Mislocalisation of hephaestin, a multicopper ferroxidase involved in basolateral intestinal iron transport, in the sex linked anaemia mouse

Background: Hephaestin is a multicopper ferroxidase required for basolateral transport of iron from enterocytes. Sex linked anaemia (sla) mice have a defect in the release of iron from intestinal enterocytes into the circulation due to an interstitial deletion in the hephaestin gene (heph). Results:...

Full description

Saved in:
Bibliographic Details
Published in:Gut 2004-02, Vol.53 (2), p.201-206
Main Authors: Kuo, Y M, Su, T, Chen, H, Attieh, Z, Syed, B A, McKie, A T, Anderson, G J, Gitschier, J, Vulpe, C D
Format: Article
Language:English
Subjects:
3′-diaminobenzidine
Amino acids
anaemia
Anemia, Iron-Deficiency - genetics
Anemia, Iron-Deficiency - metabolism
Animals
Base Sequence
Binding sites
Biological and medical sciences
Biological Transport
Cell Membrane - chemistry
Cells, Cultured
ceruloplasmin
Copper
DAB
Duodenum
Endoplasmic reticulum
Enterocytes - chemistry
Errors of metabolism
haemochromatosis
hephaestin
Homeostasis
Humans
Intestinal Mucosa - chemistry
Intestine
Intracellular Fluid - chemistry
iron
Iron - metabolism
Laboratories
Localization
Mammals
Medical sciences
Membrane Proteins - analysis
Membrane Proteins - genetics
Metabolic diseases
Mice
Mice, Inbred C57BL
Mice, Inbred Strains
Miscellaneous hereditary metabolic disorders
Molecular Sequence Data
Peptides
Plasma
Proteins
Rodents
sex linked anaemia
sla
Studies
Tfr
transferrin receptor
Citations: Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Background: Hephaestin is a multicopper ferroxidase required for basolateral transport of iron from enterocytes. Sex linked anaemia (sla) mice have a defect in the release of iron from intestinal enterocytes into the circulation due to an interstitial deletion in the hephaestin gene (heph). Results: We have demonstrated that hephaestin is primarily localised to a supranuclear compartment in both intestinal enterocytes and in cultured cells. In normal intestinal enterocytes, hephaestin was also present on the basolateral surface. In sla mice, hephaestin was present only in the supranuclear compartment. In contrast, the iron permease Ireg1 localised to the basolateral membrane in both control and sla mice. Conclusion: We suggest that mislocalisation of hephaestin likely contributes to the functional defect in sla intestinal epithelium.
ISSN:0017-5749
1468-3288
1458-3288
DOI:10.1136/gut.2003.019026