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Functional Properties of the Human Copper‐Transporting ATPase ATP7B (the Wilson's Disease Protein) and Regulation by Metallochaperone Atox1
Author(s) -
LUTSENKO SVETLANA,
TSIVKOVSKII RUSLAN,
WALKER JOEL M.
Publication year - 2003
Publication title -
annals of the new york academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.712
H-Index - 248
eISSN - 1749-6632
pISSN - 0077-8923
DOI - 10.1111/j.1749-6632.2003.tb07161.x
Subject(s) - copper , intracellular , atpase , cytosol , chemistry , atp7a , enzyme , microbiology and biotechnology , menkes disease , transport protein , biochemistry , copper metabolism , biology , organic chemistry
A bstract : Wilson's disease protein (WNDP) is a copper‐transporting P 1 ‐type ATPase which plays a key role in normal distribution of copper in a number of tissues, particularly in the liver and the brain. Copper has numerous effects on WNDP, altering its structure, activity, and intracellular localization. To better understand the function of this copper‐transporting ATPase and its regulation by copper, we have recently developed the functional expression systems for WNDP and for Atox1, a cytosolic protein that serves as an intracellular donor of copper for WNDP. Here we summarize the results of our experiments on characterization of the enzymatic properties of WNDP and the effects of Atox1 on the WNDP activity.