Copper Binding to the N-Terminal Tandem Repeat Regions of Mammalian and Avian Prion Protein

1995 ◽  
Vol 207 (2) ◽  
pp. 621-629 ◽  
Author(s):  
M.P. Hornshaw ◽  
J.R. Mcdermott ◽  
J.M. Candy
Keyword(s):  
Prion Protein ◽  
Tandem Repeat ◽  
Copper Binding

Metallic prions

2004 ◽  
Vol 71 ◽  
pp. 193-202 ◽  
Author(s):  
David R Brown
Keyword(s):  
Prion Protein ◽  
Binding Capacity ◽  
Normal Function ◽  
Transmissible Spongiform Encephalopathies ◽  
Published Data ◽  
Normal Brain ◽  
Copper Binding ◽  
Loss Of Function ◽  
Spongiform Encephalopathies ◽  
The Brain

Prion diseases, also referred to as transmissible spongiform encephalopathies, are characterized by the deposition of an abnormal isoform of the prion protein in the brain. However, this aggregated, fibrillar, amyloid protein, termed PrPSc, is an altered conformer of a normal brain glycoprotein, PrPc. Understanding the nature of the normal cellular isoform of the prion protein is considered essential to understanding the conversion process that generates PrPSc. To this end much work has focused on elucidation of the normal function and activity of PrPc. Substantial evidence supports the notion that PrPc is a copper-binding protein. In conversion to the abnormal isoform, this Cu-binding activity is lost. Instead, there are some suggestions that the protein might bind other metals such as Mn or Zn. PrPc functions currently under investigation include the possibility that the protein is involved in signal transduction, cell adhesion, Cu transport and resistance to oxidative stress. Of these possibilities, only a role in Cu transport and its action as an antioxidant take into consideration PrPc's Cu-binding capacity. There are also more published data supporting these two functions. There is strong evidence that during the course of prion disease, there is a loss of function of the prion protein. This manifests as a change in metal balance in the brain and other organs and substantial oxidative damage throughout the brain. Thus prions and metals have become tightly linked in the quest to understand the nature of transmissible spongiform encephalopathies.

scholarly journals The Prion Protein is a Combined Zinc and Copper Binding Protein:  Zn2+Alters the Distribution of Cu2+Coordination Modes

2007 ◽  
Vol 129 (50) ◽  
pp. 15440-15441 ◽  
Author(s):  
Eric D. Walter ◽  
Daniel J. Stevens ◽  
Micah P. Visconte ◽  
Glenn L. Millhauser
Keyword(s):  
Prion Protein ◽  
Binding Protein ◽  
Copper Binding ◽  
Coordination Modes ◽  
Copper Binding Protein

Copper Binding Regulates Cellular Prion Protein Function

2019 ◽  
Vol 56 (9) ◽  
pp. 6121-6133 ◽  
Author(s):  
Xuan T. A. Nguyen ◽  
Thanh Hoa Tran ◽  
Dan Cojoc ◽  
Giuseppe Legname
Keyword(s):  
Prion Protein ◽  
Protein Function ◽  
Cellular Prion Protein ◽  
Copper Binding

Trace elements and prion diseases: a review of the interactions of copper, manganese and zinc with the prion protein

2006 ◽  
Vol 7 (1-2) ◽  
pp. 97-105 ◽  
Author(s):  
Scott P. Leach ◽  
M. D. Salman ◽  
Dwayne Hamar
Keyword(s):  
Trace Elements ◽  
Prion Protein ◽  
Copper Ions ◽  
Prion Diseases ◽  
Normal Function ◽  
Transmissible Spongiform Encephalopathies ◽  
Copper Binding ◽  
Spongiform Encephalopathies ◽  
Copper Manganese ◽  
The Brain

Transmissible spongiform encephalopathies (TSEs) are a family of neurodegenerative diseases characterized by their long incubation periods, progressive neurological changes, and spongiform appearance in the brain. There is much evidence to show that TSEs are caused by an isoform of the normal cellular surface prion protein PrPC. The normal function of PrPC is still unknown, but it exhibits properties of a cupro-protein, capable of binding up to six copper ions. There are two differing views on copper's role in prion diseases. While one view looks at the PrPC copper-binding as the trigger for conversion to PrPSc, the opposing viewpoint sees a lack of PrPC copper-binding resulting in the conformational change into the disease causing isoform. Manganese and zinc have been shown to interact with PrPC as well and have been found in abnormal levels in prion diseases. This review addresses the interaction between select trace elements and the PrPC.

Antioxidant activity related to copper binding of native prion protein

2008 ◽  
Vol 76 (1) ◽  
pp. 69-76 ◽  
Author(s):  
David R. Brown ◽  
Christine Clive ◽  
Stephen J. Haswell
Keyword(s):  
Antioxidant Activity ◽  
Prion Protein ◽  
Copper Binding

The chemistry of copper binding to PrP: is there sufficient evidence to elucidate a role for copper in protein function?

2008 ◽  
Vol 410 (2) ◽  
pp. 237-244 ◽  
Author(s):  
Paul Davies ◽  
David R. Brown
Keyword(s):  
Prion Protein ◽  
Protein Function ◽  
Present Review ◽  
Sufficient Evidence ◽  
Copper Binding

There has been an enormous body of literature published in the last 10 years concerning copper and PrP (prion protein). Despite this, there is still no generally accepted role for copper in the function of PrP or any real consensus as to how and to what affinity copper associates with the protein. The present review attempts to look at all the evidence for the chemistry, co-ordination and affinity of copper binding to PrP, and then looks at what effect this has on the protein. We then connect this evidence with possible roles for PrP when bound to copper. No clear conclusions can be made from the available data, but it is clear from the present review what aspects of copper association with PrP need to be re-investigated.

Copper binding is the governing determinant of prion protein turnover

2005 ◽  
Vol 30 (2) ◽  
pp. 186-196 ◽  
Author(s):  
Cathryn L. Haigh ◽  
Kate Edwards ◽  
David R. Brown
Keyword(s):  
Prion Protein ◽  
Protein Turnover ◽  
Copper Binding
Sign in / Sign up

Export Citation Format

Share Document