Copper brain homeostasis: Role of amyloid precursor protein and prion protein

Nibaldo C. Inestrosa; Waldo Cerpa; Lorena Varela-Nallar

doi:10.1080/15216540500264620

Copper brain homeostasis: Role of amyloid precursor protein and prion protein

Nibaldo C. Inestrosa, Waldo Cerpa, Lorena Varela-Nallar

Life Sciences School

Research output: Contribution to journal › Review article › peer-review

26 Citations (Scopus)

Abstract

The main proteins associated with Alzheimer's and prion diseases (amyloid precursor protein (APP) and prion protein (PrP_C), respectively, have binding sites for copper and it has therefore been suggested that they play a role in copper metabolism. Here, we review evidence indicating that the copper binding domains (CuBD) of APP and PrP^C are able to modulate the oxidation state of copper, and prevent neurotoxic effects and memory impairments induced by copper. Results with transgenic and other animal models have established the relation between these pathogenic proteins and copper. In particular, APP transgenic models, suggest a beneficial effect for copper in AD.

Original language	English
Pages (from-to)	645-650
Number of pages	6
Journal	IUBMB Life
Volume	57
Issue number	9
DOIs	https://doi.org/10.1080/15216540500264620
Publication status	Published - Sept 2005

Keywords

APP
Copper
Copper binding domain
Metal homeostasis
Prion protein

ASJC Scopus subject areas

Biochemistry
Molecular Biology
Genetics
Clinical Biochemistry
Cell Biology

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10.1080/15216540500264620

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abstract = "The main proteins associated with Alzheimer's and prion diseases (amyloid precursor protein (APP) and prion protein (PrPC), respectively, have binding sites for copper and it has therefore been suggested that they play a role in copper metabolism. Here, we review evidence indicating that the copper binding domains (CuBD) of APP and PrPC are able to modulate the oxidation state of copper, and prevent neurotoxic effects and memory impairments induced by copper. Results with transgenic and other animal models have established the relation between these pathogenic proteins and copper. In particular, APP transgenic models, suggest a beneficial effect for copper in AD.",

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AU - Inestrosa, Nibaldo C.

AU - Cerpa, Waldo

AU - Varela-Nallar, Lorena

PY - 2005/9

Y1 - 2005/9

N2 - The main proteins associated with Alzheimer's and prion diseases (amyloid precursor protein (APP) and prion protein (PrPC), respectively, have binding sites for copper and it has therefore been suggested that they play a role in copper metabolism. Here, we review evidence indicating that the copper binding domains (CuBD) of APP and PrPC are able to modulate the oxidation state of copper, and prevent neurotoxic effects and memory impairments induced by copper. Results with transgenic and other animal models have established the relation between these pathogenic proteins and copper. In particular, APP transgenic models, suggest a beneficial effect for copper in AD.

AB - The main proteins associated with Alzheimer's and prion diseases (amyloid precursor protein (APP) and prion protein (PrPC), respectively, have binding sites for copper and it has therefore been suggested that they play a role in copper metabolism. Here, we review evidence indicating that the copper binding domains (CuBD) of APP and PrPC are able to modulate the oxidation state of copper, and prevent neurotoxic effects and memory impairments induced by copper. Results with transgenic and other animal models have established the relation between these pathogenic proteins and copper. In particular, APP transgenic models, suggest a beneficial effect for copper in AD.

KW - APP

KW - Copper

KW - Copper binding domain

KW - Metal homeostasis

KW - Prion protein

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SN - 1521-6543

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EP - 650

JO - IUBMB Life

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ER -

Copper brain homeostasis: Role of amyloid precursor protein and prion protein

Abstract

Keywords

ASJC Scopus subject areas

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