Published May 2018
| Version v1
Journal article
Copper induces structural changes in N-terminus of human prion protein
Creators
- 1. Department of Physiology, Pre-Clinical College, Guangxi Medical University, Nanning, Guangxi 530021 (China)
- 2. Department of Neurology, University of Chicago, Chicago, IL 60637 (United States)
Description
Highlights: • Copper binding to 4 histidine (H) residues in octarepeats and 1 histidine in non-octarepeats in N-terminus induces. • Proteinase K resistant. • Structural changes. Copper ions reportedly bind to the cellular prion (PrPC) and induce PrP proteinase K (PK) resistant from (PrPres). PrPC also plays a role in response to oxidative stress. By using purified human PrP23-98 containing octarepeats, we have found that Cu(II) induces PrPres determined by Western blots and atomic force microscopy, and structural changes detected by hydrogen/deuterium exchange in the PrP N-terminus. Therefore, we have provided the evidence that copper ions play an important role in the change of N-terminus of human prion protein.
Availability note (English)
Available from http://dx.doi.org/10.1016/j.bbrc.2018.03.171Additional details
Identifiers
- DOI
- 10.1016/j.bbrc.2018.03.171;
- PII
- S0006291X18306910;
Publishing Information
- Journal Title
- Biochemical and Biophysical Research Communications
- Journal Volume
- 499
- Journal Issue
- 3
- Journal Page Range
- p. 470-474
- ISSN
- 0006-291X
- CODEN
- BBRCA9
INIS
- Country of Publication
- United States
- Country of Input or Organization
- International Atomic Energy Agency (IAEA)
- INIS RN
- 54056436
- Subject category
- S60: APPLIED LIFE SCIENCES;
- Descriptors DEI
- COPPER IONS; HISTIDINE; HUMANS; PROTEINS
- Descriptors DEC
- AMINO ACIDS; ANIMALS; AZOLES; CARBOXYLIC ACIDS; CHARGED PARTICLES; HETEROCYCLIC ACIDS; HETEROCYCLIC COMPOUNDS; IMIDAZOLES; IONS; MAMMALS; ORGANIC ACIDS; ORGANIC COMPOUNDS; ORGANIC NITROGEN COMPOUNDS; PRIMATES; VERTEBRATES
Optional Information
- Copyright
- Copyright (c) 2018 Published by Elsevier Inc.