A dual-step fluorescence resonance energy transfer-based quenching assay for screening of caspase-3 inhibitors

Analytical Biochemistry

Volumn 375, Issue 1, 2008, Pages 71-81

  Valanne, A ^a   Malmi, P ^a   Appelblom, H ^a   Niemela P ^a   Soukka, T ^a  

^a UNIVERSITY OF TURKU   (Finland)

Author keywords

Caspase 3; Dual step FRET; Nanoparticle; Quenching assay; Time resolved detection

Indexed keywords

CELL DEATH; CHELATION; ENERGY TRANSFER; ENZYME ACTIVITY; ENZYME INHIBITION; EUROPIUM COMPOUNDS; FORSTER RESONANCE ENERGY TRANSFER; NANOPARTICLES;

CASPASE-3; DUAL-STEP FRET; FLUORESCENCE ENERGY TRANSFER; FLUORESCENCE RESONANCE ENERGY TRANSFER; PHARMACEUTICAL INDUSTRY; QUENCHING ASSAYS; TIME RESOLVED MEASUREMENT; TIME-RESOLVED DETECTION;

QUENCHING;

ALEXA FLUOR 680; BENZYLOXYCARBONYLASPARTYLGLUTAMYLVALYLASPARTYL FLUOROMETHYL KETONE; BLACKBERRY QUENCHER 650; CASPASE; CASPASE 3 INHIBITOR; CHELATE; EUROPIUM; NANOPARTICLE; STREPTAVIDIN; UNCLASSIFIED DRUG;

ARTICLE; ASSAY; COST EFFECTIVENESS ANALYSIS; ENZYME INHIBITION; ENZYME SUBSTRATE; FEASIBILITY STUDY; FLUORESCENCE RESONANCE ENERGY TRANSFER; IC 50; IN VITRO STUDY; PRIORITY JOURNAL; PROTEIN DEGRADATION; SCREENING;

ALEXA; RUBUS;

EID: 39749164098     PISSN: 00032697     EISSN: 10960309     Source Type: Journal    
DOI: 10.1016/j.ab.2007.12.032     Document Type: Article

References (50)

1. D.W. Nicholson From bench to clinic with apoptosis-based therapeutic agents Nature 407 2000 810 816
2. N.M. Dean C.F. Bennett Antisense oligonucleotide-based therapeutics for cancer Oncogene 22 2003 9087 9096
3. M. Thome P. Schneider K. Hofmann H. Fickenscher E. Meinl F. Neipel C. Mattmann K. Burns J-L. Bodmer M. Schröter C. Scaffidi P.H. Krammer M.E. Peter J. Tchopp Viral FLICE-inhibitory proteins (FLIPs) prevent apoptosis induced by death receptors Nature 386 1997 517 521
4. D.M. Rasper J.P. Vaillancourt S. Hadano V.M. Houtzager I. Seiden S.L.C. Keen P. Tawa S. Xanthoudakis J. Nasir D. Martindale B.F. Koop E.P. Peterson N.A. Thornberry J. Huang D.P. MacPherson S.C. Black F. Hornung M.J. Lenardo M.R. Hayden S. Roy D.W. Nicholson Cell death attenuation by “Usurpin”, a mammalian DED-caspase homologue that precludes caspase-8 recruitment and activation by the CD-95 (Fas, APO-1) receptor complex Cell. Death Differ. 5 1998 271 288
5. B. Jansen H. Schlagbauer-Wadl B.D. Brown R.N. Bryan A. Van Elsas M. Müller K. Wolff H-G. Eichler H. Pehamberger Bcl-2 antisense therapy chemosensitizes human melanoma in SCID mice Nat. Med. 4 1998 232 234
6. A. Ashkenazi R.C. Pai S. Fong S. Leung D.A. Lawrence S.A. Marsters C. Blackie L. Chang A.E. McMurtrey A. Hebert L. DeForge I.L. Koumenis D. Lewis L. Harris J. Bussiere H. Koeppen Z. Shahrokh R.H. Schwall Safety and antitumor activity of recombinant soluble Apo2 ligand J. Clin. Invest. 104 1999 155 162
7. T.W. Poh S. Huang J.L. Hirpara S. Pervaiz LY303511 amplifies TRAIL-induced apoptosis in tumor cells by enhancing DR5 oligomerization, DISC assembly, and mitochondrial permeabilization Cell. Death Differ. 14 2007 1813 1825
8. M.P. Kline S.V. Rajkumar M.M. Timm T.K. Kimlinger J.L. Haug J.A. Lust P.R. Greipp S. Kumar ABT-737, an inhibitor of Bcl-2 family proteins, is a potent inducer of apoptosis in multiple myeloma cells Leukemia 21 2007 1549 1560
9. D. Wlodkowic J. Skommer J. Pelkonen Brefeldin A triggers apoptosis associated with mitochondrial breach and enhances HA14-1- and anti-Fas-mediated cell killing in follicular lymphoma cells Leuk. Res. 31 2008 1687 1700
10. D. Chauhan M. Velankar M. Brahmandam T. Hideshima K. Podar P. Richardson R. Sclossman I. Ghobrial N. Raje N. Munshi K.C. Anderson A novel Bcl-2/Bcl-X(L)/Bcl-w inhibitor ABT-737 as therapy in multiple myeloma Oncogene 5 2007 2374 2380
11. J. Ross D. Brough R.M. Gibson S.A. Loddick N.J. Rothwell A selective, non-peptide caspase-1 inhibitor, VRT-018858, markedly reduces brain damage induced by transient ischemia in the rat Neuropharmacology 53 2007 638 642
12. M.O. Hengartner The biochemistry of apoptosis Nature 407 2000 770 776
13. N.A. Thornberry Y. Lazebnik Caspases: Enemies within Science 281 1998 1312 1316
14. S-J. Kang S. Wang H. Hara E.P. Peterson S. Namura S. Amin-Hanjani J. Huang A. Srinivasan K.J. Tomaselli N.A. Thornberry M.A. Moskowitz J. Yuan Dual role of caspase-11 in mediating activation of caspase-1 and caspase-3 under pathological conditions J. Cell. Biol. 149 2000 613 622
15. T. O’Brien D. Lee Prospects for caspase inhibitors Mini Rev. Med. Chem. 4 2004 153 165
16. D. Leung G. Abbenante D.P. Fairlie Protease inhibitors: Current status and future prospects J. Med. Chem. 43 2000 305 341
17. K. Moore S. Rees Cell-based versus isolated target screening: How lucky do you feel? J. Biomol. Screen. 6 2001 69 74
18. A.A. Gershkovich V.V. Kholodovych Fluorogenic substrates for proteases based on intramolecular fluorescence energy transfer (IFETS) J. Biochem. Biophys. Methods 33 1996 135 162
19. V. Gurtu S.R. Kain G. Zhang Fluorometric and colorimetric detection of caspase activity associated with apoptosis Anal. Biochem. 251 1997 98 102
20. M.W. Pennington N.A. Thornberry Synthesis of a fluorogenic interleukin-1(converting enzyme substrate based on resonance energy transfer Peptide Res. 7 1994 72 76
21. H. Hug M. Los W. Hirt K.M. Debatin Rhodamine 110-linked amino acids and peptides as substrates to measure caspase activity upon apoptosis induction in intact cells Biochemistry 38 1999 13906 13911
22. J. Liu M. Bhalgat C. Zhang Z. Diwu B. Hoyland D.H. Klaubert Fluorescent molecular probes V: A sensitive caspase-3 substrate for fluorometric assays Bioorg. Med. Chem. Lett. 9 1999 3231 3236
23. J. Jones R. Heim E. Hare J. Stack B.A. Pollok Development and application of a GFP–FRET intracellular caspase assay for drug screening J. Biomol. Screen. 5 2000 307 318
24. J. Karvinen A. Elomaa M-L. Mäkinen H. Hakala V-M. Mukkala J. Peuralahti P. Hurskainen J. Hovinen I. Hemmilä Caspase multiplexing: Simultaneous homogeneous time-resolved quenching assay (TruPoint) for caspases 1, 3, and 6 Anal. Biochem. 325 2004 317 325
25. J. Karvinen V. Laitala M-L. Mäkinen O. Mulari J. Tamminen J. Hermonen P. Hurkainen I. Hemmilä Fluorescence quenching-based assays for hydrolyzing enzymes: Application of time-resolved fluorometry in assays for caspase, helicase, and phosphatase Anal. Chem. 76 2004 1429 1436
26. S.M. Gopalakrishnan J. Karvinen J.L. Kofron D.J. Burns U. Warrior Application of micro arrayed compound screening (μARCS) to identify inhibitors of caspase-3 J. Biomol. Screen. 7 2002 317 323
27. M. Preaudat J. Oulef-Diaf B. Alpha-Bazin G. Mathis T. Mitsugi Y. Aono K. Takahashi H. Takemoto A homogeneous caspase-3 activity assay using HTRF technology J. Biomol. Screen. 7 2002 267 274
28. T.C. O’Riordan J. Hynes D. Yashunski G.V. Ponomarev D.B. Papkovsky Homogeneous assays for cellular proteases employing the platinum(II)-coproporphyrin label and time-resolved phosphorescence Anal. Biochem. 342 2005 111 119
29. H. Härmä T. Soukka T. Lövgren Europium nanoparticles and time-resolved fluorescence for ultrasensitive detection of prostate-specific antigen Clin. Chem. 47 2001 561 568
30. T. Soukka H. Härmä J. Paukkunen T. Lövgren Utilization of kinetically enhanced monovalent binding affinity by immunoassays based on multivalent nanoparticle–antibody bioconjugates Anal. Chem. 73 2001 2254 2260
31. L. Kokko K. Sandberg T. Lövgren T. Soukka Europium(III) chelate-dyed nanoparticles as donors in a homogeneous proximity-based immunoassay for estradiol Anal. Chim. Acta 503 2004 155 162
32. L. Kokko T. Lövgren T. Soukka Europium(III)-chelates embedded in nanoparticles are protected from interfering compounds present in assay media Anal. Chim. Acta 585 2007 17 23
33. P. von Lode J. Rosenberg K. Pettersson H. Takalo A europium chelate for quantitative point-of-care immunoassay using direct surface measurement Anal. Chem. 75 2003 3193 3201
34. R.V. Talanian C. Quinlan S. Trautz M.C. Hackett J.A. Mankovich D. Banach T. Ghayur H.D. Brady W.W. Wong Substrate specificities of caspase family proteases J. Biol. Chem. 272 1997 9677 9682
35. G.T. Hermanson Bioconjugate Techniques 1st ed. 1996 Academic Press San Diego
36. H.R. Stennicke G.S. Salvesen Biochemical characteristics of caspases-3, -6, -7, and -8 J. Biol. Chem. 272 1997 25719 25723
37. L. Kokko N. Johansson T. Lövgren T. Soukka Enzyme inhibitor screening using a homogeneous proximity-based immunoassay for estradiol J. Biomol. Screen. 10 2005 83 89
38. L. Kokko S. Jaakohuhta P. Lindroos T. Soukka Improved homogeneous proximity-based screening assay of potential inhibitors of 17β-hydroxysteroid dehydrogenases Assay Drug Dev. Technol. 4 2006 91 98
39. I. Schechter A. Berger, On the size of the active site in proteases: I. Papain Biochem. Biophys. Res. Commun. 27 1967 157 162
40. N.A. Thornberry H.G. Bull J.R. Calaycay K.T. Chapman A.D. Howard M.J. Kostura D.K. Miller S.M. Molineaux J.R. Weidner J. Aunins K.O. Elliston J.M. Ayala F.J. Casano J. Chin G. J-F. Ding L.A. Egger E.P. Gaffney G. Limjuco O.C. Palyha S.M. Raju A.M. Rolando J.P. Salley T-T. Yamin T.D. Lee J.E. Shively M. MacCross R.A. Mumford J.A. Schmidt M.J. Tocci A novel heterodimeric cysteine protease is required for interleukin-1β processing in monocytes Nature 356 1992 768 774
41. D.P. Cerretti C.J. Kozlosky B. Mosley N. Nelson K. Van Ness T.A. Greenstreet C.J. March S.R. Kronheim T. Druck L.A. Cannizzaro Molecular cloning of the interleukin-1β converting enzyme Science 256 1992 97 100
42. P. Sleath R. Hendrickson S. Kronheim C. March R. Black Substrate specificity of the protease that processes human interleukin-1β J. Biol. Chem. 265 1990 14526 14528
43. A. Howard M. Kostura N.A. Thornberry G. Ding G. Limjuco J. Weidner J. Salley K. Hogquist D. Chaplin R. Mumford J. Schmidt M. Tocci IL-1-converting enzyme requires aspartic acid residues for processing of the IL-1β precursor at two distinct sites and does not cleave 31-kDa IL-1α J. Immunol. 147 1991 2964 2969
44. L. Stryer Fluorescence energy transfer as a spectroscopic ruler Annu. Rev. Biochem. 47 1978 819 846
45. P.R. Selvin Fluorescence resonance energy transfer Methods Enzymol. 246 1995 300 334
46. I. Okun S. Malarchuk E. Dubrovskaya A. Khvat S. Tkachenko V. Kysil D. Kravchenko A. Ivachtchenko Screening for caspase-3 inhibitors: Effect of a reducing agent on identified hit chemotypes J. Biomol. Screen. 11 2006 694 703
47. A. Valanne S. Huopalahti T. Soukka R. Vainionpää T. Lövgren H. Härmä A sensitive adenovirus immunoassay as a model for using nanoparticle label technology in virus diagnostics J. Clin. Virol. 33 2005 217 223
48. A. Valanne S. Huopalahti R. Vainionpää T. Lövgren H. Härmä Rapid and sensitive HBsAg immunoassay based on fluorescent nanoparticle labels and time-resolved detection J. Virol. Methods 129 2005 83 90
49. A-M. Pelkkikangas S. Jaakohuhta T. Lövgren H. Härmä Simple, rapid, and sensitive thyroid-stimulating hormone immunoassay using europium(III) nanoparticle label Clin. Chim. Acta 517 2004 169 176
50. C. Meyer, M. Haase, W. Hoheisel, K. Bohmann, Core/shell nanoparticles suitable for (F)RET-assays, Patent WO 2004/096944 A1 (2004).