Bimoclomol, a heat shock protein co-inducer, acts by the prolonged activation of heat shock factor-1

Biochemical and Biophysical Research Communications

Volumn 307, Issue 3, 2003, Pages 689-695

  Hargitai, Judit ^a   Lewis, Hannah ^b   Boros, Imre ^c   Rácz, Tímea ^a   Fiser, András ^d   Kurucz, István ^a,g   Benjamin, Ivor ^e   Vígh, László ^c   Pénzes, Zoltán ^a   Csermely, Péter ^a,f   Latchman, David S ^b  

^a POB 348 H 8201   (Hungary)

^b UNIVERSITY COLLEGE LONDON   (United Kingdom)

^c INSTITUTE OF EXPERIMENTAL MEDICINE   (Hungary)

^d ROCKEFELLER UNIVERSITY   (United States)

^e UNIVERSITY OF TEXAS SOUTHWESTERN MEDICAL CENTER   (United States)

^f SEMMELWEIS UNIVERSITY   (Hungary)

^g Institute for Drug Research Budapest   (Hungary)

Author keywords

Bimoclomol; Chaperones; HSF 1; Hsp47; Hsp70; Hsp90

Indexed keywords

BIMOCLOMOL; HEAT SHOCK PROTEIN; HYDROXYLAMINE; UNCLASSIFIED DRUG;

ANIMAL CELL; ARTICLE; CELL PROTECTION; CONTROLLED STUDY; DNA BINDING; ENZYME ACTIVATION; MOUSE; NONHUMAN; PRIORITY JOURNAL; PROTEIN EXPRESSION; STRESS;

EID: 0042170384     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-291X(03)01254-3     Document Type: Article

References (24)

1. Morimoto R.I. Regulation of the heat shock transcriptional response: cross talk between a family of heat shock factors, molecular chaperones, and negative regulators. Genes Dev. 12:1998;3788-3796.
2. Biro K., Palhalmi J., Toth A.J., Kukorelli T., Juhasz G. Bimoclomol improves early electrophysiological signs of retinopathy in diabetic rats. Neuroreport. 9:1998;2029-2033.
3. Biro K., Jednakovits A., Kukorelli T., Hegedus E., Koranyi L. Bimoclomol (BRLP-42) ameliorates peripheral neuropathy in streptozotocin-induced diabetic rats. Brain Res. Bull. 44:1997;259-263.
4. Polakowski J.S., Wegner C.D., Cox B.F. Bimoclomol elevates heat shock protein 70 and cytoprotects rat neonatal cardiomyocytes. Eur. J. Pharmacol. 435:2002;73-77.
5. Lubbers N.L., Polakowski J.S., Wegner C.D., Burke S.E., Diaz G.J., Daniell K., Cox B.F. Oral bimoclomol elevates heat shock protein 70 and reduces myocardial infarct size in rats. Eur. J. Pharmacol. 435:2002;79-83.
6. Erdo F., Erdo S.L. Bimoclomol protects against vascular consequences of experimental subarachnoid hemorrhage in rats. Brain Res. Bull. 45:1998;163-166.
7. Vigh L., Literati P.N., Horvath I., Torok Z., Balogh G., Glatz A., Kovacs E., Boros I., Ferdinandy P., Farkas B., Jaszlits L., Jednakovits A., Koranyi L., Maresca B. Bimoclomol: a nontoxic, hydroxylamine derivative with stress protein-inducing activity and cytoprotective effects. Nat. Med. 3:1997;1150-1154.
8. Yenari M.A., Fink S.L., Sun G.H., Chang L.K., Patel M.K., Kunis D.M., Onley D., Ho D.Y., Sapolsky R.M., Steinberg G.K. Gene therapy with HSP72 is neuroprotective in rat models of stroke and epilepsy. Ann. Neurol. 44:1998;584-591.
9. Suzuki K., Sawa Y., Kaneda Y., Ichikawa H., Shirakura R., Matsuda H. Overexpressed heat shock protein 70 attenuates hypoxic injury in coronary endothelial cells. J. Mol. Cell.Cardiol. 6:1998;1129-1136.
10. Warrick J.M., Chan H.Y., Gray-Board G.L., Chai Y., Paulson H.L., Bonini N.M. Suppression of polyglutamine-mediated neurodegeneration in Drosophila by the molecular chaperone HSP70. Nat. Genet. 23:1999;425-428.
11. McMillan D.R., Xiao X., Shao L., Graves K., Benjamin I.J. Targeted disruption of heat shock transcription factor 1 abolishes thermotolerance and protection against heat-inducible apoptosis. J. Biol. Chem. 273:1998;7523-7528.
12. Xiao X., Zuo X., Davis A.A., McMillan D.R., Curry B.B., Richardson J.A., Benjamin I.J. HSF1 is required for extra-embryonic development, postnatal growth and protection during inflammatory responses in mice. EMBO J. 18:1999;5943-5952.
13. Kurucz I., Tombor B., Prechl J., Erdo F., Hegedus E., Nagy Z., Vitai M., Koranyi L., Laszlo L. Ultrastructural localization of Hsp-72 examined with a new polyclonal antibody raised against the truncated variable domain of the heat shock protein. Cell Stress Chaperon. 4:1999;139-152.
14. Rivory L.P., Pond S.M., Winzor D.J. The influence of pH on the interaction of lipophilic anthracyclines with bovine serum albumin. Quantitative characterization by measurement of fluorescence quenching. Biochem. Pharmacol. 44:1992;2347-2355.
15. Rabindran S., Giorgi G., Clos J., Wu C. Molecular cloning and expression of a human heat shock factor, HSF-1. Proc. Natl. Acad. Sci. USA. 88:1991;6906-6910.
16. Soncin F., Prevelige R., Calderwood S.K. Expression and purification of human heat-shock transcription factor 1. Protein Expr. Purif. 9:1997;27-32.
17. Kadonaga J., Tjian R. Affinity purification of sequence-specific DNA binding proteins. Proc. Natl. Acad. Sci. USA. 83:1986;5889-5893.
18. Manuel M., Rallu M., Loones M.-T., Zimarino V., Mezger V., Morange M. Determination of the consensus binding sequence for the purified embryonic heat shock factor 2. Eur. J. Biochem. 269:2002;2527-2537.
19. Csermely P., Kajtar J., Hollosi M., Jalsovszky G., Holly S., Kahn C.R., Gergely P. Jr., Soti C., Mihaly K., Somogyi J. ATP induces a conformational change of the 90-kDa heat shock protein (hsp90). J. Biol. Chem. 268:1993;1901-1907.
20. Ausubel F.M., Brent R., Kingston R.E., Moore D.D., Seidman J.G., Smith J.A., Struhl K. Current Protocols in Molecular Biology. 2001;John Wiley & Sons Inc. USA.
21. Petersen R., Lindquist S. The Drosophila hsp70 message is rapidly degraded at normal temperatures and stabilized by heat shock. Gene. 72:1988;161-168.
22. Johnson A.D., Berberian P.A., Tytell M., Bond M.G. Differential distribution of 70-kDa heat shock protein in atherosclerosis. Its potential role in arterial SMC survival. Atherioscler. Thromb. Vasc. Biol. 15:1995;27-36.
23. Visy J., Fitos I., Mady G., Urge L., Krajcsi P., Simonyi M. Enantioselective plasma protein binding of bimoclomol. Chirality. 14:2002;638-642.
24. Török Z., Tsvetkova N.M., Balogh G., Horváth I., Nagy E., Pénzes Z., Hargitai J., Bensaude O., Csermely P., Crowe J.H., Maresca B., Vígh L. Heat shock protein co-inducers with no effect on protein denaturation specifically modulate the membrane lipid phase. Proc. Natl. Acad. Sci. USA. 100:2003;3131-3136.