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Amyloid fibril polymorphism: a challenge for molecular imaging and therapy
Ulm Univ, Germany.
Linköping University, Department of Physics, Chemistry and Biology, Chemistry. Linköping University, Faculty of Science & Engineering.
Linköping University, Department of Physics, Chemistry and Biology, Chemistry. Linköping University, Faculty of Science & Engineering.ORCID iD: 0000-0002-5582-140X
Univ Lyon, France.
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2018 (English)In: Journal of Internal Medicine, ISSN 0954-6820, E-ISSN 1365-2796, Vol. 283, no 3, p. 218-237Article in journal (Refereed) Published
Abstract [en]

The accumulation of misfolded proteins (MPs), both unique and common, for different diseases is central for many chronic degenerative diseases. In certain patients, MP accumulation is systemic (e.g. TTR amyloid), and in others, this is localized to a specific cell type (e.g. Alzheimers disease). In neurodegenerative diseases, NDs, it is noticeable that the accumulation of MP progressively spreads throughout the nervous system. Our main hypothesis of this article is that MPs are not only markers but also active carriers of pathogenicity. Here, we discuss studies from comprehensive molecular approaches aimed at understanding MP conformational variations (polymorphism) and their bearing on spreading of MPs, MP toxicity, as well as MP targeting in imaging and therapy. Neurodegenerative disease (ND) represents a major and growing societal challenge, with millions of people worldwide suffering from Alzheimers or Parkinsons diseases alone. For all NDs, current treatment is palliative without addressing the primary cause and is not curative. Over recent years, particularly the shape-shifting properties of misfolded proteins and their spreading pathways have been intensively researched. The difficulty in addressing ND has prompted most major pharma companies to severely downsize their nervous system disorder research. Increased academic research is pivotal for filling this void and to translate basic research into tools for medical professionals. Recent discoveries of targeting drug design against MPs and improved model systems to study structure, pathology spreading and toxicity strongly encourage future studies along these lines to provide an opportunity for selective imaging, prognostic diagnosis and therapy.

Place, publisher, year, edition, pages
WILEY , 2018. Vol. 283, no 3, p. 218-237
Keywords [en]
Alzheimers disease; amyloidosis; biochemistry; chronic diseases; pathology
National Category
Neurosciences
Identifiers
URN: urn:nbn:se:liu:diva-145436DOI: 10.1111/joim.12732ISI: 000425521000001PubMedID: 29360284OAI: oai:DiVA.org:liu-145436DiVA, id: diva2:1194619
Conference
6th Amyloid Disease Annual Meeting - Molecular Perspectives of Misfolded Proteins
Note

Funding Agencies|Swedish Research Council [2015-04521, 2015-05868]; Goran Gustafsson Foundation; Swedish Alzheimer Foundation; Linkoping University; NIH/NINDS [R21 NS080576]; BrightFocus Foundation [A2014044S]; French ANR [ANR-14-CE09-0024B]; Deutsche Forschungsgemeinschaft [FA 456/15-1]

Available from: 2018-04-03 Created: 2018-04-03 Last updated: 2018-04-25

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