Non-fibrillar components of amyloid deposits mediate the self-association and tangling of amyloid fibrils
AuthorMacRaild, CA; Stewart, CR; Mok, YF; Gunzburg, MJ; Perugini, MA; Lawrence, LJ; Tirtaatmadja, V; Cooper-White, JJ; Howlett, GJ
Source TitleJOURNAL OF BIOLOGICAL CHEMISTRY
PublisherAMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
University of Melbourne Author/sMOK, YEE-FOONG; Perugini, Matthew; COOPER-WHITE, JUSTIN; Howlett, Geoffrey; TIRTAATMADJA, VIYADA; Mok, Yee-Foong; MACRAILD, CHRISTOPHER ANDREW; STEWART, CAMERON ROBERT; GUNZBURG, MENACHEM JOSEPH
AffiliationBiochemistry And Molecular Biology
Document TypeJournal Article
CitationsMacRaild, C. A., Stewart, C. R., Mok, Y. F., Gunzburg, M. J., Perugini, M. A., Lawrence, L. J., Tirtaatmadja, V., Cooper-White, J. J. & Howlett, G. J. (2004). Non-fibrillar components of amyloid deposits mediate the self-association and tangling of amyloid fibrils. JOURNAL OF BIOLOGICAL CHEMISTRY, 279 (20), pp.21038-21045. https://doi.org/10.1074/jbc.M314008200.
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C1 - Journal Articles Refereed
Amyloid deposits are proteinaceous extra-cellular aggregates associated with a diverse range of disease states. These deposits are composed predominantly of amyloid fibrils, the unbranched, beta-sheet rich structures that result from the misfolding and subsequent aggregation of many proteins. In addition, amyloid deposits contain a number of non-fibrillar components that interact with amyloid fibrils and are incorporated into the deposits in their native folded state. The influence of a number of the non-fibrillar components in amyloid-related diseases is well established; however, the mechanisms underlying these effects are poorly understood. Here we describe the effect of two of the most important non-fibrillar components, serum amyloid P component and apolipoprotein E, upon the solution behavior of amyloid fibrils in an in vitro model system. Using analytical ultracentrifugation, electron microscopy, and rheological measurements, we demonstrate that these non-fibrillar components cause soluble fibrils to condense into localized fibrillar aggregates with a greatly enhanced local density of fibril entanglements. These results suggest a possible mechanism for the observed role of non-fibrillar components as mediators of amyloid deposition and deposit stability.
KeywordsBiochemistry and Cell Biology not elsewhere classified ; Biological Sciences
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