Alzheimer's disease amyloid β-protein mutations and deletions that define neuronal binding/internalization as early stage nonfibrillar/fibrillar aggregates and late stage fibrils

Biochemistry

Volumn 51, Issue 19, 2012, Pages 3993-4003

  Poduslo, Joseph F ^a   Howell, Kyle G ^a   Olson, Nicole C ^a   Ramirez Alvarado, Marina ^a   Kandimalla, Karunya K ^a,b  

^a MAYO CLINIC   (United States)

^b UNIVERSITY OF MINNESOTA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AGGREGATION STATE; ALZHEIMER'S DISEASE; AMYLOID PLAQUES; DOSE-DEPENDENT; EXTRACELLULAR SPACE; FIBRILLAR STRUCTURES; FLUORESCENCE ANISOTROPY; HISTIDINE RESIDUES; LATE STAGE; MULTIPLE PATHWAYS; NEURODEGENERATION; PC12 CELLS; PRE-TREATMENT; PROTEIN MUTATIONS; ROOM TEMPERATURE; STRUCTURAL BASIS; THERAPEUTIC TARGETS; TRANSFECTED CELLS; TRANSGENIC MICE;

AGGREGATES; AMINO ACIDS; ATOMIC FORCE MICROSCOPY; CENTRIFUGATION; DIMETHYL SULFOXIDE; GLYCOPROTEINS; MAMMALS; ORGANIC SOLVENTS; RIGIDITY; TRANSMISSION ELECTRON MICROSCOPY;

PROTEINS;

AMYLOID BETA PROTEIN; AMYLOID BETA PROTEIN[1-40]; AMYLOID BETA PROTEIN[1-42]; DIMETHYL SULFOXIDE; GLUTAMIC ACID; HISTIDINE; LYSOZYME; TYROSINE;

ALZHEIMER DISEASE; ANISOTROPY; ARTICLE; ATOMIC FORCE MICROSCOPY; CENTRIFUGATION; DEMENTIA; DISEASE SEVERITY; EARLY STAGE FIBRILLAR AGGREGATE; EARLY STAGE NONFIBRILLAR AGGREGATE; EMISSION ANISOTROPY; GENE DELETION; GENE MUTATION; HIPPOCAMPUS; LATE STAGE FIBRIL; NERVE DEGENERATION; NERVOUS SYSTEM PARAMETERS; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN BINDING; ROOM TEMPERATURE; TRANSMISSION ELECTRON MICROSCOPY;

ALZHEIMER DISEASE; AMINO ACID SEQUENCE; AMYLOID; AMYLOID BETA-PEPTIDES; ANIMALS; DIMETHYL SULFOXIDE; FLUORESCENCE POLARIZATION; HISTIDINE; HUMANS; MICROSCOPY, ATOMIC FORCE; MICROSCOPY, ELECTRON, TRANSMISSION; MOLECULAR SEQUENCE DATA; MUTATION; NEURONS; PC12 CELLS; PROTEIN STRUCTURE, TERTIARY; RATS;

MUS MUSCULUS;

EID: 84861142911     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi300275g     Document Type: Article

References (15)

1. Echeverria, V. and Cuello, A. C. (2002) Intracellular A-β amyloid, a sign for worse things to come? Mol. Neurobiol. 26, 299-316
2. Tseng, B. P., Kitazawa, M., and LaFerla, F. M. (2004) Amyloid β-peptide: The inside story Curr. Alzheimer Res. 1, 231-239
3. Wirths, O., Multhaup, G., and Bayer, T. A. (2004) A modified β-amyloid hypothesis: Intraneuronal accumulation of the β-amyloid peptide-the first step of a fatal cascade J. Neurochem. 91, 513-520
4. Gouras, G. K., Almeida, C. G., and Takahashi, R. H. (2005) Intraneuronal Aβ accumulation and origin of plaques in Alzheimer's disease Neurobiol. Aging 26, 1235-1244
5. Li, M., Chen, L., Lee, D. H., Yu, L. C., and Zhang, Y. (2007) The role of intracellular amyloid β in Alzheimer's disease Prog. Neurobiol. 83, 131-139
6. Kandimalla, K. K., Scott, O. G., Fulzele, S., Davidson, M. W., and Poduslo, J. F. (2009) Mechanism of neuronal versus endothelial cell uptake of Alzheimer's disease amyloid β protein PLoS One 4, e4627
7. Poduslo, J. F., Gilles, E. J., Ramakrishnan, M., Howell, K. G., Wengenack, T. M., Curran, G. L., and Kandimalla, K. K. (2010) HH domain of Alzheimer's disease Aβ provides structural basis for neuronal binding in PC12 and mouse cortical/hippocampal neurons PLoS One 5, e8813
8. Tomiyama, T., Nagata, T., Shimada, H., Teraoka, R., Fukushima, A., Kanemitsu, H., Takuma, H., Kuwano, R., Imagawa, M., Ataka, S., Wada, Y., Yoshioka, E., Nishizaki, T., Watanabe, Y., and Mori, H. (2008) A new amyloid β variant favoring oligomerization in Alzheimer's-type dementia Ann. Neurol. 63, 377-387
9. Nishitsuji, K., Tomiyama, T., Ishibashi, K., Ito, K., Teraoka, R., Lambert, M. P., Klein, W. L., and Mori, H. (2009) The E693Δ mutation in amyloid precursor protein increases intracellular accumulation of amyloid β oligomers and causes endoplasmic reticulum stress-induced apoptosis in cultured cells Am. J. Pathol. 174, 957-969
10. Tomiyama, T., Matsuyama, S., Iso, H., Umeda, T., Takuma, H., Ohnishi, K., Ishibashi, K., Teraoka, R., Sakama, N., Yamashita, T., Nishitsuji, K., Ito, K., Shimada, H., Lambert, M. P., Klein, W. L., and Mori, H. (2010) A mouse model of amyloid β oligomers: Their contribution to synaptic alteration, abnormal tau phosphorylation, glial activation, and neuronal loss in vivo J. Neurosci. 30, 4845-4856
11. Ovchinnikova, O. Y., Finder, V. H., Vodopivec, I., Nitsch, R. M., and Glockshuber, R. (2011) The Osaka FAD mutation E22Δ leads to the formation of a previously unknown type of amyloid β fibrils and modulates Aβ neurotoxicity J. Mol. Biol. 408, 780-791
12. Cloe, A. L., Orgel, J. P., Sachleben, J. R., Tycko, R., and Meredith, S. C. (2011) The Japanese mutant Aβ (ΔE22-Aβ(1-39)) forms fibrils instantaneously, with low-thioflavin T fluorescence: seeding of wild-type Aβ(1-40) into atypical fibrils by ΔE22-Aβ(1-39) Biochemistry 50, 2026-2039
13. Lakowicz, J. R. (1983) in Principles of Fluorescence Spectroscopy, Chapter 5, Plenum Press, New York.
14. Ren, P. H., Lauckner, J. E., Kachirskaia, I., Heuser, J. E., Melki, R., and Kopito, R. R. (2009) Cytoplasmic penetration and persistent infection of mammalian cells by polyglutamine aggregates Nat. Cell Biol. 11, 219-225
15. Frost, B., Jacks, R. L., and Diamond, M. I. (2009) Propagation of tau misfolding from the outside to the inside of a cell J. Biol. Chem. 284, 12845-12852