Aβ1-42 induces mild endoplasmic reticulum stress in an aggregation state-dependent manner

Antioxidants and Redox Signaling

Volumn 9, Issue 12, 2007, Pages 2245-2254

  Chafekar, Sidhartha M ^a   Hoozemans, Jeroen J M ^a,b   Zwart, Rob ^a   Baas, Frank ^a   Scheper, Wiep ^a,c  

^a UNIVERSITY OF AMSTERDAM   (Netherlands)

^b VU UNIVERSITY MEDICAL CENTER   (Netherlands)

^c ACADEMIC MEDICAL CENTER   (Netherlands)

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID BETA PROTEIN[1-42]; AMYLOID BETA PROTEIN; AMYLOID BETA PROTEIN (1 42); AMYLOID BETA-PROTEIN (1-42); CALNEXIN; DIMETHYL SULFOXIDE; FLUORESCENT DYE; FORMAZAN; MTT FORMAZAN; PEPTIDE FRAGMENT; TETRAZOLIUM; THIAZOLE DERIVATIVE; THIOFLAVINE; TUNICAMYCIN; UNCLASSIFIED DRUG;

ALZHEIMER DISEASE; ARTICLE; CONTROLLED STUDY; ENDOPLASMIC RETICULUM STRESS; HUMAN; HUMAN CELL; NEUROBLASTOMA CELL; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN CONFORMATION; PROTEIN FOLDING; CELL DIFFERENTIATION; CELL LINE; CELL SURVIVAL; CHEMICALLY INDUCED DISORDER; CHEMISTRY; COMPARATIVE STUDY; DOSE RESPONSE; DRUG EFFECT; ENDOPLASMIC RETICULUM; GENETIC TRANSFECTION; METABOLISM; NEUROBLASTOMA; NICK END LABELING; PATHOLOGY; STRESS; TEMPERATURE; TIME; ULTRASTRUCTURE;

AMYLOID BETA-PROTEIN; CALNEXIN; CELL DIFFERENTIATION; CELL LINE; CELL SURVIVAL; DIMETHYL SULFOXIDE; DOSE-RESPONSE RELATIONSHIP, DRUG; ENDOPLASMIC RETICULUM; FLUORESCENT DYES; FORMAZANS; HUMANS; IN SITU NICK-END LABELING; NEUROBLASTOMA; PEPTIDE FRAGMENTS; PROTEIN CONFORMATION; STRESS; TEMPERATURE; TETRAZOLIUM SALTS; THIAZOLES; TIME FACTORS; TRANSFECTION; TUNICAMYCIN;

EID: 35848951621     PISSN: 15230864     EISSN: None     Source Type: Journal    
DOI: 10.1089/ars.2007.1797     Document Type: Article

References (22)

1. Dahlgren KN, Manelli AM, Stine WB Jr, Baker LK, Krafft GA, and LaDu MJ. Oligomeric and fibrillar species of amyloid-beta peptides differentially affect neuronal viability. J Biol Chem 277: 32046-32053, 2002.
2. Demuro A, Mina E, Kayed R, Milton SC, Parker I, and Glabe CG. Calcium dysregulation and membrane disruption as a ubiquitous neurotoxic mechanism of soluble amyloid oligomers. J Biol Chem 280: 17294-17300, 2005.
3. Engel WK and Askanas V. Inclusion-body myositis: clinical, diagnostic, and pathologic aspects. Neurology 66: S20-S29, 2006.
4. 2+ release through ryanodine and inositol 1,4,5-triphosphate receptors in the neurotoxic effects induced by the amyloid-beta peptide. J Neurosci Res 76: 872-880, 2004.
5. Forman MS, Lee VM, and Trojanowski JQ. "Unfolding" pathways in neurodegenerative disease. Trends Neurosci 26: 407-410, 2003.
6. Hitomi J, Katayama T, Eguchi Y, Kudo T, Taniguchi M, Koyama Y, Manabe T, Yamagishi S, Bando Y, Imaizumi K, Tsujimoto Y, and Tohyama M. Involvement of caspase-4 in endoplasmic reticulum stress-induced apoptosis and Abeta-induced cell death. J Cell Biol 165: 347-356, 2004.
7. Hoozemans JJ, Chafekar SM, Baas F, Eikelenboom P, and Scheper W. Always around, never the same: pathways of amyloid beta induced neurodegeneration throughout the pathogenic cascade of Alzheimer's disease. Curr Med Chem 13: 2599-2605, 2006.
8. Hoozemans JJ, Stieler J, van Haastert ES, Veerhuis R, Rozemuller AJ, Baas F, Eikelenboom P, Arendt T, and Scheper W. The unfolded protein response affects neuronal cell cycle protein expression: implications for Alzheimer's disease pathogenesis. Exp Gerontol 41: 380-386, 2006.
9. Hoozemans JJ, Veerhuis R, Rozemuller AJ, Baas F, Eikelenboom P, and Scheper W. The unfolded protein response is activated in Alzheimer's disease. Acta Neuropathol (Berl) 110: 165-172, 2005.
10. Iuvone T, Esposito G, Esposito R, Santamaria R, Di Rosa M, and Izzo AA. Neuroprotective effect of cannabidiol, a non-psychoactive component from Cannabis sativa, on beta-amyloid-induced toxicity in PC12 cells. J Neurochem 89: 134-141, 2004.
11. Iwawaki T, Akai R, Kohno K, and Miura M. A transgenic mouse model for monitoring endoplasmic reticulum stress. Nat Med 10: 98-102, 2004.
12. Kayed R, Head E, Thompson JL, McIntire TM, Milton SC, Cotman CW, and Glabe CG. Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis. Science 300: 486-489, 2003.
13. Klyubin I, Walsh DM, Lemere CA, Cullen WK, Shankar GM Betts V, Spooner ET, Jiang L, Anwyl R, Selkoe DJ, and Rowan MJ. Amyloid beta protein immunotherapy neutralizes Abeta oligomers that disrupt synaptic plasticity in vivo. Nat Med 11: 556-561, 2005.
14. Lambert MP, Barlow AK, Chromy BA, Edwards C, Freed R, Liosatos M, Morgan TE, Rozovsky I, Trommer B, Viola KL, Wals P, Zhang C, Finch CE, Krafft GA, and Klein WL. Diffusible, nonfibrillar ligands derived from Abeta1-42 are potent central nervous system neurotoxins. Proc Natl Acad Sci U S A 95: 6448-6453, 1998.
15. Mattson MP. Pathways towards and away from Alzheimer's disease. Nature 430: 631-639, 2004.
16. Nakagawa T, Zhu H, Morishima N, Li E, Xu J, Yankner BA, and Yuan J. Caspase-12 mediates endoplasmic-reticulum-specific apoptosis and cytotoxicity by amyloid-beta. Nature 403: 98-103, 2000.
17. Rutkowski DT and Kaufman RJ. A trip to the ER: coping with stress. Trends Cell Biol 14: 20-28, 2004.
18. Suen, KC Lin KF, Elyaman W, So KF, Chang RC, and Hugon J. Reduction of calcium release from the endoplasmic reticulum could only provide partial neuroprotection against beta-amyloid peptide toxicity. J Neurochem 87: 1413-1426, 2003.
19. Unterberger U, Hoftberger R, Gelpi E, Flicker H, Budka H, and Voigtlander T. Endoplasmic reticulum stress features are prominent in Alzheimer disease but not in prion diseases in vivo. J Neuropathol Exp Neurol 65: 348-357, 2006.
20. Vattemi G, Engel WK, McFerrin J, and Askanas V. Endoplasmic reticulum stress and unfolded protein response in inclusion body myositis muscle. Am J Pathol 164: 1-7, 2004.
21. Yu MS, Suen KC, Kwok NS, So KF, Hugon J, and Chuen-Chung Chang R. Beta-amyloid peptides induces neuronal apoptosis via a mechanism independent of unfolded protein responses. Apoptosis 11: 687-700, 2006.
22. Yu Z, Luo, H, Fu W, and Mattson MP. The endoplasmic reticulum stress-responsive protein GRP78 protects neurons against excitotoxicity and apoptosis: suppression of oxidative stress and stabilization of calcium homeostasis. Exp Neurol 155: 302-314, 1999.