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Intracellular iron-binding macromolecules in HeLa cells.

E Robbins, J Fant, W Norton

Proceedings of the National Academy of Sciences of the United States of America

|December 1, 1972

Summary

Iron chelators inhibit both iron entry and DNA synthesis in HeLa cells. Intracellular iron is bound to polysaccharides in the cytoplasm and proteins in the nucleus, suggesting iron

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Area of Science:

Cell Biology
Biochemistry
Molecular Biology

Background:

Iron is essential for cellular processes, including DNA synthesis.
The precise mechanisms of intracellular iron binding and its role in DNA synthesis are not fully understood.
Desferrioxamine (Desferal) is an iron-chelating agent used to treat iron overload.

Purpose of the Study:

To investigate the relationship between iron uptake, DNA synthesis, and intracellular iron binding sites in HeLa cells.
To characterize the nature of iron binding in different cellular compartments (cytoplasm, nucleolus, nucleus).

Main Methods:

HeLa cells were treated with varying concentrations of desferrioxamine (Desferal).
Iron uptake and DNA synthesis were measured.
Intracellular iron-binding components were analyzed using ultracentrifugation and polyacrylamide gel electrophoresis (PAGE) under different sodium dodecyl sulfate (SDS) conditions.

Main Results:

The concentration of Desferal inhibiting iron entry also inhibited DNA synthesis.
Cytoplasmic iron is primarily bound to a glucose-containing polysaccharide sedimenting at 32 S.
Nucleolar iron is bound to a single protein, unaffected by SDS concentration.
Non-nucleolar nuclear iron exhibits heterogeneous binding to proteins, influenced by SDS concentration.

Conclusions:

Iron uptake is critical for DNA synthesis in HeLa cells.
Intracellular iron is compartmentalized and bound to distinct molecules (polysaccharides and proteins) in different cellular locations.
Nuclear iron binding involves proteins, potentially through intermediate molecules, suggesting a role in DNA-related processes.

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