NDLI: The structural basis for amyloid formation by plasma apolipoproteins: a review

Content Provider	Springer Nature Link
Author	Hatters, Danny M. Howlett, Geoffrey J.
Copyright Year	2001
Abstract	The formation of amyloid and other protein deposits in vivo is synonymous with many pathological conditions such as Alzheimer's disease, Creutzfeldt-Jakob disease and Parkinson's disease. Interestingly, many plasma apolipoproteins are also associated with amyloid deposits, including apolipoprotein (apo) A-I, apoA-II and apoE. Apolipoproteins share a number of structural and conformational properties, namely a large proportion of class A amphipathic α-helices and limited conformational stability in the absence of lipid. Other proteins that form amyloid such as α-synuclein and serum amyloid A also contain amphipathic α-helical domains similar to those found in apolipoproteins. In this review we develop a hypothesis to account for the widespread occurrence of apolipoproteins in amyloid deposits. We describe the conformational stability of human apoC-II and the stabilization of α-helical structure in the presence of phospholipid. We propose that lipid-free apoC-II forms partially folded intermediates prone to amyloid formation. Parameters that affect apolipoprotein lipid binding in vivo, such as protein and lipid oxidation or protein truncations and mutations, could promote apolipoprotein-related pathologies including those associated within amyloid deposits of atherosclerotic plaques.
Starting Page	2
Ending Page	8
Page Count	7
File Format	PDF
ISSN	01757571
Journal	European Biophysics Journal
Volume Number	31
Issue Number	1
e-ISSN	14321017
Language	English
Publisher	Springer-Verlag
Publisher Date	2014-02-08
Publisher Place	Berlin, Heidelberg
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Biochemistry Biophysics and Biological Physics Cell Biology Neurobiology Membrane Biology Nanotechnology
Content Type	Text
Resource Type	Article
Subject	Medicine Biophysics

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