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Characteristics and expression of binding sites specific for ferritin H-chain on human cell lines.

Authors
  • Fargion, S
  • Arosio, P
  • Fracanzani, A L
  • Cislaghi, V
  • Levi, S
  • Cozzi, A
  • Piperno, A
  • Fiorelli, G
Type
Published Article
Journal
Blood
Publication Date
Mar 01, 1988
Volume
71
Issue
3
Pages
753–757
Identifiers
PMID: 3422830
Source
Medline
License
Unknown

Abstract

Purified recombinant human ferritin composed solely of H subunit was radiolabeled and incubated with proerythroleukemic K562 human cells. A specific binding was detected, and it could be displaced only by ferritins, natural or recombinant, containing large proportion of the H subunit. The specific ferritin H-chain binding was saturable, and cells showed 17,000 to 23,000 binding sites per cell. The affinity constant measured at 37 degrees C was of 3 x 10(8) M-1. Treatment with pronase eliminated the specific binding. The binding sites were expressed in a high number during the cellular exponential phase of growth and progressively decreased to disappear when cells reached the plateau phase. Treatment of the cells with desferrioxamine increased recombinant H-ferritin binding, while iron had little effect. K562 cells induced to differentiate by hemin failed to bind ferritin H. Ferritin H-chain binding capacity is present on various cell lines such as HL60, lung cancer, and hepatoma cells. Analysis of the binding sites by western blotting showed a peptide with apparent mol wt of about 100 kd.

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