Development of a fluorescence polarization assay for the molecular chaperone Hsp90

Journal of Biomolecular Screening

Volumn 9, Issue 5, 2004, Pages 375-381

  Kim, Joungnam ^a   Felts, Sara ^b   Llauger, Laura ^a   He, Huazhong ^a   Huezo, Henri ^a   Rosen, Neal ^a   Chiosis, Gabriela ^a  

^a MEMORIAL SLOAN KETTERING CANCER CENTER   (United States)

^b MAYO GRADUATE SCHOOL   (United States)

Author keywords

Competitive assay; Fluorescence polarization; High throughput screening; Hsp90

Indexed keywords

4,4 DIFLUORO 1,3,5,7 TETRAMETHYL 4 BORA 3A,4A DIAZA S INDACENE; ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; FLUORESCENT DYE; GELDANAMYCIN; HEAT SHOCK PROTEIN 90; HEAT SHOCK PROTEIN 90 INHIBITOR; NATURAL PRODUCT; PROTEIN INHIBITOR; UNCLASSIFIED DRUG; 4,4 DIFLUORO 4 BORA 3A,4A DIAZA S INDACENE; 4,4-DIFLUORO-4-BORA-3A,4A-DIAZA-S-INDACENE; BENZOQUINONE DERIVATIVE; BORON DERIVATIVE; MACROCYCLIC LACTAM; QUINONE DERIVATIVE;

AMINO TERMINAL SEQUENCE; ARTICLE; BINDING SITE; CONCENTRATION RESPONSE; DRUG IDENTIFICATION; DRUG LABELING; DRUG PROTEIN BINDING; FLUORESCENCE POLARIZATION IMMUNOASSAY; HIGH THROUGHPUT SCREENING; PRIORITY JOURNAL; PROTEIN DETERMINATION; PROTEIN FUNCTION; PROTEIN PURIFICATION; RELIABILITY; SIGNAL NOISE RATIO; FLUORESCENCE POLARIZATION; METABOLISM;

BENZOQUINONES; BORON COMPOUNDS; FLUORESCENCE POLARIZATION; FLUORESCENT DYES; HSP90 HEAT-SHOCK PROTEINS; LACTAMS, MACROCYCLIC; QUINONES;

EID: 16644376293     PISSN: 10870571     EISSN: None     Source Type: Journal    
DOI: 10.1177/1087057104265995     Document Type: Article

References (19)

1. Neckers L: Hsp90 inhibitors as novel cancer chemotherapeutic agents. Trends Mol Med 2002;8:S55-S61.
2. Maloney A, Workman P: HSP90 as a new therapeutic target for cancer therapy: the story unfolds. Expert Opin Biol Ther 2002;2:3-24.
3. Solit DB, Zheng FF, Drobnjak M, Munster PN, Higgins B, Verbel D, et al: 17-allylamino-17-demethoxygeldanamycin induces the degradation of androgen receptor and HER-2/neu and inhibits the growth of prostate cancer xenografts. Clin Cancer Res 2002;8:986-993.
4. Bagatell R, Khan O, Paine-Murrieta G, Taylor CW, Akinaga S, Whitesell L: Destabilization of steroid receptors by heat shock protein 90-binding drugs: a ligand-independent approach to hormonal therapy of breast cancer. Clin Cancer Res 2001;7:2076-2084.
5. Whitesell L, Mimnaugh EG, De Costa B, Myers CE, Neckers LM: Inhibition of heat shock protein HSP90-pp60v-src heteroprotein complex formation by benzoquinone ansamycins: essential role for stress proteins in oncogenic transformation. Proc Natl Acad Sci U S A 1994;91:8324-8328.
6. Xu W, Mimnaugh E, Rosser MF, Nicchitta C, Marcu M, Yarden Y, et al: Sensitivity of mature Erbb2 to geldanamycin is conferred by its kinase domain and is mediated by the chaperone protein Hsp90. J Biol Chem 2001;276:3702-3708.
7. Chiosis G, Lucas B, Shtil A, Huezo H, Rosen N: Development of a purine-scaffold novel class of Hsp90 binders that inhibit the proliferation of cancer cells and induce the degradation of Her2 tyrosine kinase. Bioorg Med Chem 2002;1:3555-3564.
8. Roe SM, Prodromou C, O'Brien R, Ladbury JE, Piper PW, Pearl LH: Structural basis for inhibition of the Hsp90 molecular chaperone by the antitumor antibiotics radicicol and geldanamycin. J Med Chem 1999;42:260-266.
9. Prodromou C, Siligardi G, O'Brien R, Woolfson DN, Regan L, Panaretou B, et al: Regulation of Hsp90 ATPase activity by tetratricopeptide repeat (TPR)-domain co-chaperones. EMBO J 1999;18:754-762.
10. Panaretou C, Prodromou C, Roe SM, O'Brien R, Ladbury JE, Piper PW, et al: ATP binding and hydrolysis are essential to the function of the HSP90 molecular chaperone in vivo. EMBO J 1998;17:4829-4836.
11. Obermann WM, Sondermann H, Russo AA, Pavletich NP, Hartl FU: In vivo function of Hsp90 is dependent on ATP binding and ATP hydrolysis. J Cell Biol 1998;143:901-910.
12. Richter K, Muschler P, Hainzl O, Buchner J: Coordinated ATP hydrolysis by the HSP90 dimer. J Biol Chem 2001;276:33689-33696.
13. Weikl T, Muschler P, Richter K, Veit T, Reinstein J, Buchner J: C-terminal regions of Hsp90 are important for trapping the nucleotide during the ATPase cycle. J Mol Biol 2000;303:583-592.
14. Carreras CW, Schirmer A, Zhong Z, Santi DV: Filter binding assay for the geldanamycin-heat shock protein 90 interaction. Anal Biochem 2003;317:40-46.
15. Llauger-Bufi L, Felts SJ, Huezo H, Rosen N, Chiosis G: Synthesis of novel fluorescent probes for the molecular chaperone Hsp90. Bioorg Med Chem Lett 2003;13:3975-3978.
16. Zhang J-H, Chung TDY, Oldenburg KR: A simple statistical parameter for use in evaluation and validation of high throughput screening assays. J Biomol Screen 1999;4:67-73.
17. Lobel LI, Morseman JP, Zeng X, Lustbader JW, Chen H, Allnutt FCT: Development of a fluorescence based high throughput assay for antagonists of the human chorionic gonadotropin receptor extracellular domain: analysis of peptide inhibitors. J Biomol Screen 2001;6:151-158.
18. Lakowitz JR: Fluorescence anisotropyh. In Lakowitz JR (ed): Principles of Fluorescence Spectroscopy. 2nd ed. New York: Plenum, 1999:291-319.
19. Turek-Etienne TC, Small EC, Soh SC, Xin TA, Gaitonde PV, Barrabee EB, et al: Evaluation of fluorescent compound interference in 4 fluorescence polarization assays: 2 kinases, 1 protease, and 1 phosphatase. J Biomol Screen 2003;8:176-184.