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Tetrapyrroles pp 184-207 | Cite as

Novel Heme-Protein Interactions— Some More Radical Than Others

  • Ann Smith
Part of the Molecular Biology Intelligence Unit book series (MBIU)

Abstract

Heme (iron-protoporphyrin IX), as well as being an essential cofactor for cytochromes, oxidases and oxygen-binding proteins, is an important biological regulator acting via noncovalent, reversible interactions with a variety of proteins. These include DNA-binding transcription factors (e.g., Bach 1, NPAS2 and Fur), and the cytoprotective, calcium-sensitive, K+ Slol channel. The biological processes affected by heme may be as complex as the control of certain types of memory and the regulation of circadian rhythms. Heme contributes to the control of global iron homeostasis in mammals because heme catabolism generates iron, and heme and iron metabolism merge within the enterocyte after dietary heme uptake. Novel low-spin interactions of heme with proteins (e.g., hemopexin) protect cells from heme-mediated oxidative stress. Receptor-mediated uptake of heme from hemopexin regulates gene expression (e.g., heme oxygenase) and ligand binding to the hemopexin receptor activates a signaling network of three pathways. The acceptance of control of heme synthesis with degradation thus stringently regulating heme levels has been called into question with recent proposals that heme transporters (e.g., ABCG2 and FLVCR) function to limit intracellular heme toxicity in stem cells and that heme deficiency states develop that contribute to neurodegeneration. How, and whether, the balance of regulatory heme-protein interactions is controlled by moving heme via transporters through cell compartments as well as its uptake and export across the plasma membrane will soon be apparent.

Keywords

Heme Oxygenase Erythroid Cell Heme Binding Heme Synthesis Feline Leukemia Virus 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Landes Bioscience and Springer Science+Business Media 2009

Authors and Affiliations

  1. 1.School of Biological SciencesUniversity of Missouri at Kansas CityKansas CityUSA

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