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How Mammalian Cells Acquire Copper: An Essential but Potentially Toxic Metal. | LitMetric

How Mammalian Cells Acquire Copper: An Essential but Potentially Toxic Metal.

Biophys J

Department of Biochemistry and Molecular Genetics, University of Illinois College of Medicine, Chicago, Illinois.

Published: January 2016

AI Article Synopsis

  • * The body's copper content is low, and improper function of copper-related proteins can lead to several diseases; the uptake of copper into cells is a vital first step in maintaining homeostasis.
  • * This review highlights hCTR1, the primary protein responsible for transporting copper into cells, discussing its function, the challenges in understanding its structure, and its role in regulating copper levels to prevent toxicity.

Article Abstract

Cu is an essential micronutrient, and its role in an array of critical physiological processes is receiving increasing attention. Among these are wound healing, angiogenesis, protection against reactive oxygen species, neurotransmitter synthesis, modulation of normal cell and tumor growth, and many others. Free Cu is absent inside cells, and a network of proteins has evolved to deliver this essential, but potentially toxic, metal ion to its intracellular target sites following uptake. Although the total body content is low (∼100 mg), dysfunction of proteins involved in Cu homeostasis results in several well-characterized human disease states. The initial step in cellular Cu handling is its transport across the plasma membrane, a subject of study for only about the last 25 years. This review focuses on the initial step in Cu homeostasis, the properties of the major protein, hCTR1, that mediates Cu uptake, and the status of our understanding of this highly specialized transport system. Although a high-resolution structure of the protein is still lacking, an array of biochemical and biophysical studies have provided a picture of how hCTR1 mediates Cu(I) transport and how Cu is delivered to the proteins in the intracellular milieu. Recent studies provide evidence that the transporter also plays a key protective role in the regulation of cellular Cu via regulatory endocytosis, lowering its surface expression, in response to elevated Cu loads.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4805867PMC
http://dx.doi.org/10.1016/j.bpj.2015.11.025DOI Listing

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