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Review
. 2003 Dec;71(12):6693-700.
doi: 10.1128/IAI.71.12.6693-6700.2003.

Hepcidin: the missing link between hemochromatosis and infections

Houman Ashrafian  1
Affiliations
Review

Hepcidin: the missing link between hemochromatosis and infections

Houman Ashrafian. Infect Immun. 2003 Dec.
No abstract available

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Figures

FIG. 1.
FIG. 1.
Iron uptake mechanisms in gram-negative bacteria. Outer membrane receptor proteins (many exist and only a few are shown: FepA, TbpA/B, HemR, HpuA/B, HmbR, and HasR) bind iron-containing ligands (siderophores, lactoferrin, transferrin, heme, hemoglobin, and the S. marcescens hemophore HasA) and transport them to the periplasm. PBTs (e.g., FepB, FbpA, and HemT) then facilitate the TonB-ExbB/D-dependent transport to the ATP-driven cytoplasmic-membrane transporters (e.g., FepCDG, FbpBC, and HemUV), a process that depends on the proton motive force. Under anaerobic conditions, outer membrane porins transport soluble Fe2+ directly to the periplasm and then enter the cytoplasm via ATP-dependent FeoABC channels. (Adapted from reference with permission of the publisher.)
FIG. 2.
FIG. 2.
Diagram of the possible role of iron in hepcidin processing. As detailed in the text, although as yet experimentally undetermined, iron may modify hepcidin mRNA expression and translation, the 84-amino-acid propeptide localization and intracellular transport, the endoplasmic reticulum (ER) signal sequence cleavage, the 60-amino-acid propeptide cellular extrusion and further cleavage, and the proportions of hepcidin remnants and 35-amino-acid proregion (these elements may together or in isolation have their own functional effects). Most importantly, iron may cause a hepcidin pseudodeficiency by electrostatically competing with the cationic hepcidin to bind to pathogens, altering hepcidin aggregation, preventing pathogen lysis and opsonization, altering chemotaxis, and preventing phagocytosis or the inhibition of the respiratory burst. αα, amino acid.
See this image and copyright information in PMC

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