AJP - GI Fuel your research with LabChart
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

Am J Physiol Gastrointest Liver Physiol 258: G988-G991, 1990;
0193-1857/90 $5.00
This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by McArdle, H. J.
Right arrow Articles by Wedd, A. G.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by McArdle, H. J.
Right arrow Articles by Wedd, A. G.

AJP - Gastrointestinal and Liver Physiology, Vol 258, Issue 6 988-G991, Copyright © 1990 by American Physiological Society

ARTICLES

Role of albumin's copper binding site in copper uptake by mouse hepatocytes

H. J. McArdle, S. M. Gross, D. M. Danks and A. G. Wedd
Scobie and Claire Mackinnon Trace Element Research Group, Murdoch Institute, Royal Children's Hospital, Melbourne, Victoria, Australia.

It is possible, in vitro, to label albumin with copper either exclusively on the specific binding site or partly on the specific site and also on other sites by altering the pH at which the two ligands are mixed. Copper attached exclusively to the specific site is taken up more rapidly than copper attached to that site and others on albumin. The effect is proportional to the amount of copper on the specific site. Additional histidine stimulates uptake irrespective of the copper binding site on albumin. The effect is related to the histidine on position 3 of the albumin, since it is not seen when dog albumin is labeled under the same conditions. The data suggest that the cell recognizes and presumably binds the copper-albumin (CuAlb) complex but may preferentially recognize the ternary complex formed by CuAlb and histidine. We suggest that, in vivo, copper is bound mainly as the ternary complex and that the structure formed, presumably similar to that formed by a copper-histidine complex, is what is actually recognized by the cell. After binding, the albumin and histidine are released, possibly by a reduction step, and the copper is transported across the membrane. If the copper cannot be transported (as occurs when the cells are incubated at 4 degrees C), it blocks further binding of the ternary complex.


This article has been cited by other articles:


Home page
 Am. J. Physiol. Gastrointest. Liver Physiol.Home page
S. Ferruzza, M.-L. Scarino, G. Rotilio, M. R. Ciriolo, P. Santaroni, A. O. Muda, and Y. Sambuy
Copper treatment alters the permeability of tight junctions in cultured human intestinal Caco-2 cells
Am J Physiol Gastrointest Liver Physiol, December 1, 1999; 277(6): G1138 - G1148.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Visit Other APS Journals Online