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Home > A. Molecular pathology > amyloidogenic proteins

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amyloidogenic proteins

The various protein deposits of brain amyloidosis share common ultrastructural, biophysical, and histological properties. These amyloidogenic deposits can be composed of distinct proteins, which are conceptually associated with different diseases.

Amyloidogenic proteins are typically soluble monomeric precursors, which undergo remarkable conformation changes associated with the polymerization into 8- to 10-nm wide fibrils, which culminate in the formation of amyloid aggregates.

Some amyloidogenic inclusions are extracellular, such as senile plaques of Alzheimer’s disease, which are composed of amyloid beta (Abeta) peptides.

Intracytoplasmic amyloid aggregates, such as neurofibrillary tangles in Alzheimer’s disease and Lewy bodies in Parkinson’s disease, are composed of the proteins tau and alpha-synuclein, respectively. These proteins are directly linked to the etiology of spectrum of neurodegenerative diseases, coining the terms "tauopathies" and "synucleinopathies."

References

- Giasson BI, Lee VM, Trojanowski JQ. Interactions of amyloidogenic proteins. Neuromolecular Med. 2003;4(1-2):49-58. PMID: 14528052 [PubMed - indexed for MEDLINE]

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