Binding and suppressive activity of human recombinant ferritins on erythroid cells

Am J Hematol. 1992 Apr;39(4):264-8. doi: 10.1002/ajh.2830390406.

Abstract

We studied the relation between ferritin cellular binding and suppressive activity of recombinant H- and L-ferritin on human erythroid cells at different proliferation/differentiation phases. L-ferritin failed to show any suppressive activity or detectable binding to erythroblasts at any stage of maturation. In contrast, H-ferritin demonstrated binding to erythroblasts derived from peripheral BFU-E cells which increased steadily between 7-14 days of culture up to 15,000 molecules per cell. Reticulocytes and erythrocytes failed to bind either L- or H-ferritin. H-ferritin suppressed BFU-E colony formation and reduced K562 cell proliferation at nanomolar concentrations. This suggests that the expression of H-ferritin binding sites is modulated by cellular proliferation and differentiation, that cells expressing H-ferritin binding sites are sensitive to ferritin suppressive activity and that a causal relation exists between ferritin cellular binding and suppressive activity.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Binding Sites
  • Cell Differentiation / drug effects
  • Cell Differentiation / physiology
  • Cell Division / drug effects
  • Cell Division / physiology
  • Cells, Cultured
  • Erythrocytes / metabolism
  • Erythroid Precursor Cells / drug effects*
  • Erythroid Precursor Cells / metabolism
  • Erythroid Precursor Cells / physiology
  • Erythropoiesis / drug effects
  • Ferritins / metabolism
  • Ferritins / pharmacology*
  • Fetal Blood / cytology
  • Humans
  • Leukemia, Erythroblastic, Acute / metabolism
  • Leukemia, Erythroblastic, Acute / pathology
  • Protein Binding / drug effects
  • Recombinant Proteins / pharmacology
  • Reticulocytes / metabolism
  • Tumor Cells, Cultured / metabolism
  • Tumor Cells, Cultured / pathology

Substances

  • Recombinant Proteins
  • Ferritins