Formation and participation of nano-amyloids in pathogenesis of Alzheimer's disease and other amyloidogenic diseases
Author(s) -
Alexander V. Maltsev,
Oxana V. Galzitskaya
Publication year - 2010
Publication title -
biomeditsinskaya khimiya
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.192
H-Index - 15
eISSN - 2310-6972
pISSN - 2310-6905
DOI - 10.18097/pbmc20105606624
Subject(s) - pathogenesis , amyloid (mycology) , gene isoform , disease , pathological , fibril , alzheimer's disease , amyloid fibril , peptide , biochemistry of alzheimer's disease , protein folding , neuroscience , amyloid beta , chemistry , amyloid β , biology , medicine , microbiology and biotechnology , amyloid precursor protein , biochemistry , immunology , pathology , gene
Studies of neurodegenetrative disorders have become particularly actual attracting the attention of researchers from over the world because of the dissemination of Alzheimer's disease. The reason for such pathogenesis is the transition of a "healthy" molecule or peptide from the native conformation into a very stable "pathological" isoform. During this, molecules in the "pathological" conformation aggregate, forming amyloid fibrils that can increase without any control. Novel knowledge is required on sporadic isoforms of Alzheimer's disease, on the nature of triggering mechanisms of conformational transitions of beta-amyloid fragments from normally functioning proteins into new formations - nano-beta-amyloids - that spiral out of control of neurons and organism which leads to the loss of neurons. Herein we review studies devoted to the formation of amyloid fibrils and their role in pathogenesis of amyloid diseases.
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