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PMID: 3464611 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Control of heme synthesis during Friend cell differentiation: role of iron and transferrin.

Journal of cellular physiology ·Vol. 129 ·No. 2 ·1986-11-00 ·Pages 185-92

Laskey JD, Ponka P, Schulman HM

Abstract

In many types of cells the synthesis of delta-aminolevulinic acid (ALA) limits the rate of heme formation. However, results from our laboratory with reticulocytes suggest that the rate of iron uptake from transferrin (Tf), rather than ALA synthase activity, limits the rate of heme synthesis in erythroid cells. To determine whether changes occur in iron metabolism and the control of heme synthesis during erythroid cell development Friend erythroleukemia cells induced to erythroid differentiation by dimethylsulfoxide (DMSO) were studied. While added ALA stimulated heme synthesis in uninduced Friend cells (suggesting ALA synthase is limiting) it did not do so in induced cells. Therefore the possibility was investigated that, in induced cells, iron uptake from Tf limits and controls heme synthesis. Several aspects of iron metabolism were investigated using the synthetic iron chelator salicylaldehyde isonicotinoyl hydrazone (SIH). Both induced and uninduced Friend cells take up and utilize Fe for heme synthesis directly from Fe-SIH without the involvement of transferrin and transferrin receptors and to a much greater extent than from saturating levels of Fe-Tf (20 microM). Furthermore, in induced Friend cells 100 microM Fe-SIH stimulated 2-14C-glycine incorporation into heme up to 3.6-fold as compared to the incorporation observed with saturating concentrations of Fe-Tf. In contrast, Fe-SIH, even when added in high concentrations, did not stimulate heme synthesis in uninduced Friend cells but was able to do so as early as 24 to 48 h following induction. In addition, contrary to previous results with rabbit reticulocytes, Fe-SIH also stimulated globin synthesis in induced Friend cells above the level seen with saturating concentrations of transferrin. These results indicate that some step(s) in the pathway of iron from extracellular Tf to protoporphyrin, rather than the activity of ALA synthase, limits and controls the overall rate of heme and possibly hemoglobin synthesis in differentiating Friend erythroleukemia cells.

MeSH Terms
Aminolevulinic Acid/biosynthesis Animals Cell Differentiation Friend murine leukemia virus Glycine/metabolism Heme/biosynthesis Humans Iron/metabolism Leukemia, Erythroblastic, Acute/metabolism Mice Transferrin/metabolism
Chemicals
Transferrin Heme Aminolevulinic Acid Iron Glycine
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Laskey J D
Ponka P
Schulman H M
Article Info
Journal
Journal of cellular physiology
Abbr.
J Cell Physiol
ISSN
0021-9541
Published
1986-11-00
Pages
185-92
Language
English
Region
United States
NLM ID
0050222
Subset
IM
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