Heat shock protein 90 in Alzheimer's disease

BioMed Research International

Volumn 2014, Issue , 2014, Pages

  Ou, Jiang Rong ^a   Tan, Meng Shan ^b   Xie, An Mu ^a   Yu, Jin Tai ^a,b   Tan, Lan ^a,b  

^a QINGDAO UNIVERSITY   (China)

^b OCEAN UNIVERSITY OF CHINA   (China)

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID BETA PROTEIN; CHAPERONE; HEAT SHOCK PROTEIN 90; HEAT SHOCK TRANSCRIPTION FACTOR 1; TAU PROTEIN;

ALZHEIMER DISEASE; HEAT SHOCK RESPONSE; HUMAN; PATHOGENESIS; PROTEIN AGGREGATION; PROTEIN FOLDING; PROTEIN TARGETING; REVIEW; CHEMISTRY; METABOLISM; MOLECULARLY TARGETED THERAPY;

ALZHEIMER DISEASE; HSP90 HEAT-SHOCK PROTEINS; HUMANS; MOLECULAR TARGETED THERAPY;

EID: 84908323870     PISSN: 23146133     EISSN: 23146141     Source Type: Journal    
DOI: 10.1155/2014/796869     Document Type: Review

References (62)

1. Selkoe D. J., Schenk D., Alzheimer's disease: molecular understanding predicts amyloid-based therapeutics. Annual Review of Pharmacology and Toxicology 2003 43 545 584 10.1146/annurev.pharmtox.43.100901.140248 2-s2.0-0001181116
2. Paul S., Mahanta S., Association of heat-shock proteins in various neurodegenerative disorders: is it a master key to open the therapeutic door? Molecular and Cellular Biochemistry 2014 386 1-2 45 61 10.1007/s11010-013-1844-y 2-s2.0-84891547570
3. Johnson J. L., Evolution and function of diverse Hsp90 homologs and cochaperone proteins. Biochimica et Biophysica Acta 2012 1823 3 607 613 10.1016/j.bbamcr.2011.09.020 2-s2.0-84857048585
4. Kakimura J.-I., Kitamura Y., Takata K., Umeki M., Suzuki S., Shibagaki K., Taniguchi T., Nomura Y., Gebicke-Haerter P. J., Smith M. A., Perry G., Shimohama S., Microglial activation and amyloid- β clearance induced by exogenous heat-shock proteins. The FASEB Journal 2002 16 6 601 603 10.1096/fj.01-0530fje 2-s2.0-0036551332
5. Dickey C. A., Kamal A., Lundgren K., Klosak N., Bailey R. M., Dunmore J., Ash P., Shoraka S., Zlatkovic J., Eckman C. B., Patterson C., Dickson D. W., Nahman N. S. Jr., Hutton M., Burrows F., Petrucelli L., The high-affinity HSP90-CHIP complex recognizes and selectively degrades phosphorylated tau client proteins. The Journal of Clinical Investigation 2007 117 3 648 658 10.1172/JCI29715 2-s2.0-33847369469
6. Waza M., Adachi H., Katsuno M., Minamiyama M., Sang C., Tanaka F., Inukai A., Doyu M., Sobue G., 17-AAG, an Hsp90 inhibitor, ameliorates polyglutamine-mediated motor neuron degeneration. Nature Medicine 2005 11 10 1088 1095 10.1038/nm1298 2-s2.0-27144503120
7. Thomas M., Harrell J. M., Morishima Y., Peng H. M., Pratt W. B., Lieberman A. P., Pharmacologic and genetic inhibition of hsp90-dependent trafficking reduces aggregation and promotes degradation of the expanded glutamine androgen receptor without stress protein induction. Human Molecular Genetics 2006 15 11 1876 1883 10.1093/hmg/ddl110 2-s2.0-33744770333
8. Waza M., Adachi H., Katsuno M., Minamiyama M., Tanaka F., Sobue G., Alleviating neurodegeneration by an anticancer agent: an Hsp90 inhibitor (17-AAG). Annals of the New York Academy of Sciences 2006 1086 21 34 10.1196/annals.1377.012 2-s2.0-34447540087
9. Sharp F. R., Massa S. M., Swanson R. A., Heat-shock protein protection. Trends in Neurosciences 1999 22 3 97 99 10.1016/S0166-2236(98)01392-7 2-s2.0-0033104877
10. Xu Z.-S., Li Z.-Y., Chen Y., Chen M., Li L.-C., Ma Y.-Z., Heat shock protein 90 in plants: molecular mechanisms and roles in stress responses. International Journal of Molecular Sciences 2012 13 12 15706 15723 10.3390/ijms131215706 2-s2.0-84871700505
11. Wegele H., Müller L., Buchner J., Hsp70 and Hsp90-a relay team for protein folding. Reviews of physiology, biochemistry and pharmacology 2004 151 1 44 10.1007/s10254-003-0021-1 2-s2.0-4644278673
12. Didenko T., Duarte A. M. S., Karagöz G. E., Rüdiger S. G. D., Hsp90 structure and function studied by NMR spectroscopy. Biochimica et Biophysica Acta 2012 1823 3 636 647 10.1016/j.bbamcr.2011.11.009 2-s2.0-84857048019
13. Li J., Buchner J., Structure, function and regulation of the Hsp90 machinery. Biomedical Journal 2013 36 3 106 117 10.4103/2319-4170.113230 2-s2.0-84881218748
14. Ali M. M. U., Mark Roe S., Vaughan C. K., Meyer P., Panaretou B., Piper P. W., Prodromou C., Pearl L. H., Crystal structure of an Hsp90-nucleotide-p23/Sba1 closed chaperone complex. Nature 2006 440 7087 1013 1017 10.1038/nature04716 2-s2.0-33646176246
15. Prodromou C., Roe S. M., O'Brien R., Ladbury J. E., Piper P. W., Pearl L. H., Identification and structural characterization of the ATP/ADP-binding site in the Hsp90 molecular chaperone. Cell 1997 90 1 65 75 10.1016/S0092-8674(00)80314-1 2-s2.0-0031444238
16. Pearl L. H., Prodromou C., Structure and mechanism of the Hsp90 molecular chaperone machinery. Annual Review of Biochemistry 2006 75 271 294 10.1146/annurev.biochem.75.103004.142738 2-s2.0-33746364784
17. Zhang M., Botër M., Li K., Kadota Y., Panaretou B., Prodromou C., Shirasu K., Pearl L. H., Structural and functional coupling of Hsp90- and Sgt1-centred multi-protein complexes. The EMBO Journal 2008 27 20 2789 2798 10.1038/emboj.2008.190 2-s2.0-54349122449
18. Vaughan C. K., Gohlke U., Sobott F., Good V. M., Ali M. M. U., Prodromou C., Robinson C. V., Saibil H. R., Pearl L. H., Structure of an Hsp90-Cdc37-Cdk4 complex. Molecular Cell 2006 23 5 697 707 10.1016/j.molcel.2006.07.016 2-s2.0-33747878717
19. Park S. J., Borin B. N., Martinez-Yamout M. A., Dyson H. J., The client protein p53 adopts a molten globule-like state in the presence of Hsp90. Nature Structural and Molecular Biology 2011 18 5 537 541 10.1038/nsmb.2045 2-s2.0-79955642720
20. Hessling M., Richter K., Buchner J., Dissection of the ATP-induced conformational cycle of the molecular chaperone Hsp90. Nature Structural and Molecular Biology 2009 16 3 287 293 10.1038/nsmb.1565 2-s2.0-61949349758
21. Mickler M., Hessling M., Ratzke C., Buchner J., Hugel T., The large conformational changes of Hsp90 are only weakly coupled to ATP hydrolysis. Nature Structural and Molecular Biology 2009 16 3 281 286 10.1038/nsmb.1557 2-s2.0-61949212626
22. Meyer P., Prodromou C., Hu B., Vaughan C., Roe S. M., Panaretou B., Piper P. W., Pearl L. H., Structural and functional analysis of the middle segment of Hsp90: implications for ATP hydrolysis and client protein and cochaperone interactions. Molecular Cell 2003 11 3 647 658 10.1016/S1097-2765(03)00065-0 2-s2.0-0037352446
23. Harris S. F., Shiau A. K., Agard D. A., The crystal structure of the carboxy-terminal dimerization domain of htpG, the Escherichia coli Hsp90, reveals a potential substrate binding site. Structure 2004 12 6 1087 1097 10.1016/j.str.2004.03.020 2-s2.0-2942533020
24. Hagn F., Lagleder S., Retzlaff M., Rohrberg J., Demmer O., Richter K., Buchner J., Kessler H., Structural analysis of the interaction between Hsp90 and the tumor suppressor protein p53. Nature Structural and Molecular Biology 2011 18 10 1086 1093 10.1038/nsmb.2114 2-s2.0-80455155014
25. Zhang M., Windheim M., Roe S. M., Peggie M., Cohen P., Prodromou C., Pearl L. H., Chaperoned ubiquitylation: crystal structures of the CHIP U box E3 ubiquitin ligase and a CHIP-Ubc13-Uev1a complex. Molecular Cell 2005 20 4 525 538 10.1016/j.molcel.2005.09.023 2-s2.0-27944495299
26. Scheufler C., Brinker A., Bourenkov G., Pegoraro S., Moroder L., Bartunik H., Hartl F. U., Moarefi I., Structure of TPR domain-peptide complexes: critical elements in the assembly of the Hsp70-Hsp90 multichaperone machine. Cell 2000 101 2 199 210 10.1016/S0092-8674(00)80830-2 2-s2.0-0034646511
27. Prodromou C., Panaretou B., Chohan S., Siligardi G., O'Brien R., Ladbury J. E., Roe S. M., Piper P. W., Pearl L. H., The ATPase cycle of Hsp90 drives a molecular 'clamp' via transient dimerization of the hi-terminal domains. The EMBO Journal 2000 19 16 4383 4392 10.1093/emboj/19.16.4383 2-s2.0-0034663806
28. Makhnevych T., Houry W. A., The role of Hsp90 in protein complex assembly. Biochimica et Biophysica Acta-Molecular Cell Research 2012 1823 3 674 682 10.1016/j.bbamcr.2011.09.001 2-s2.0-84857053558
29. Samakovli D., Thanou A., Valmas C., Hatzopoulos P., Hsp90 canalizes developmental perturbation. Journal of Experimental Botany 2007 58 13 3513 3524 10.1093/jxb/erm191 2-s2.0-36849021614
30. Specchia V., Piacentini L., Tritto P., Fanti L., Dalessandro R., Palumbo G., Pimpinelli S., Bozzetti M. P., Hsp90 prevents phenotypic variation by suppressing the mutagenic activity of transposons. Nature 2010 463 7281 662 665 10.1038/nature08739 2-s2.0-76349117871
31. Zuehlke A., Johnson J. L., Hsp90 and co-chaperones twist the functions of diverse client proteins. Biopolymers 2010 93 3 211 217 10.1002/bip.21292 2-s2.0-75149177573
32. Johnson J. L., Brown C., Plasticity of the Hsp90 chaperone machine in divergent eukaryotic organisms. Cell Stress and Chaperones 2009 14 1 83 94 10.1007/s12192-008-0058-9 2-s2.0-58149271606
33. Taipale M., Jarosz D. F., Lindquist S., HSP90 at the hub of protein homeostasis: emerging mechanistic insights. Nature Reviews Molecular Cell Biology 2010 11 7 515 528 10.1038/nrm2918 2-s2.0-77953916528
34. Li J., Soroka J., Buchner J., The Hsp90 chaperone machinery: conformational dynamics and regulation by co-chaperones. Biochimica et Biophysica Acta-Molecular Cell Research 2012 1823 3 624 635 10.1016/j.bbamcr.2011.09.003 2-s2.0-84857042271
35. Krukenberg K. A., Street T. O., Lavery L. A., Agard D. A., Conformational dynamics of the molecular chaperone Hsp90. Quarterly Reviews of Biophysics 2011 44 2 229 255 10.1017/S0033583510000314 2-s2.0-79955984427
36. Pratt W. B., Toft D. O., Regulation of signaling protein function and trafficking by the hsp90/hsp70-based chaperone machinery. Experimental Biology and Medicine 2003 228 2 111 133 2-s2.0-0037315208
37. Adachi H., Katsuno M., Waza M., Minamiyama M., Tanaka F., Sobue G., Heat shock proteins in neurodegenerative diseases: pathogenic roles and therapeutic implications. International Journal of Hyperthermia 2009 25 8 647 654 10.3109/02656730903315823 2-s2.0-73649130290
38. McClellan A. J., Scott M. D., Frydman J., Folding and quality control of the VHL tumor suppressor proceed through distinct chaperone pathways. Cell 2005 121 5 739 748 10.1016/j.cell.2005.03.024 2-s2.0-20444413061
39. Koren J. III, Jinwal U. K., Lee D. C., Jones J. R., Shults C. L., Johnson A. G., Anderson L. J., Dickey C. A., Chaperone signalling complexes in Alzheimer's disease. Journal of Cellular and Molecular Medicine 2009 13 4 619 630 10.1111/j.1582-4934.2008.00557.x 2-s2.0-65249106782
40. Paris D., Ganey N. J., Laporte V., Patel N. S., Beaulieu-Abdelahad D., Bachmeier C., March A., Ait-Ghezala G., Mullan M. J., Reduction of β -amyloid pathology by celastrol in a transgenic mouse model of Alzheimer's disease. Journal of Neuroinflammation 2010 7, article 17 10.1186/1742-2094-7-17 2-s2.0-77950377674
41. Meyer-Luehmann M., Spires-Jones T. L., Prada C., Garcia-Alloza M., De Calignon A., Rozkalne A., Koenigsknecht-Talboo J., Holtzman D. M., Bacskai B. J., Hyman B. T., Rapid appearance and local toxicity of amyloid- β plaques in a mouse model of Alzheimer's disease. Nature 2008 451 7179 720 724 10.1038/nature06616 2-s2.0-38949123792
42. 1-42 in rat hippocampus in vivo. Neuroscience Letters 2003 344 2 87 90 10.1016/S0304-3940(03)00447-6 2-s2.0-0038356802
43. Evans C. G., Wisén S., Gestwicki J. E., Heat shock proteins 70 and 90 inhibit early stages of amyloid β -(1-42) aggregation in vitro. Journal of Biological Chemistry 2006 281 44 33182 33191 10.1074/jbc.M606192200 2-s2.0-33845918172
44. Peterson L. B., Blagg B. S., To fold or not to fold: modulation and consequences of Hsp90 inhibition. Future Medicinal Chemistry 2009 1 2 267 283 10.4155/fmc.09.17 2-s2.0-74249109889
45. Luo W., Dou F., Rodina A., Chip S., Kim J., Zhao Q., Moulick K., Aguirre J., Wu N., Greengard P., Chiosis G., Roles of heat-shock protein 90 in maintaining and facilitating the neurodegenerative phenotype in tauopathies. Proceedings of the National Academy of Sciences of the United States of America 2007 104 22 9511 9516 10.1073/pnas.0701055104 2-s2.0-34547183507
46. Goedert M., Tau protein and neurodegeneration. Seminars in Cell and Developmental Biology 2004 15 1 45 49 10.1016/j.semcdb.2003.12.015 2-s2.0-0842281547
47. Mandelkow E. M., Biochemistry and cell biology of tau protein in neurofibrillary degeneration. Cold Spring Harbor Perspectives in Medicine 2012 2 7 a006247 10.1101/cshperspect.a006247 2-s2.0-84868677556
48. Takalo M., Salminen A., Soininen H., Hiltunen M., Haapasalo A., Protein aggregation and degradation mechanisms in neurodegenerative diseases. American Journal of Neurodegenerative Disease 2013 2 1 1 14
49. Dickey C. A., Koren J., Zhang Y.-J., Xu Y.-F., Jinwal U. K., Birnbaum M. J., Monks B., Sun M., Cheng J. Q., Patterson C., Bailey R. M., Dunmore J., Soresh S., Leon C., Morgan D., Petrucelli L., Akt and CHIP coregulate tau degradation through coordinated interactions. Proceedings of the National Academy of Sciences of the United States of America 2008 105 9 3622 3627 10.1073/pnas.0709180105 2-s2.0-42149111606
50. Lau L.-F., Schachter J. B., Seymour P. A., Sanner M. A., Tau protein phosphorylation as a therapeutic target in Alzheimer's disease. Current Topics in Medicinal Chemistry 2002 2 4 395 415 10.2174/1568026024607526 2-s2.0-0036546454
51. Luo W., Sun W., Taldone T., Rodina A., Chiosis G., Heat shock protein 90 in neurodegenerative diseases. Molecular Neurodegeneration 2010 5 1, article 24 10.1186/1750-1326-5-24 2-s2.0-77953012604
52. Wandinger S. K., Richter K., Buchner J., The Hsp90 chaperone machinery. The Journal of Biological Chemistry 2008 283 27 18473 18477 10.1074/jbc.R800007200 2-s2.0-49649117517
53. Sahara N., Murayama M., Mizoroki T., Urushitani M., Imai Y., Takahashi R., Murata S., Tanaka K., Takashima A., In vivo evidence of CHIP up-regulation attenuating tau aggregation. Journal of Neurochemistry 2005 94 5 1254 1263 10.1111/j.1471-4159.2005.03272.x 2-s2.0-24144440041
54. Dickey C. A., Yue M., Lin W.-L., Dickson D. W., Dunmore J. H., Lee W. C., Zehr C., West G., Cao S., Clark A. M. K., Caldwell G. A., Caldwell K. A., Eckman C., Patterson C., Hutton M., Petrucelli L., Deletion of the ubiquitin ligase CHIP leads to the accumulation, but not the aggregation, of both endogenous phospho- and caspase-3-cleaved tau species. Journal of Neuroscience 2006 26 26 6985 6996 10.1523/JNEUROSCI.0746-06.2006 2-s2.0-33745959291
55. Garcia-Carbonero R., Carnero A., Paz-Ares L., Inhibition of HSP90 molecular chaperones: moving into the clinic. The Lancet Oncology 2013 14 9 e358 e369 10.1016/S1470-2045(13)70169-4 2-s2.0-84880787644
56. Zhao H., Michaelis M. L., Blagg B. S. J., Hsp90 modulation for the treatment of Alzheimer's disease. Advances in Pharmacology 2012 64 1 25 10.1016/B978-0-12-394816-8.00001-5 2-s2.0-84864301098
57. Selkoe D. J., Alzheimer disease: mechanistic understanding predicts novel therapies. Annals of Internal Medicine 2004 140 8 627 238 10.7326/0003-4819-140-8-200404200-00010 2-s2.0-5644239087
58. Dou F., Yuan L.-D., Zhu J.-J., Heat shock protein 90 indirectly regulates ERK activity by affecting Raf protein metabolism. Acta Biochimica et Biophysica Sinica 2005 37 7 501 505 10.1111/j.1745-7270.2005.00069.x 2-s2.0-24944546195
59. Pei J. J., Braak H., An W. L., Winblad B., Cowburn R. F., Iqbal K., Grundke-Iqbal I., Up-regulation of mitogen-activated protein kinases ERK1/2 and MEK1/2 is associated with the progression of neurofibrillary degeneration in Alzheimer's disease. Molecular Brain Research 2002 109 1-2 45 55 10.1016/S0169-328X(02)00488-6 2-s2.0-12244279939
60. Gezen-Ak D., Dursun E., Hanaasi H., Bilgiç B., Lohman E., Araz Ö. S., Atasoy I. L., Alayliolu M., Önal B., Gürvit H., Yilmazer S., BDNF, TNFα HSP90, CFH, and IL-10 serum levels in patients with early or late onset Alzheimer's disease or mild cognitive impairment. Journal of Alzheimer's Disease 2013 37 1 185 195 10.3233/JAD-130497 2-s2.0-84883187048
61. Ansar S., Burlison J. A., Hadden M. K., Yu X. M., Desino K. E., Bean J., Neckers L., Audus K. L., Michaelis M. L., Blagg B. S. J., A non-toxic Hsp90 inhibitor protects neurons from A β -induced toxicity. Bioorganic and Medicinal Chemistry Letters 2007 17 7 1984 1990 10.1016/j.bmcl.2007.01.017 2-s2.0-33847660142
62. Yokota T., Mishra M., Akatsu H., Tani Y., Miyauchi T., Yamamoto T., Kosaka K., Nagai Y., Sawada T., Heese K., Brain site-specific gene expression analysis in Alzheimer's disease patients. European Journal of Clinical Investigation 2006 36 11 820 830 10.1111/j.1365-2362.2006.01722.x 2-s2.0-33749998298