Amyloid and amyloidosis - download pdf or read online

By Gilles Grateau, Robert A. Kyle, Martha Skinner

ISBN-10: 0849335345

ISBN-13: 9780849335341

This authoritative quantity comprises 179 chapters through foreign specialists on contemporary advancements in our knowing of amyloid proteins, protein folding problems, and new and proposed medical trials in amyloidosis. themes comprise detection and characterization suggestions; organic features; genetics; issues, prognosis, and coverings, together with organ transplants and drug treatments; effects from broad medical stories; and epidemiology. this can be a invaluable source for clinicians who take care of sufferers with systemic and localized kinds of amyloidosis, and for researchers in biochemistry, neurobiology, and phone biology.

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The molecular species of lipids present in amyloid deposits are given in table 1. The relative peak intensities were distinguished in 3 categories: ++ denotes high intensity, + moderate and 0 indicates just detectable amounts of lipids. 15 16 Amyloid and Amyloidosis Table 1. Membrane lipid classes and their molecular species found in ex vivo amyloid fibrils AA1 GC SU PE PS PC SM 18:0 18:1 20:1 22:0 22:1 22:2 22:4 24:0 24:1 24:2 26:0 26:1 26:2 26:3 26:4 24: 0 24:3 26:6 18:0/20:4 18:0/22:4 18:0/22:6 18:0/24:3 (p)18:0/18:2 (p)18:0/20:4 PI 16:0/22:4 18:0/20:4 18:1/20:4 18:1/22:6 16:0/16:1 16:1/18:1 16:1/18:2 16:0/20:2 16:0/22:0 18:0/18:1 18:0/20:4 18:0/22:0 18:0/22:4 18:0/22:6 18:1/18:2 (p)20:0/22:1 (p)20:0/22:2 16:0/16:0 16:0/18:1 16:0/20:4 18:0/20:4 18:1/20:4 18:0 18:1 22:0 24:0 24:1 24:2 AA2 AA3 AL1 AL2 AL3 AL4 AL5 AL6 + + + ++ + + ++ ++ 0 ++ ++ 0 ++ + + ++ ++ + + ++ + ++ + + + ++ + + ++ ++ + + ++ + + + + + + + ++ + + ++ ++ ++ + ++ + + ++ ++ 0 ++ ++ 0 ++ ++ ++ + + ++ ++ + + ++ ++ + ++ + + + + ++ 0 + ++ ++ + 0 ++ ++ + + + + ++ ++ ++ + ++ + 0 ++ + + ++ + ++ ++ + Our analyses revealed that the lipid composition of amyloid fibrils is distinct from healthy tissue in that it is particularly rich in cholesterol and sphingolipids and contain only very rare amounts of those phospholipids, PE and PC, that occur in undiseased tissues in very high amounts (Fig.

THERAPEUTIC IMPLICATIONS Reversion of misfolded proteins to their native state and clearance of amyloid deposits by destabilization of the aggregates have been shown to be winning therapeutic strategies to treat both neurodegenerative and systemic diseases related to protein aggregation (2-3). Our study suggests that the population of aggregates, at least in the case of AcP, is made of species with distinct sizes and thermodynamic properties and could provide a base for the design of appropriate approaches to the treatment of diseases associated with protein aggregation.

The recombinat variant, rec-stB, which is the least stable, starts Amyloid Fibrillogenesis 23 fibril growth after a lag phase of about 200 hours, and the EPM1 mutant - G4R, after a lag phase of about 400 hours. The yield of mature fibrils (as judged by intensity of ThT fluorescence) follows the same trend : wt-stB > rec-stB> G4R. Especially striking is the behavior of the EPM1 mutant, G4R, which is of equal stability than the wild-type (see Table 1) yet it has the lowest propensity to fibrillise.

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Amyloid and amyloidosis by Gilles Grateau, Robert A. Kyle, Martha Skinner


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