Upon incubation of peripheral leucocytes with
copper sulphate a dramatic cellular
copper uptake reaching levels of 25-50-fold compared to that of the natural
copper content was measured. The orange-red fluorescence of the
copper-treated white blood cells was assigned to the formation of
Cu(I)-thiolate clusters in
Cu(I)-thionein. A
protein of 6-8 kDa was isolated from homogenized bovine leucocytes and characterized by its electronic absorption and
amino acid composition to be identical to the above
Cu(I)-thionein. More than 70% of the intracellular
copper was attributed to this
protein in its monomeric and polymeric form.
Cu-thionein formation was more pronounced in monocytes than in granulocytes. As most intriguing phenomenon, the release of this
Cu-thionein from leucocytes, was also noticed. The occurrence of
Cu-thionein in leucocytes and the excretion of the intact
Cu(I)-thiolate protein is of considerable interest with respect to the observed elevated
copper levels in white blood cells and plasma during
tumor malignancies and inflammatory processes.