Human Serum Transferrin cobalt complex: Stability and cellular uptake of cobalt

Timothy Andrew Davies Smith

Research output: Contribution to journalArticle

26 Citations (Scopus)

Abstract

Transferrin (To receptor expression is up-regulated on tumour cells. The human serum iron transport protein transferrin (Tf) can bind to many metals including gallium and cobalt. Cobalt has a positron-emitting isotope with a half-life of IS h and would thus be a useful isotope for imaging purposes. This study has examined the stability of the Co-Tf in the presence of serum and albumin and the uptake of radioactive Co from Co-Tf by tumour cells. Dialysis of Co-57-Tf with serum or with apo-Tf resulted in loss of Most (CO)-C-57 from the complex. The time course of Co uptake from cells incubated with Co-Tf showed an initial rapid association with cells, then a slower rate of accumulation, that is, a similar uptake profile to that of iron. Competition and displacement experiments showed that uptake specifically occurred by interaction with Tf receptors. (c) 2005 Elsevier Ltd. All rights reserved.

Original languageEnglish
Pages (from-to)4576-4579
Number of pages3
JournalBioorganic & Medicinal Chemistry
Volume13
Issue number14
DOIs
Publication statusPublished - 2005

Keywords

  • transferrin
  • cobalt
  • tumour
  • IN-VIVO
  • BINDING
  • TRANSPORT
  • CANCER
  • CELLS
  • IRON

Cite this

Human Serum Transferrin cobalt complex: Stability and cellular uptake of cobalt. / Smith, Timothy Andrew Davies.

In: Bioorganic & Medicinal Chemistry, Vol. 13, No. 14, 2005, p. 4576-4579.

Research output: Contribution to journalArticle

Smith, Timothy Andrew Davies. / Human Serum Transferrin cobalt complex: Stability and cellular uptake of cobalt. In: Bioorganic & Medicinal Chemistry. 2005 ; Vol. 13, No. 14. pp. 4576-4579.
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