K, Deshayes K et al. cIAP1 and TAK1 protect cells from TNF-induced necrosis by preventing RIP1/RIP3- dependent reactive oxygen species production. Cell Death Differ 2011; 18: 656-665.
26. Muller AJ, DuHadaway JB, Donover PS, Sutanto-Ward E, Prendergast GC. Inhibition of indoleamine 2,3-dioxygenase, an immunoregulatory target of the cancer suppression gene Bin1, potentiates cancer chemotherapy. Nat Med 2005; 11: 312-319.
27. Soliman H, Mediavilla-Varela M, Antonia S. Indoleamine 2,3-dioxygenase: is it an immune suppressor? Cancer J 2010; 16: 354-359.
28. Thackray SJ, Mowat CG, Chapman SK. Exploring the mechanism of tryptophan 2,3- dioxygenase. Biochem Soc Trans 2008; 36: 1120-1123.
29. Heikenwalder M, Polymenidou M, Junt T, Sigurdson C, Wagner H, Akira S et al. Lymphoid follicle destruction and immunosuppression after repeated CpG oligodeoxynucleotide administration. Nat Med 2004; 10: 187-192.
30. Puccetti P, Grohmann U. IDO and regulatory T cells: a role for reverse signalling and non-canonical NF-kappaB activation. Nat Rev Immunol 2007; 7: 817-823.
31. Zelante T, Fallarino F, Bistoni F, Puccetti P, Romani L. Indoleamine 2,3-dioxygenase in infection: the paradox of an evasive strategy that benefits the host. Microbes Infect 2009; 11: 133-141.
32. Hill M, Tanguy-Royer S, Royer P, Chauveau C, Asghar K, Tesson L et al. IDO expands human CD4+CD25high regulatory T cells by promoting maturation of LPS-treated dendritic cells. Eur J Immunol 2007; 37: 3054-3062.
33. Tattevin P, Monnier D, Tribut O, Dulong J, Bescher N, Mourcin F et al. Enhanced indoleamine 2,3-dioxygenase activity in patients with severe sepsis and septic shock. J Infect Dis 2010; 201: 956-966.
34. Jung ID, Lee MG, Chang JH, Lee JS, Jeong YI, Lee CM et al. Blockade of indoleamine 2,3- dioxygenase protects mice against lipopolysaccharide-induced endotoxin shock. J Immunol 2009; 182: 3146-3154.
35. Wang Y, Liu H, McKenzie G, Witting PK, Stasch JP, Hahn M et al. Kynurenine is an endothelium-derived relaxing factor produced during inflammation. Nat Med 2010; 16: 279-285.
36. Teng X, Degterev A, Jagtap P, Xing X, Choi S, Denu R et al. Structure-activity relationship study of novel necroptosis inhibitors. Bioorg Med Chem Lett 2005; 15: 5039-5044.
37. Shimizu T, Nomiyama S, Hirata F, Hayaishi O. Indoleamine 2,3-dioxygenase. Purification and some properties. J Biol Chem 1978; 253: 4700-4706.
38. Cady SG, Sono M. 1-Methyl-DL-tryptophan, beta-(3-benzofuranyl)-DL-alanine (the oxygen analog of tryptophan), and beta-[3-benzo(b)thienyl]-DL-alanine (the sulfur analog of tryptophan) are competitive inhibitors for indoleamine 2,3-dioxygenase. Arch Biochem Biophys 1991; 291: 326-333.
39. Sugimoto H, Oda S, Otsuki T, Hino T, Yoshida T, Shiro Y. Crystal structure of human indoleamine 2,3-dioxygenase: catalytic mechanism of O2 incorporation by a hemecontaining dioxygenase. Proc Natl Acad Sci USA 2006; 103: 2611-2616.
40. Trott O, Olson AJ. AutoDock vina: improving the speed and accuracy of docking with a new scoring function, efficient optimization, and multithreading. J Comput Chem 2010; 31: 455-461.
41. Tamura Y, Chiba Y, Tanioka T, Shimizu N, Shinozaki S, Yamada M et al. NO donor induces Nec-1-inhibitable, but RIP1-independent, necrotic cell death in pancreatic betacells. FEBS Lett 2011; 585: 3058-3064.
42. Linkermann A, Brasen JH, De Zen F, Weinlich R, Schwendener RA, Green DR et al. Dichotomy between RIP1- and RIP3-mediated necroptosis in tumor necrosis factor-alphainduced shock. Mol Med 2012; 18: 577-586.
43. McNeal SI, LeGolvan MP, Chung CS, Ayala A. The dual functions of receptor interacting protein 1 in fas-induced hepatocyte death during sepsis. Shock 2011; 35: 499-505.
44. Dudley KH, Butler TC, Bius DL. The role of dihydropyrimidinase in the metabolism of some hydantoin and succinimide drugs. Drug Metab Dispos 1974; 2: 103-112.
45. Andersen G. Uracil and beta-alanine degradation in Saccharomyces kluyveri - discovery of a novel catabolic pathway. Ph.D. Technical University of Denmark: Lyngby, Denmark, 2006.
46. Waniek T. Untersuchungen zur Substratspezifität und Enantioselektivität mikrobieller Hydantoinasen. Ph.D. University Stuttgart: Stuttgart, 2000.
47. Vercammen D, Brouckaert G, Denecker G, Van de Craen M, Declercq W, Fiers W et al. Dual signaling of the Fas receptor: initiation of both apoptotic and necrotic cell death pathways. J Exp Med 1998; 188: 919-930.
48. Kumar S, Jaller D, Patel B, LaLonde JM, DuHadaway JB, Malachowski WP et al. Structure based development of phenylimidazole-derived inhibitors of indoleamine 2,3-dioxygenase. J Med Chem 2008; 51: 4968-4977.
49. Littlejohn TK, Takikawa O, Skylas D, Jamie JF, Walker MJ, Truscott RJ. Expression and purification of recombinant human indoleamine 2, 3-dioxygenase. Protein Expr Purif 2000; 19: 22-29.
50. Morris GM, Huey R, Lindstrom W, Sanner MF, Belew RK, Goodsell DS et al. AutoDock4 and AutoDockTools4: automated docking with selective receptor flexibility. J Comput Chem 2009; 30: 2785-2791.
51. Hanwell MD, Curtis DE, Lonie DC, Vandermeersch T, Zurek E, Hutchison GR. Avogadro: an advanced semantic chemical editor, visualization, and analysis platform. J Cheminform 2012; 4: 17.
52. Halgren TA. Merck molecular force field.1. Basis, form, scope, parameterization, and performance of MMFF94. J Comput Chem 1996; 17: 490-519.