Hsp90 is a direct target of the anti-allergic drugs disodium cromoglycate and amlexanox

Biochemical Journal

Volumn 374, Issue 2, 2003, Pages 433-441

  Okada, Miki ^a   Itoh, Hideaki ^b   Hatakeyama, Takashi ^a   Tokumitsu, Hiroshi ^a   Kobayashi, Ryoji ^a  

^a KAGAWA UNIVERSITY   (Japan)

^b AKITA UNIVERSITY   (Japan)

Author keywords

Amlexanox; Anti allergic drug; Chaperone; Citrate synthase; Cohort protein; Disodium cromoglycate; Hsp90; Rhodanese

Indexed keywords

DRUG PRODUCTS; PHYSIOLOGY; PROTEINS;

ANTI-ALLERGIC DRUGS;

BIOCHEMISTRY;

AMLEXANOX; ANTIALLERGIC AGENT; CHAPERONE; CITRATE SYNTHASE; CROMOGLYCATE DISODIUM; CYCLOPHILIN; HEAT SHOCK PROTEIN 90;

AMINO TERMINAL SEQUENCE; ANIMAL TISSUE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CATTLE; COMPLEX FORMATION; CONTROLLED STUDY; DRUG PROTEIN BINDING; DRUG TARGETING; IC 50; NONHUMAN; NUCLEOTIDE SEQUENCE; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; WILD TYPE;

AMINO ACID SEQUENCE; AMINOPYRIDINES; ANIMALS; ANTI-ALLERGIC AGENTS; BINDING SITES; BRAIN CHEMISTRY; CARRIER PROTEINS; CATTLE; CROMOLYN SODIUM; CYCLOPHILINS; HEAT-SHOCK PROTEINS; HSP70 HEAT-SHOCK PROTEINS; HSP90 HEAT-SHOCK PROTEINS; HUMANS; MACROMOLECULAR SUBSTANCES; MOLECULAR SEQUENCE DATA; PEPTIDE FRAGMENTS; PEPTIDYLPROLYL ISOMERASE; PROTEIN BINDING; PROTEIN FOLDING; PROTEIN STRUCTURE, TERTIARY; RATS; RECEPTORS, DRUG; SEQUENCE DELETION; SIGNAL TRANSDUCTION;

ANIMALIA; BOS TAURUS;

EID: 0041328582     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20030351     Document Type: Article

References (36)

1. Lindquist, S. and Craig, E. A. (1988) The heat-shock proteins. Annu. Rev. Genet. 22, 631-677
2. Freeman, B. C. and Morimoto, R. I. (1996) The human cytosolic molecular chaperones hsp90, hsp70 (hsc70) and hdj-1 have distinct roles in recognition of a non-native protein and protein refolding. EMBO J. 15, 2969-2979
3. Morimoto, R. I., Sarge, K. D. and Abravaya, K. (1992) Transcriptional regulation of heat shock genes. A paradigm for inducible genomic responses. J. Biol. Chem. 267, 21987-21990
4. Parsell, D. A. and Lindquist, S. (1994) Heat shock proteins and stress tolerance. In The Biology of Heat Shock Proteins and Molecular Chaperones (Morimoto, R. I., Tissiers, A. and Georgopoulos, D., eds.), pp. 457-495, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
5. Young, J. C., Moarefi, I. and Hartl, F. U. (2001) Hsp90: a specialized but essential protein-folding tool. J. Cell. Biol. 154, 267-273
6. Goebl, M. and Yanagida, M. (1991) The TPR snap helix: a novel protein repeat motif from mitosis to transcription. Trends Biochem. Sci. 16, 173-177
7. Radanyi, C., Chambraud, B. and Baulieu, E. E. (1994) The ability of immunophilin FKBP59-HBI to interact with the 90-kDa heat shock protein is encoded by its tetratricopeptide repeat domain. Proc. Natl. Acad. Sci. U.S.A. 91, 11197-11201
8. Owens-Grillo, J. K., Czar, M. J., Hutchison, K. A., Hoffmann, K., Perdew, G. H. and Pratt, W. B. (1996) A model of protein targeting mediated by immunophilins and other proteins that bind to hsp90 via tetratricopeptide repeat domains. J. Biol. Chem. 271, 13468-13475
9. Ratajczak, T. and Carrello, A. (1996) Cyclophilin 40 (CyP-40), mapping of its hsp90 binding domain and evidence that FKBP52 competes with CyP-40 for hsp90 binding. J. Biol. Chem. 271, 2961-2965
10. Irmer, H. and Hohfeld, J. (1997) Characterization of functional domains of the eukaryotic co-chaperone Hip. J. Biol. Chem. 272, 2230-2235
11. Chen, S. and Smith, D. F. (1998) Hop as an adaptor in the heat shock protein 70 (Hsp70) and hsp90 chaperone machinery. J. Biol. Chem. 273, 35194-35200
12. Hohfeld, J., Minami, Y. and Hartl, F. U. (1995) Hip, a novel co-chaperone involved in the eukaryotic Hsc70/Hsp40 reaction cycle. Cell 83, 589-598
13. Smith, D. F. (1993) Dynamics of heat shock protein 90-progesterone receptor binding and the disactivation loop model for steroid receptor complexes. Mol. Endocrinol. 7, 1418-1429
14. Sullivan, W. P. and Tort, D. O. (1993) Mutational analysis of hsp90 binding to the progesterone receptor. J. Biol. Chem. 268, 20373-20379
15. Pratt, W. B. and Toft, D. O. (1997) Steroid receptor interactions with heat shock protein and immunophilin chaperones. Endocr. Rev. 18, 306-360
16. Stancato, L. F., Chow, Y. H., Hutchison, K. A., Perdew, G. H., Jove, R. and Pratt, W. B. (1993) Raf exists in a native heterocomplex with hsp90 and p50 that can be reconstituted in a cell-free system. J. Biol. Chem. 268, 21711-21716
17. Wartmann, M. and Davis, R. J. (1994) The native structure of the activated Raf protein kinase is a membrane-bound multi-subunit complex. J. Biol. Chem. 269, 6695-6701
18. Young, J. C., Schneider, C. and Hartl, F. U. (1997) In vitro evidence that hsp90 contains two independent chaperone sites. FEBS Lett. 418, 139-143
19. Scheibel, T., Weikl, T. and Buchner, J. (1998) Two chaperone sites in Hsp90 differing in substrate specificity and ATP dependence. Proc. Natl. Acad. Sci. U.S.A. 95, 1495-1499
20. Prodromou, C., Roe, S. M., O'Brien, R., Ladbury, J. E., Piper, P. W. and Pearl, L. H. (1997) Identification and structural characterization of the ATP/ADP-binding site in the Hsp90 molecular chaperone. Cell 90, 65-75
21. Stebbins, C. E., Russo, A. A., Schneider, C., Rosen, N., Hartl, F. U. and Pavletich, N. P. (1997) Crystal structure of an Hsp90-geldanamycin complex: targeting of a protein chaperone by an antitumor agent. Cell 89, 239-250
22. Roe, S. M., Prodromou, C., O'Brien, R., Ladbury, J. E., Piper, P. W. and Pearl, L. H. (1999) Structural basis for inhibition of the Hsp90 molecular chaperone by the antitumor antibiotics radicicol and geldanamycin. J. Med. Chem. 42, 260-266
23. Grenert, J. P., Sullivan, W. P., Fadden, P., Haystead, T. A., Clark, J., Mimnaugh, E., Krutzsch, H., Ochel, H. J., Schulte, T. W., Sausville, E. et al. (1997) The amino-terminal domain of heat shock protein 90 (hsp90) that binds geldanamycin is an ATP/ADP switch domain that regulates hsp90 conformation. J. Biol. Chem. 272, 23843-23850
24. Schulte, T. W., Akinaga, S., Murakata, T., Agatsuma, T., Sugimoto, S., Nakano, H., Lee, Y. S., Simen, B. B., Argon, Y., Felts, S. et al. (1999) Interaction of radicicol with members of the heat shock protein 90 family of molecular chaperones. Mol. Endocrinol. 13, 1435-1448
25. Marcu, M. G., Chadli, A, Bouhouche, I., Catelli, M. and Neckers, L. M. (2000) The heat shock protein 90 antagonist novobiocin interacts with a previously unrecognized ATP-binding domain in the carboxyl terminus of the chaperone. J. Biol. Chem. 275, 37181-37186
26. Marcu, M. G., Schulte, T. W. and Neckers, L. (2000) Novobiocin and related coumarins and depletion of heat shock protein 90-dependent signaling proteins. J. Natl. Cancer Inst. 92, 242-248
27. Oyama, Y., Shishibori, T., Yamashita, K., Naya, T., Nakagiri, S., Maeta, H. and Kobayashi, R. (1997) Two distinct anti-allergic drugs, amlexanox and cromolyn, bind to the same kinds of calcium binding proteins, except calmodulin, in bovine lung extract. Biochem. Biophys. Res. Commun. 240, 341-347
28. Itoh, H., Toyoshima, I., Mizunuma, H., Kobayashi, R. and Tashima, Y. (1990) Three-step purification method and characterization of the bovine brain 90-kDa heat shock protein. Arch. Biochem. Biophys. 282, 290-296
29. Jakob, U., Lilie, H., Meyer, I. and Buchner, J. (1995) Transient interaction of Hsp90 with early unfolding intermediates of citrate synthase. Implications for heat shock in vivo. J. Biol. Chem. 270, 7288-7294
30. Ramsey, A. J., Russell, L. C., Whitt, S. R. and Chinkers, M. (2000) Overlapping sites of tetratricopeptide repeat protein binding and chaperone activity in heat shock protein 90. J. Biol. Chem. 275, 17857-17862
31. Johnson, J. L., Beito, T. G., Krco, C. J. and Toft, D. O. (1994) Characterization of a novel 23-kilodalton protein of unactive progesterone receptor complexes. Mol. Cell. Biol. 14, 1956-1963
32. Scheufler, C., Drinker, A., Bourenkov, G., Pegoraro, S., Moroder, L., Bartunik, H., Hard, F. U. and Moarefi, I. (2000) Structure of TPR domain-peptide complexes: critical elements in the assembly of the Hsp70-Hsp90 multichaperone machine. Cell 101, 199-210
33. Scheibel, T. and Buchner, J. (1998) The Hsp96 complex - a super-chaperone machine as a novel drug target. Biochem. Pharmacol. 56, 675-682
34. Garnier, C., Lafitte, D., Tsvetkov, P. O., Barbier, P., Leclerc-Devin, J., Millot, J. M., Briand, C., Makarov, A. A., Catelli, M. G. and Peyrot, V. (2002) Binding of ATP to heat shock protein 90: evidence for an ATP-binding site in the C-terminal domain. J. Biol. Chem. 277, 12208-12214
35. Young, J. C., Obermann, W. M. and Harl, F. U. (1998) Specific binding of tetratricopeptide repeat proteins to the C-terminal 12-kDa domain of hsp90. J. Biol. Chem. 273, 18007-18010
36. Carrello, A., Ingley, E., Minchin, R. F., Tsai, S. and Ratajczak, T. (1999) The common tetratricopeptide repeat acceptor site for steroid receptor-associated immunophilins and hop is located in the dimerization domain of Hsp90. J. Biol. Chem. 274, 2682-2689