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Transthyretin Inter...
Transthyretin Interferes with Aβ Amyloid Formation by Redirecting Oligomeric Nuclei into Non-Amyloid Aggregates
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- Nilsson, Lina (author)
- Umeå universitet,Institutionen för medicinsk kemi och biofysik
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- Pamrén, Annelie (author)
- Umeå universitet,Institutionen för medicinsk kemi och biofysik
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- Islam, Tohidul (author)
- Umeå universitet,Institutionen för medicinsk kemi och biofysik
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- Brännström, Kristoffer (author)
- Umeå universitet,Institutionen för medicinsk kemi och biofysik
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- Golchin, Solmaz A. (author)
- Umeå universitet,Institutionen för medicinsk kemi och biofysik
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- Pettersson, Nina (author)
- Umeå universitet,Institutionen för medicinsk kemi och biofysik
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- Iakovleva, Irina (author)
- Umeå universitet,Institutionen för medicinsk kemi och biofysik
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- Sandblad, Linda (author)
- Umeå universitet,Institutionen för molekylärbiologi (Medicinska fakulteten)
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- Gharibyan, Anna L. (author)
- Umeå universitet,Institutionen för medicinsk kemi och biofysik
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- Olofsson, Anders (author)
- Umeå universitet,Institutionen för medicinsk kemi och biofysik
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(creator_code:org_t)
- Elsevier, 2018
- 2018
- English.
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In: Journal of Molecular Biology. - : Elsevier. - 0022-2836 .- 1089-8638. ; 430:17, s. 2722-2733
- Related links:
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https://urn.kb.se/re...
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https://doi.org/10.1...
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Abstract
Subject headings
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- The pathological Aβ aggregates associated with Alzheimer's disease follow a nucleation-dependent path of formation. A nucleus represents an oligomeric assembly of Aβ peptides that acts as a template for subsequent incorporation of monomers to form a fibrillar structure. Nuclei can form de novo or via surface-catalyzed secondary nucleation, and the combined rates of elongation and nucleation control the overall rate of fibril formation. Transthyretin (TTR) obstructs Aβ fibril formation in favor of alternative non-fibrillar assemblies, but the mechanism behind this activity is not fully understood. This study shows that TTR does not significantly disturb fibril elongation; rather, it effectively interferes with the formation of oligomeric nuclei. We demonstrate that this interference can be modulated by altering the relative contribution of elongation and nucleation, and we show how TTR's effects can range from being essentially ineffective to almost complete inhibition of fibril formation without changing the concentration of TTR or monomeric Aβ.
Subject headings
- MEDICIN OCH HÄLSOVETENSKAP -- Medicinska och farmaceutiska grundvetenskaper -- Cell- och molekylärbiologi (hsv//swe)
- MEDICAL AND HEALTH SCIENCES -- Basic Medicine -- Cell and Molecular Biology (hsv//eng)
Keyword
- Aβ
- Surface Plasmon Resonance
- Thioflavin-T
- amyloid
- transthyretin
Publication and Content Type
- ref (subject category)
- art (subject category)
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To the university's database
- By the author/editor
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Nilsson, Lina
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Pamrén, Annelie
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Islam, Tohidul
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Brännström, Kris ...
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Golchin, Solmaz ...
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Pettersson, Nina
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show more...
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Iakovleva, Irina
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Sandblad, Linda
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Gharibyan, Anna ...
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Olofsson, Anders
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show less...
- About the subject
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- MEDICAL AND HEALTH SCIENCES
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MEDICAL AND HEAL ...
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and Basic Medicine
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and Cell and Molecul ...
- Articles in the publication
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Journal of Molec ...
- By the university
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Umeå University