Hostname: page-component-848d4c4894-m9kch Total loading time: 0 Render date: 2024-05-21T00:51:14.755Z Has data issue: false hasContentIssue false
  • English
  • Français

Nanogold-Labeled Amyloid β Protein Targets 20s Proteasome

Published online by Cambridge University Press:  02 July 2020

James F. Hainfeld ,
Luisa Gregori ,
Martha N. Simon  and
Dmitry Goldgaber
James F. Hainfeld
Affiliation:
Biology Department, Brookhaven National Lab., Upton, NY, 11973
Luisa Gregori
Affiliation:
Biology Department, Brookhaven National Lab., Upton, NY, 11973
Martha N. Simon
Affiliation:
Biology Department, Brookhaven National Lab., Upton, NY, 11973
Dmitry Goldgaber
Affiliation:
Biology Department, Brookhaven National Lab., Upton, NY, 11973
Get access

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

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

1.Gregori, L.et al., J. Biol. Chem. 270(1995)19702.10.1074/jbc.270.34.19702CrossRefGoogle Scholar
2. Nanoprobes, 25 East Loop Rd, Ste. 124, Stony Brook, NY 11790, www.nanoprobes.com.Google Scholar
3.Gregori, L.et al., J. Biol. Chem. 272(1997)58.10.1074/jbc.272.1.58CrossRefGoogle Scholar
4.Hainfeld, J. F.et al., Proc. Ann MSA Meeting 52(1994)132.Google Scholar
5.Wenzel, T. and Baumeister, W., Nature Str. Biol. 2(1995)199.10.1038/nsb0395-199CrossRefGoogle Scholar
6.The authors would like to thank Dr. M. Figueiredo-Pereira (Mount Sinai, CUNY, New York) for providing the purified proteasomes and Dr. C. Gable (University of California, Irvine) for synthesizing the Aβi-39C40- The authors also thank B. Lin, J. Wall, and F. Kito of the BNL STEM facility. This work was supported by NIH grant RR 01777 and US Dept of Energy, OHER.Google Scholar