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Cellular copper transport and metabolism.

¹Department of Biochemistry and Biophysics and the Faculty of Nutrition, Texas A&M University, College Station, Texas 77843-2128, USA. eharris@tamu.edu

Annual Review of Nutrition

|August 15, 2000

Summary

Cellular copper (Cu) transport and metabolism rely on membrane proteins and peptides for homeostasis. This system regulates Cu influx, intracellular transport, and expulsion, involving ATPases and copper chaperones.

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Area of Science:

Cellular Biology
Biochemistry
Molecular Medicine

Background:

Cellular copper (Cu) homeostasis is crucial for normal physiological function.
Disruptions in Cu transport and metabolism are linked to genetic disorders like Menkes and Wilson diseases.

Purpose of the Study:

To elucidate the integrated system of membrane proteins and peptides involved in cellular copper transport and metabolism.
To describe the roles of specific proteins, including ATP7A, ATP7B, and copper chaperones, in maintaining copper balance.

Main Methods:

Analysis of integral membrane proteins responsible for copper ion selection and transport across the plasma membrane.
Investigation of the function of copper-transporting ATPase enzymes (ATP7A and ATP7B) in copper trafficking.
Examination of the interaction between copper chaperones and ATPases for copper incorporation into enzymes or cellular expulsion.

Main Results:

Integral membrane proteins facilitate selective copper ion entry into cells.
ATP7A and ATP7B ATPases actively transport copper intracellularly or expel it from the cell.
Copper chaperones interact with ATPases to deliver copper to enzymes or facilitate its incorporation into metalloproteins.

Conclusions:

A coordinated system of membrane proteins, ATPases, and copper chaperones maintains cellular copper homeostasis.
This integrated system responds to varying copper levels, ensuring proper cellular function and preventing toxicity.

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