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Copper transport: Insights into a ceruloplasmin-based delivery system

Journal Article · · Advances in Experimental Medicine and Biology; (USA)
;  [1]
  1. Texas A M Univ., College Station (USA)
Ceruloplasmin binds to the membranes of K562 cells. The binding has been shown to result in a temperature-dependent transfer of ceruloplasmin-bound copper into the cytosol. Ascorbic acid (100 microM) stimulates the transmembrane transfer nearly 10-fold, depending on the initial concentration of {sup 67}Cu-ceruloplasmin. The protein moiety of ceruloplasmin does not enter the cells. Bathocuproine disulfonate, a chelator specific for cuprous copper, inhibits the uptake, suggesting copper atoms are reduced concomitant with their removal from ceruloplasmin. Cytosolic {sup 67}Cu from ceruloplasmin was found mainly bound to Cu, Zn superoxide dismutase, the major cytosolic copper protein in these cells. Evidence supporting the various phases in the ceruloplasmin-mediated transport mechanism are presented.
OSTI ID:
6855229
Journal Information:
Advances in Experimental Medicine and Biology; (USA), Journal Name: Advances in Experimental Medicine and Biology; (USA) Vol. 258; ISSN 0065-2598; ISSN AEMBA
Country of Publication:
United States
Language:
English

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