| RESEARCH |
Peptide causes iron exporter's demise Researchers have pinpointed how the peptide hormone hepcidin regulates iron uptake and distribution in the body. A team led by Jerry Kaplan of the University of Utah's School of Medicine and Tomas Ganz of the David Geffen School of Medicine at UCLA has found that the hairpin-shaped peptide controls iron levels by binding to ferroportin, an iron-exporting protein found on the surface of specific iron-containing cells [Science, published online Oct. 28, http://dx.doi.org/10. 1126/science.1104742]. Using radiolabeled hepcidin and chemical cross-linking, the team showed that binding of hepcidin to ferroportin causes the iron exporter to be internalized and degraded by the cell. Without ferroportin, iron remains trapped in the cell. The team suggests that blocking the hepcidin-ferroportin interaction might be a useful strategy for treating anemia of inflammation, a blood iron deficiency associated with too much hepcidin. They also propose that a form of hepcidin might be used to treat hemochromatosis, a common genetic disorder that causes excess iron to accumulate in body tissues. |
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