Biochemical characterization of the human copper transporter Ctr1.

Published

Journal Article

The trace metal copper is an essential cofactor for a number of biological processes including mitochondrial oxidative phosphorylation, free radical detoxification, neurotransmitter synthesis and maturation, and iron metabolism. Consequently, copper transport at the cell surface and the delivery of copper to intracellular proteins are critical events in normal physiology. Little is known about the molecules and biochemical mechanisms responsible for copper uptake at the plasma membrane in mammals. Here, we demonstrate that human Ctr1 (hCtr1) is a component of the copper transport machinery at the plasma membrane. hCtr1 transports copper with high affinity in a time-dependent and saturable manner and is metal-specific. hCtr1-mediated (64)Cu transport is an energy-independent process and is stimulated by extracellular acidic pH and high K(+) concentrations. hCtr1 exists as a homomultimer at the plasma membrane in mammalian cells. This is the first report on the biochemical characterization of the human copper transporter hCtr1, which is important for understanding mechanisms for mammalian copper transport at the plasma membrane.

Full Text

Duke Authors

Cited Authors

  • Lee, J; Peña, MMO; Nose, Y; Thiele, DJ

Published Date

  • February 8, 2002

Published In

Volume / Issue

  • 277 / 6

Start / End Page

  • 4380 - 4387

PubMed ID

  • 11734551

Pubmed Central ID

  • 11734551

International Standard Serial Number (ISSN)

  • 0021-9258

Digital Object Identifier (DOI)

  • 10.1074/jbc.M104728200

Language

  • eng

Conference Location

  • United States