Characteristics and expression of binding site for ferritin H-chain on human cell lines

S. Fargion, P. Arosio, A. L. Fracanzani, V. Cislaghi, S. Levi, A. Cozzi, A. Piperno, G. Fiorelli

Research output: Contribution to journalArticlepeer-review

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°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.

Original languageEnglish
Pages (from-to)753-757
Number of pages5
JournalBlood
Volume71
Issue number3
Publication statusPublished - 1988

ASJC Scopus subject areas

  • Hematology

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