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Copper-thionein in leucocytes.

H J Hartmann1, T Schechinger, U Weser

  • 1Anorganische Biochemie, Physiologisch-Chemisches Institut, Universität Tübingen, Federal Republic of Germany.

Biology of Metals
|January 1, 1989
PubMed
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White blood cells rapidly absorb copper, forming Cu(I)-thionein, a protein that binds over 70% of intracellular copper. This protein is released from leucocytes, potentially explaining elevated copper levels in disease.

Area of Science:

  • Biochemistry
  • Cell Biology
  • Toxicology

Background:

  • Leukocytes play a role in copper homeostasis.
  • Elevated copper levels are observed in white blood cells and plasma during certain diseases.

Purpose of the Study:

  • To investigate copper uptake and binding in peripheral leukocytes.
  • To identify and characterize copper-binding proteins in leukocytes.
  • To explore the release of copper-binding proteins from leukocytes.

Main Methods:

  • Incubation of peripheral leukocytes with copper sulfate.
  • Spectroscopic analysis (fluorescence, electronic absorption) to detect copper.
  • Protein isolation and characterization (molecular weight, amino acid composition).
  • Differential analysis of copper-thionein formation in monocytes and granulocytes.

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Main Results:

  • Leukocytes exhibited a 25-50 fold increase in cellular copper uptake.
  • Copper uptake led to the formation of orange-red fluorescence, indicative of Cu(I)-thiolate clusters in Cu(I)-thionein.
  • A 6-8 kDa protein identical to Cu(I)-thionein was isolated from bovine leukocytes.
  • Cu(I)-thionein accounted for over 70% of intracellular copper, with higher formation in monocytes.
  • The release of intact Cu(I)-thionein from leukocytes was observed.

Conclusions:

  • Leukocytes actively accumulate copper, primarily binding it to Cu(I)-thionein.
  • Cu(I)-thionein formation and release from leukocytes may contribute to altered copper levels in disease states.
  • The findings suggest a novel mechanism for copper transport and regulation involving leukocytes.