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Non-chaperone Prote...
Non-chaperone Proteins Can Inhibit Aggregation and Cytotoxicity of Alzheimer Amyloid beta Peptide
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Luo, Jinghui (author)
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- Wärmländer, Sebastian K. T. S. (author)
- Stockholms universitet,Institutionen för biokemi och biofysik
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- Gräslund, Astrid (author)
- Stockholms universitet,Institutionen för biokemi och biofysik
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Abrahams, Jan Pieter (author)
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(creator_code:org_t)
- 2014
- 2014
- English.
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In: Journal of Biological Chemistry. - 0021-9258 .- 1083-351X. ; 289:40, s. 27766-27775
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https://doi.org/10.1...
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https://urn.kb.se/re...
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Abstract
Subject headings
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- Background: A amyloid formation is associated with Alzheimer disease. Results: Non-chaperone proteins prevent amyloid formation and reduce the cytotoxicity of the A peptide. Conclusion: Non-chaperone proteins may affect the onset and development of Alzheimer disease by interfering with A peptide aggregation. Significance: Non-chaperone proteins can function as a chaperone protein to regulate the pathway of the A fibrillation in proteostasis providing a new strategy in the treatment of Alzheimer disease. Many factors are known to influence the oligomerization, fibrillation, and amyloid formation of the A peptide that is associated with Alzheimer disease. Other proteins that are present when A peptides deposit in vivo are likely to have an effect on these aggregation processes. To separate specific versus broad spectrum effects of proteins on A aggregation, we tested a series of proteins not reported to have chaperone activity: catalase, pyruvate kinase, albumin, lysozyme, -lactalbumin, and -lactoglobulin. All tested proteins suppressed the fibrillation of Alzheimer A(1-40) peptide at substoichiometric ratios, albeit some more effectively than others. All proteins bound non-specifically to A, stabilized its random coils, and reduced its cytotoxicity. Surprisingly, pyruvate kinase and catalase were at least as effective as known chaperones in inhibiting A aggregation. We propose general mechanisms for the broad-spectrum inhibition A fibrillation by proteins. The mechanisms we discuss are significant for prognostics and perhaps even for prevention and treatment of Alzheimer disease.
Subject headings
- NATURVETENSKAP -- Biologi -- Biokemi och molekylärbiologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Biochemistry and Molecular Biology (hsv//eng)
Keyword
- Alzheimer Disease
- Amyloid- (AB)
- Protein Aggregation
- Protein-Protein Interaction
- Spectroscopy
- Aggregates
- Fibrillation
- Toxicity
Publication and Content Type
- ref (subject category)
- art (subject category)
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