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Methods and models in neurodegenerative and systemic protein aggregation diseases
Linköping University, Department of Physics, Chemistry and Biology, Molecular Biotechnology . Linköping University, The Institute of Technology.
University of Cambridge.
University of Cambridge.
University of Cambridge.
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2010 (English)In: Frontiers in bioscience : a journal and virtual library, ISSN 1093-4715, Vol. 15, 373-396 p.Article, review/survey (Refereed) Published
Abstract [en]

Protein misfolding and aggregation are implicated in a wide range of increasingly prevalent human diseases ranging from dementia to diabetes. In this review we discuss the current experimental strategies that are being employed in the investigation of the pathogenesis of three important protein misfolding disorders. The first, Alzheimers disease (AD), is the most prevalent neurodegenerative disease and is thought to be initiated by the aggregation of a natively unstructured peptide called amyloid beta (Abeta). We discuss methods for the characterization of the aggregation properties of Abeta in vitro and how the results of such experiments can be correlated with data from animal models of disease. We then consider another form of amyloidosis, where a systemic distribution of amyloid deposit is caused by aggregation and deposition of mutational variants of lysozyme. We describe how experiments in vitro, and more recently in vivo, have provided insights into the origins of this disease. Finally we outline the varied paradigms that have been employed in the study of the serpinopathies, and in particular, a dementia caused by neuroserpin polymerization.

Place, publisher, year, edition, pages
Frontiers in Bioscience Publications , 2010. Vol. 15, 373-396 p.
National Category
Engineering and Technology
URN: urn:nbn:se:liu:diva-57011ISI: 000282619800026PubMedID: 20036826OAI: diva2:324074
Available from: 2010-06-14 Created: 2010-06-09 Last updated: 2010-10-29

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Brorsson, Ann-Christin
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Molecular Biotechnology The Institute of Technology
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