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Nanogold-Labeled Amyloid β Protein Targets 20s Proteasome
Published online by Cambridge University Press: 02 July 2020
Extract
Proteasomes are multicatalytic structures found in cells that play a major role in the proteolytic degradation of proteins. Before entering the proteasome, proteins are marked like trees to be cut by attachment of ubiquitin. Neurodegenerative disorders of aging, including Alzheimer's, show abnormal accumulation of plaques and neurofibrillary tangles (NT). The latter are composed of paired helical filaments containing ubiquitinated tau protein. The fact that ubiquitinated tau is not degraded by the proteasomes may be a key to the formation of NT. Proteasomes, like other cellular pathways, are controlled by various mechanisms. It was found that amyloid β protein (Aβ) inhibits chymotrypsin-like proteasomal activity. Additionally, Aβ was found in elevated quantity in NTs in Alzheimer's diseased brain tissue. Understanding the mechanism of action of Aβ therefore becomes important.
In order to track the regulatory Aβ protein (Aβ1-40), a variant was synthesized with a terminal cysteine (Aβ1-40C40) that could be gold labeled.
- Type
- Application of Novel Microscopic Approaches to Cellular Damage and Response
- Information
- Microscopy and Microanalysis , Volume 3 , Issue S2: Proceedings: Microscopy & Microanalysis '97, Microscopy Society of America 55th Annual Meeting, Microbeam Analysis Society 31st Annual Meeting, Histochemical Society 48th Annual Meeting, Cleveland, Ohio, August 10-14, 1997 , August 1997 , pp. 45 - 46
- Copyright
- Copyright © Microscopy Society of America 1997