Exogenous delivery of chaperonin subunit fragment ApiCCT1 modulates mutant Huntingtin cellular phenotypes

Proceedings of the National Academy of Sciences of the United States of America

Volumn 110, Issue 8, 2013, Pages 3077-3082

  Sontag, Emily M ^a,b   Joachimiak, Lukasz A ^c   Tan, Zhiqun ^a,b   Tomlinson, Anthony ^c   Housman, David E ^d   Glabe, Charles G ^b   Potkinj, Steven G ^b   Frydman, Judith ^c   Thompson, Leslie M ^a,b  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b UNIVERSITY OF CALIFORNIA   (United States)

^c STANFORD UNIVERSITY   (United States)

^d MASSACHUSETTS INSTITUTE OF TECHNOLOGY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

APICCT1 PROTEIN; HUNTINGTIN; NEUROPROTECTIVE AGENT; RECOMBINANT PROTEIN; UNCLASSIFIED DRUG;

ANIMAL CELL; ANIMAL MODEL; ARTICLE; CELL FRACTIONATION; CELL INCLUSION; CELL MEMBRANE; CELL RESPIRATION; CELL VIABILITY; CONCENTRATION RESPONSE; CONTROLLED STUDY; DRUG DELIVERY SYSTEM; DRUG PENETRATION; DRUG TARGETING; EXON; HUNTINGTON CHOREA; IMMUNOCYTOCHEMISTRY; IN VITRO STUDY; MOUSE; NEUROPROTECTION; NONHUMAN; PHENOTYPE; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN EXPRESSION; PROTEIN HOMEOSTASIS; PROTEIN SUBUNIT; STEM CELL;

AMINO ACID SEQUENCE; ANIMALS; BLOTTING, WESTERN; CELL SURVIVAL; CHAPERONINS; ELECTROPHORESIS, POLYACRYLAMIDE GEL; MICE; MOLECULAR SEQUENCE DATA; MUTATION; NERVE TISSUE PROTEINS; NUCLEAR PROTEINS; PC12 CELLS; PHENOTYPE; RATS;

EID: 84874237482     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1222663110     Document Type: Article

References (40)

1. Davies SW, et al. (1997) Formation of neuronal intranuclear inclusions underlies the neurological dysfunction in mice transgenic for the HD mutation. Cell 90 (3):537-548.
2. The Huntington's Disease Collaborative Research Group (1993) A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington's disease chromosomes. Cell 72 (6):971-983.
3. Gusella JF, MacDonald ME (1995) Huntington's disease. Semin Cell Biol 6 (1):21-28.
4. Muchowski PJ, Wacker JL (2005) Modulation of neurodegeneration by molecular chaperones. Nat Rev Neurosci 6 (1):11-22.
5. Muchowski PJ, et al. (2000) Hsp70 and hsp40 chaperones can inhibit self-assembly of polyglutamine proteins into amyloid-like fibrils. Proc Natl Acad Sci USA 97 (14):7841-7846.
6. Chen B, Retzlaff M, Roos T, Frydman J (2011) Cellular strategies of protein quality control. Cold Spring Harb Perspect Biol 3 (8):a004374.
7. Voisine C, Pedersen JS, Morimoto RI (2010) Chaperone networks: Tipping the balance in protein folding diseases. Neurobiol Dis 40 (1):12-20.
8. Warrick JM, et al. (1999) Suppression of polyglutamine-mediated neurodegeneration in Drosophila by the molecular chaperone HSP70. Nat Genet 23 (4):425-428.
9. Cummings CJ, et al. (2001) Over-expression of inducible HSP70 chaperone suppresses neuropathology and improves motor function in SCA1 mice. Hum Mol Genet 10 (14):1511-1518.
10. Wacker JL, et al. (2009) Loss of Hsp70 exacerbates pathogenesis but not levels of fibrillar aggregates in a mouse model of Huntington's disease. J Neurosci 29 (28):9104-9114.
11. Spiess C, Meyer AS, Reissmann S, Frydman J (2004) Mechanism of the eukaryotic chap-eronin: Protein folding in the chamber of secrets. Trends Cell Biol 14 (11):598-604.
12. Yang W, Dunlap JR, Andrews RB, Wetzel R (2002) Aggregated polyglutamine peptides delivered to nuclei are toxic to mammalian cells. Hum Mol Genet 11 (23):2905-2917.
13. Behrends C, et al. (2006) Chaperonin TRiC promotes the assembly of polyQ expansion proteins into nontoxic oligomers. Mol Cell 23 (6):887-897.
14. Kitamura A, et al. (2006) Cytosolic chaperonin prevents polyglutamine toxicity with altering the aggregation state. Nat Cell Biol 8 (10):1163-1170.
15. Tam S, Geller R, Spiess C, Frydman J (2006) The chaperonin TRiC controls polygluta-mine aggregation and toxicity through subunit-specific interactions. Nat Cell Biol 8 (10):1155-1162.
16. Tam S, et al. (2009) The chaperonin TRiC blocks a huntingtin sequence element that promotes the conformational switch to aggregation. Nat Struct Mol Biol 16 (12):1279-1285.
17. DiFiglia M, et al. (1997) Aggregation of huntingtin in neuronal intranuclear inclusions and dystrophic neurites in brain. Science 277 (5334):1990-1993.
18. Saudou F, Finkbeiner S, Devys D, Greenberg ME (1998) Huntingtin acts in the nucleus to induce apoptosis but death does not correlate with the formation of intranuclear inclusions. Cell 95 (1):55-66.
19. Balch WE, Morimoto RI, Dillin A, Kelly JW (2008) Adapting proteostasis for disease intervention. Science 319 (5865):916-919.
20. Koren E, Torchilin VP (2012) Cell-penetrating peptides: Breaking through to the other side. Trends Mol Med 18 (7):385-393.
21. Lindgren M, Hällbrink M, Prochiantz A, Langel U (2000) Cell-penetrating peptides. Trends Pharmacol Sci 21 (3):99-103.
22. Derossi D, et al. (1996) Cell internalization of the third helix of the Antennapedia homeodomain is receptor-independent. J Biol Chem 271 (30):18188-18193.
23. Vivès E, Brodin P, Lebleu B (1997) A truncated HIV-1 Tat protein basic domain rapidly translocates through the plasma membrane and accumulates in the cell nucleus. J Biol Chem 272 (25):16010-16017.
24. Apostol BL, et al. (2003) A cell-based assay for aggregation inhibitors as therapeutics of polyglutamine-repeat disease and validation in Drosophila. Proc Natl Acad Sci USA 100 (10):5950-5955.
25. Arrasate M, Mitra S, Schweitzer ES, Segal MR, Finkbeiner S (2004) Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death. Nature 431 (7010):805-810.
26. Legleiter J, et al. (2010) Mutant huntingtin fragments form oligomers in a polygluta-mine length-dependent manner in vitro and in vivo. J Biol Chem 285 (19):14777-14790.
27. Sontag EM, et al. (2012) Methylene blue modulates huntingtin aggregation intermediates and is protective in Huntington's disease models. J Neurosci 32 (32):11109-11119.
28. Sontag EM, et al. (2012) Detection of mutant huntingtin aggregation conformers and modulation of SDS-soluble fibrillar oligomers by small molecules. Journal of Hun-tington's Disease 1 (1):127-140.
29. Weiss A, et al. (2008) Sensitive biochemical aggregate detection reveals aggregation onset before symptom development in cellular and murine models of Huntington's disease. J Neurochem 104 (3):846-858.
30. Trettel F, et al. (2000) Dominant phenotypes produced by the HD mutation in STHdh (Q111) striatal cells. Hum Mol Genet 9 (19):2799-2809.
31. Apostol BL, et al. (2008) CEP-1347 reduces mutant huntingtin-associated neurotoxicity and restores BDNF levels in R6/2 mice. Mol Cell Neurosci 39 (1):8-20.
32. Rost B, Yachdav G, Liu J (2004) The PredictProtein server. Nucleic Acids Res 32 (Web Server issue):W321-W326.
33. Inden M, et al. (2006) PARK7 DJ-1 protects against degeneration of nigral dopami-nergic neurons in Parkinson's disease rat model. Neurobiol Dis 24 (1):144-158.
34. Benn CL, et al. (2005) Contribution of nuclear and extranuclear polyQ to neurological phenotypes in mouse models of Huntington's disease. Hum Mol Genet 14 (20):3065-3078.
35. Mayhew M, et al. (1996) Protein folding in the central cavity of the GroEL-GroES chaperonin complex. Nature 379 (6564):420-426.
36. Liggett A, Crawford LJ, Walker B, Morris TC, Irvine AE (2010) Methods for measuring proteasome activity: Current limitations and future developments. Leuk Res 34 (11):1403-1409.
37. Sun SY, An CN, Pu XP (2012) DJ-1 protein protects dopaminergic neurons against 6-OHDA/MG-132-induced neurotoxicity in rats. Brain Res Bull 88 (6):609-616.
38. Hacot S, et al. (2001) Isolation of nucleoli. Curr Protoc Cell Biol Chapter 3:Unit3.36.
39. Miyata N, Fujiki Y (2005) Shuttling mechanism of peroxisome targeting signal type 1 receptor Pex5: ATP-independent import and ATP-dependent export. Mol Cell Biol 25 (24):10822-10832.
40. Scherzinger E, et al. (1997) Huntingtin-encoded polyglutamine expansions form amyloid-like protein aggregates in vitro and in vivo. Cell 90 (3):549-558.