ArticleThe Biochemical journal2003
The haemochromatosis protein HFE induces an apparent iron-deficient phenotype in H1299 cells that is not corrected by co-expression of beta 2-microglobulin.
Article in The Biochemical journal, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 28 citations in OpenAlex.
- Genetic and Dietary Iron Overload Differentially Affect the Course ofFrontiers in cellular and infection microbiology · 2017Article
- The role of hepatic transferrin receptor 2 in the regulation of iron homeostasis in the body.Frontiers in pharmacology · 2014Review
- A computational model of liver iron metabolism.PLoS computational biology · 2013Article
- Impact of hemochromatosis gene (HFE) mutations on epithelial ovarian cancer risk and prognosis.International journal of cancer · 2011Article
- Function of the hemochromatosis protein HFE: Lessons from animal models.World journal of gastroenterology · 2008Article
- Hepatic macrophage iron aggravates experimental alcoholic steatohepatitis.American journal of physiology. Gastrointestinal and liver physiology · 2008Article
- Iron overload in adult Hfe-deficient mice independent of changes in the steady-state expression of the duodenal iron transporters DMT1 and Ireg1/ferroportin.Journal of molecular medicine (Berlin, Germany) · 2004Article
- Contribution of the H63D mutation in HFE to murine hereditary hemochromatosis.Proceedings of the National Academy of Sciences of the United States of America · 2003Article
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3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
HFE, an atypical MHC class I type molecule, has a critical, yet still elusive function in the regulation of systemic iron metabolism. HFE mutations are linked to hereditary haemochromatosis type 1, a common autosomal recessive disorder of iron overload. Most patients are homozygous for a C282Y point mutation that abrogates the interaction of HFE with beta(2)-microglobulin (beta(2)M) and, thus, impairs its proper processing and expression on the cell surface. An H63D substitution is also associated with disease. To investigate the function of HFE we have generated clones of human H1299 lung cancer cells that express wild-type, C282Y or H63D HFE under the control of a tetracycline-inducible promoter. Consistent with earlier observations in other cell lines, the expression of wild-type or H63D, but not C282Y, HFE induces an apparent iron-deficient phenotype, manifested in the activation of iron-regulatory protein and concomitant increase in transferrin receptor levels and decrease in ferritin content. This phenotype persists in cells expressing wild-type HFE after transfection with a beta(2)M cDNA. Whereas endogenous beta(2)M is sufficient for the presentation of at least a fraction of chimeric HFE on the cell surface, this effect is stimulated by approx. 2.8-fold in beta(2)M transfectants. The co-expression of exogenous beta(2)M does not significantly affect the half-life of HFE. These results suggest that the apparent iron-deficient phenotype elicited by HFE is not linked to beta(2)M insufficiency.
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