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Histidine-stimulated divalent metal uptake in human erythrocytes and in the erythroleukaemic cell line HEL.92.1.7

Record type: Article

The uptake of Zn-65 by human erythrocytes was investigated in the presence of high (40 mm) and low (5 mm) concentrations of histidine and 0-500 muM cobalt, nickel, manganese and zinc. Varying concentrations of metal mono- and bis-histidine complexes will be formed and the inhibition of Zn-65 uptake could be correlated with the calculated complex concentrations to investigate competition between metals. For each metal, the calculated concentrations of bis-histidine complex giving 50% inhibition of Zn-65 uptake were similar at both 5 mm and 40 mm histidine. Manganese-bis-histidine appeared to have a much higher affinity for the binding site than the other metal-bis-histidine complexes, which had similar affinities to each other. Studies of the inhibition of histidine-stimulated Mn-54 uptake by the addition of manganese confirmed that manganese-bis-histidine does act as a substrate for the transporter in a similar fashion to the other metals studied. In addition, human erythroleukaemic cells (HEL cells) were used as a model for erythroid precursor cells. L-histidine, but not D-histidine, stimulated Zn-65 uptake in a saturable fashion. The other metals competed with zinc in a similar manner to that seen in erythrocytes, and the affinity for manganese-bis-histidine was much greater than for the bis-histidine complexes of the other three metals. Both the capacity for metal transport per cell, and the affinity of the transporter for the metal-bis-histidine complexes, were much greater in the HEL cells than in the erythrocyte. It is suggested that histidine-stimulated metal transport may play a role in the supply of metals to maturing erythroid cells.

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Citation

Oakley, F., Horn, N.M. and Thomas, A.L. (2004) Histidine-stimulated divalent metal uptake in human erythrocytes and in the erythroleukaemic cell line HEL.92.1.7 The Journal of Physiology, 561, (561), pp. 525-534. (doi:10.1113/jphysiol.2004.072389).

More information

Submitted date: 22 July 2004
Published date: 14 October 2004
Organisations: Biological Sciences

Identifiers

Local EPrints ID: 55739
URI: http://eprints.soton.ac.uk/id/eprint/55739
ISSN: 0022-3751
PURE UUID: 6ddd9a67-75d3-42d6-8548-50b08d6b82b9

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Date deposited: 05 Aug 2008
Last modified: 17 Jul 2017 14:32

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Contributors

Author: F. Oakley
Author: N.M. Horn
Author: A.L. Thomas

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