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Am J Physiol Gastrointest Liver Physiol 271: G741-G746, 1996;
0193-1857/96 $5.00
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AJP - Gastrointestinal and Liver Physiology, Vol 271, Issue 5 741-G746, Copyright © 1996 by American Physiological Society

ARTICLES

ATP-dependent copper transporter, in the Golgi apparatus of rat hepatocytes, transports Cu(II) not Cu(I)

M. J. Bingham, T. J. Ong, W. J. Ingledew and H. J. McArdle
Department of Child Health, Ninewells Hospital and Medical School, University of Dundee, United Kingdom.

The Wilson disease adenosinetriphosphatase (ATPase; ATP7B) is believed to bind copper as Cu(I). We provide evidence to suggest that the ATPase actually transports Cu as Cu(II). When the copper is presented to rat liver microsomes as Cu(I), virtually all uptake is ATP independent. If the copper is presented as copper oxalate [Cu(II)], total uptake is reduced to approximately 10% of Cu(I) levels, but ATP-dependent uptake rises, both as a proportion of total uptake and in absolute terms. The reducing agent vitamin C and the Cu(I) chelator bathocuproine both override the effect of oxalate. The data indicate that there are two transporters in the microsomes, an ATP-independent Cu(I) transporter and an ATP-dependent Cu(II) pump. The activity of the Cu(I) transporter correlates most strongly with alkaline phosphatase, suggesting that it is derived from plasma membrane contamination. Cu(II) ATP-dependent transport correlates only with beta-1, 4-galactosyltransferase, which indicates that it is located in the Golgi apparatus.


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J. R. Forbes, G. Hsi, and D. W. Cox
Role of the Copper-binding Domain in the Copper Transport Function of ATP7B, the P-type ATPase Defective in Wilson Disease
J. Biol. Chem., April 30, 1999; 274(18): 12408 - 12413.
[Abstract] [Full Text] [PDF]


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