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Archives of biochemistry and biophysics1998; 359(1); 69-76; doi: 10.1006/abbi.1998.0891

Iron loading into ferritin by an intracellular ferroxidase.

Abstract: An intracellular, membrane-bound enzyme exhibiting both p-phenylenediamine oxidase activity and ferrous iron oxidase activity was isolated with the plasma membrane fraction of horse heart and studied for its ability to load iron into ferritin. The ferroxidase activity of the tissue oxidase was stimulated approximately twofold by horse spleen apoferritin, and the iron was loaded into ferritin. The loading of iron into ferritin by the tissue oxidase was inhibited by anti-horse serum ceruloplasmin antibody. The stoichiometry of iron oxidation and oxygen consumption during iron loading into ferritin by the tissue-derived oxidase and serum ceruloplasmin were 3.6 +/- 0.2 and 3.9 +/- 0.2, respectively. These data provide evidence that an enzyme analogous to ceruloplasmin is present on the plasma membrane of horse heart and that this ferroxidase is capable of catalyzing the loading of iron into ferritin. The implications of these data on the present models for the uptake and storage of iron by cells are discussed.
Publication Date: 1998-11-04 PubMed ID: 9799562DOI: 10.1006/abbi.1998.0891Google Scholar: Lookup
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  • Journal Article
  • Research Support
  • U.S. Gov't
  • P.H.S.

Summary

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This study found an enzyme existing in horse heart tissues that enables iron to be loaded into ferritin, a protein responsible for storing iron in the body. The researchers found that this enzyme functioned similarly to ceruloplasmin, a copper-carrying protein known to have a role in iron metabolism, providing new insights into how iron is absorbed and stored in cells.

Research Purpose and Methods

The primary aim of this research was to identify and study the enzyme that facilitates the loading of iron into ferritin within a cell. The scientists identified the enzyme in the plasma membrane fraction of horse heart tissues and then conducted a series of tests, including ferroxidase activity and stoichiometry of iron oxidation and oxygen consumption during the loading of iron into ferritin.

  • The enzyme was detected for its p-phenylenediamine oxidase and ferrous iron oxidase activities.
  • Horse spleen apoferritin was used to stimulate the ferroxidase activity of the tissue oxidase, which led to the loading of iron into ferritin.
  • The study also explored the effect of the anti-horse serum ceruloplasmin antibody on the loading of iron into ferritin by the tissue oxidase.

Main Findings and Implications

This research demonstrated that there is an enzyme present in heart tissues, similar to ceruloplasmin, which aids in the loading of iron into ferritin, a crucial step in iron storage in cells.

  • The ferroxidase activity was found to be incited about twofold by horse spleen apoferritin, and this led to iron being loaded into ferritin.
  • The pace at which iron is loaded into ferritin by the enzyme was deterred by the anti-horse serum ceruloplasmin antibody.
  • Iron oxidation and oxygen consumption rates during iron loading into ferritin by the tissue-derived oxidase and serum ceruloplasmin were close to one another, indicating similar activity patterns.

These findings extend our understanding of iron uptake and storage by cells, potentially opening up new avenues to explore in iron metabolism disorders. Further research is needed to validate these findings in other tissue types and species. These findings also raise questions about the existence and function of similar enzymes in other organs involved in iron metabolism.

Cite This Article

APA
Reilly CA, Aust SD. (1998). Iron loading into ferritin by an intracellular ferroxidase. Arch Biochem Biophys, 359(1), 69-76. https://doi.org/10.1006/abbi.1998.0891

Publication

ISSN: 0003-9861
NlmUniqueID: 0372430
Country: United States
Language: English
Volume: 359
Issue: 1
Pages: 69-76

Researcher Affiliations

Reilly, C A
  • Biotechnology Center, Utah State University, Logan, Utah, 84322-4705, USA.
Aust, S D

    MeSH Terms

    • Animals
    • Apoferritins / metabolism
    • Ceruloplasmin / antagonists & inhibitors
    • Ceruloplasmin / metabolism
    • Enzyme Activation / drug effects
    • Enzyme Inhibitors / pharmacology
    • Ferritins / metabolism
    • Horses
    • Intracellular Fluid / enzymology
    • Iron / metabolism
    • Myocardium / enzymology
    • Oxidoreductases Acting on CH-NH Group Donors / antagonists & inhibitors
    • Oxidoreductases Acting on CH-NH Group Donors / metabolism
    • Spleen / enzymology
    • Spleen / metabolism

    Grant Funding

    • DK52823 / NIDDK NIH HHS
    • ES05056 / NIEHS NIH HHS

    Citations

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