Amyloidogenic metal-binding proteins: new investigative pathways.

TY - JOUR

T1 - Amyloidogenic metal-binding proteins

T2 - new investigative pathways.

AU - Davies, Paul

AU - Fontaine, Sarah N.

AU - Moualla, Dima

AU - Wang, Xiaoyan

AU - Wright, Josephine A.

AU - Brown, David R.

PY - 2008/12

Y1 - 2008/12

N2 - Neurodegenerative diseases remain perplexing and problematic for modern research. Those associated with amyloidogenic proteins have often been lumped together simply because those proteins aggregate. However, research has identified a more logical reason to group some of these diseases together. The associated proteins not only aggregate, but also bind copper. The APP (amyloid precursor protein) binds copper in an N-terminal region. Binding of copper has been suggested to influence generation of β-amyloid from the protein. PrP (prion protein) binds copper, and this appears to be necessary for its normal function and might also reduce its probability of conversion into an infectious prion. α-Synuclein, a protein associated with Parkinson's disease, also binds copper, but, in this case, it potentially increases the rate at which the protein aggregates. The similarities between these proteins, in terms of metal binding, has allowed us to investigate them using similar approaches. In the present review, we discuss some of these approaches.

AB - Neurodegenerative diseases remain perplexing and problematic for modern research. Those associated with amyloidogenic proteins have often been lumped together simply because those proteins aggregate. However, research has identified a more logical reason to group some of these diseases together. The associated proteins not only aggregate, but also bind copper. The APP (amyloid precursor protein) binds copper in an N-terminal region. Binding of copper has been suggested to influence generation of β-amyloid from the protein. PrP (prion protein) binds copper, and this appears to be necessary for its normal function and might also reduce its probability of conversion into an infectious prion. α-Synuclein, a protein associated with Parkinson's disease, also binds copper, but, in this case, it potentially increases the rate at which the protein aggregates. The similarities between these proteins, in terms of metal binding, has allowed us to investigate them using similar approaches. In the present review, we discuss some of these approaches.

KW - Alzheimer's disease

KW - Amyloid precursor protein

KW - Neurodegeneration

KW - Parkinson's disease

KW - Prion

KW - synuclein

KW - Transmissible spongiform encephalopathy

UR - http://europepmc.org/abstract/med/19021544

U2 - 10.1042/bst0361299

DO - 10.1042/bst0361299

M3 - Conference article

C2 - 19021544

SN - 0300-5127

VL - 36

SP - 1299

EP - 1303

JO - Biochemical Society Transactions

JF - Biochemical Society Transactions

IS - 6

ER -