Alzheimer's disease is the most common form of dementia and the generation of oligomeric species of amyloid-β is causal to the initiation and progression of it. Amyloid-β oligomers bind to the N-terminus of plasma membrane-bound cellular prion protein (PrP(C)) initiating a series of events leading to synaptic degeneration. Composition of bound amyloid-β oligomers, binding regions within PrP(C),...

Oskarsson, M. 2015. Islet amyloid polypeptide (IAPP) in Type 2 diabetes and Alzheimer disease. Digital Comprehensive Summaries of Uppsala Dissertations from the Faculty of Medicine 1158. 55 pp. Uppsala: Acta Universitatis Upsaliensis. ISBN 978-91-554-9400-1. The misfolding and aggregation of the beta cell hormone islet amyloid polypeptide (IAPP) into amyloid fibrils is the main pathological fin...

Amyloid folds not only represent the underlying cause of a large class of human diseases but also display a variety of functional roles both in prokaryote and eukaryote organisms. Among these roles is a recently-described activity in signal transduction cascades functioning in host defense and programmed cell death and involving Nod-like receptors (NLRs). In different fungal species, prion amyl...

BACKGROUND Amyloidosis refers to a heterogeneous group of disorders associated with the deposition of chemically distinct amyloid fibril proteins. Precise determination of chemical amyloid type has diagnostic, therapeutic, and prognostic relevance. Although immunohistochemical techniques are used routinely to determine the amyloid type, the results can be negative or inconclusive, so that bioch...

Amyloidosis describes a group of protein folding diseases in which amyloid proteins are abnormally deposited in organs and/or tissues as fine fibrils. Mouse senile amyloidosis is a disorder in which apolipoprotein A-II (apoA-II) deposits as amyloid fibrils (AApoAII) and can be transmitted from one animal to another both by the feces and milk excreted by mice with amyloidosis. Thus, mouse AApoAI...

Treatment of Alzheimer’s disease (AD) is hampered by the fact that the disease progression cannot be tracked in vivo at this time. Understanding the properties of Aβ amyloid fibrils associated with AD is imperative to finding a way to track the progression of the disease. Recently, fluorescent markers, derived from thioflavin T have been developed as markers of AD. This project examines the int...

Hilar and mediastinal lymphadenopathy associated with localized pulmonary amyloid is very rare. We describe two cases of this unusual combination, one of endobronchial amyloid with adenopathy and the other of nodular parenchymal amyloid with hilar nodes. In both these cases the nodes contained calcification, and in the nodular parenchymal case in particular, this appearance is highly suggestive...

Fluorescent molecules that specifically target amyloid structures are highly desirable for amyloid research. Herein, we show a dimeric design of thioflavin T improves its binding affinity to Abeta amyloid by up to 70 fold, while not sacrificing the specificity and the "light-up" feature upon amyloid binding.

Two patients with muscle weakness caused by amyloid myopathy are described. Characteristic features such as pseudohypertrophy and abnormal firmness, and tumours of muscles were absent. It is suggested that muscle weakness in amyloid myopathy is caused by layers of amyloid covering muscle fibres. In middle aged or elderly patients with proximal muscle weakness the diagnosis of amyloid myopathy s...

Systemic light chain amyloidosis is a lethal disease characterized by excess immunoglobulin light chains and light chain fragments composed of variable domains, which aggregate into amyloid fibers. These fibers accumulate and damage organs. Some light chains induce formation of amyloid fibers, whereas others do not, making it unclear what distinguishes amyloid formers from non-formers. One mech...