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The oligomers are toxic to nerve cells. A recent study suggested that APP and its amyloid potential is of ancient origins, dating as far back as early deuterostomes.
The glymphatic system clears metabolic waste from the mammalian brain, and in particular beta amyloids. The plaques are composed of a tangle of regularly ordered fibrillar aggregates called amyloid fibers,  a protein fold shared by other peptides such as the prions associated with protein misfolding diseases.
An alternative hypothesis is that amyloid oligomers rather than plaques are responsible for the disease. Studies focusing on human breast cancer cell lines have further demonstrated that these cancerous cells display an increased level of expression of amyloid precursor protein.
Amyloid beta is commonly thought to be intrinsically unstructured , meaning that in solution it does not acquire a unique tertiary fold but rather populates a set of structures.
As such, it cannot be crystallized and most structural knowledge on amyloid beta comes from NMR and molecular dynamics. Low-temperature and low-salt conditions allowed to isolate pentameric disc-shaped oligomers devoid of beta structure.
The suggested mechanisms by which amyloid beta may damage and cause neuronal death include the generation of reactive oxygen species during the process of its self-aggregation.
When this occurs on the membrane of neurons in vitro, it causes lipid peroxidation and the generation of a toxic aldehyde called 4-hydroxynonenal which, in turn, impairs the function of ion-motive ATPases, glucose transporters and glutamate transporters.
As a result, amyloid beta promotes depolarization of the synaptic membrane, excessive calcium influx and mitochondrial impairment. To date, human testing has been avoided due to concern that it might interfere with signaling via Notch proteins and other cell surface receptors.
Imaging compounds, notably Pittsburgh compound B , 6-OH-BTA-1, a thioflavin , can selectively bind to amyloid beta in vitro and in vivo.
Amyloid beta can be measured semiquantitatively with immunostaining , which also allows one to determine location. Amyloid beta may be primarily vascular, as in cerebral amyloid angiopathy , or in senile plaques in white matter.
One sensitive method is ELISA which is an immunosorbent assay which utilizes a pair of antibodies that recognize amyloid beta. Atomic force microscopy , which can visualize nanoscale molecular surfaces, can be used to determine the aggregation state of amyloid beta in vitro.
Dual polarisation interferometry is an optical technique which can measure early stages of aggregation by measuring the molecular size and densities as the fibrils elongate.
New research has shown promise in testing whole blood samples for amyloid beta levels on the basis of electrical impedance. Interdigitated microelectrodes prepared with amyloid beta antibody measure differentiated impedance of flow in samples before and after antibody reactions to amyloid beta, comparing with normalization to account for regular variance between electrodes.
From Wikipedia, the free encyclopedia. Amyloid beta peptide beta-APP A partially folded structure of amyloid beta 1 40 in an aqueous environment pdb 2lfm .
Biochemical and Biophysical Research Communications. Applied Biochemistry and Biotechnology. Journal of Medical Hypotheses and Ideas. Biochimica et Biophysica Acta.
The Journal of Neuroscience. Frontiers in Bioscience Scholar Edition. The Mac OS you are using is no longer supported. Please upgrade to There may be a community-supported version for your distribution here.
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