Transferrin receptor is necessary for development of erythrocytes and the nervous system View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1999-04

AUTHORS

Joanne E. Levy, Ou Jin, Yuko Fujiwara, Frank Kuo, Nancy Andrews

ABSTRACT

Plasma iron circulates bound to transferrin (Trf), which solubilizes the ferric ion and attenuates its reactivity. Diferric Trf interacts with cell-surface Trf receptor (Trfr) to undergo receptor-mediated endocytosis into specialized endosomes. Endosomal acidification leads to iron release, and iron is transported out of the endosome through the activity of divalent metal transporter 1 (DMT1, formerly Nramp2), a transmembrane iron transporter that functions only at low pH. Trf and Trfr then return to the cell surface for reuse, completing a highly efficient cycle. Although the Trf cycle is assumed to be the general mechanism for cellular iron uptake, this has not been validated experimentally. Mice with hypotransferrinaemia (hpx) have little or no plasma Trf. They have severe anaemia, indicating that the Trf cycle is essential for iron uptake by erythroid cells. Other hpx tissues, however, are generally normal, and there is a paradoxical increase in intestinal iron absorption and iron storage. To test the hypothesis that the Trf cycle has unique importance for erythropoiesis, we disrupted the Trfr gene in mice. This results in elimination of the Trf cycle, but leaves other Trf functions intact. Mice lacking Trfr have a more severe phenotype than hpx mice, affecting both erythropoiesis and neurologic development. Furthermore, haploinsufficiency for Trfr results in impaired erythroid development and abnormal iron homeostasis. More... »

PAGES

ng0499_396

References to SciGraph publications

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/7727

DOI

http://dx.doi.org/10.1038/7727

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1036887929

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/10192390


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