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Titolo:
Transferrin receptor is necessary for development of erythrocytes and the nervous system
Autore:
Levy, JE; Jin, O; Fujiwara, Y; Kuo, F; Andrews, NC;
Indirizzi:
Childrens Hosp, Div Hematol Oncol, Boston, MA 02115 USA Childrens Hosp Boston MA USA 02115 iv Hematol Oncol, Boston, MA 02115 USA Brigham & Womens Hosp, Howard Hughes Med Inst, Boston, MA 02115 USA Brigham & Womens Hosp Boston MA USA 02115 Med Inst, Boston, MA 02115 USA Brigham & Womens Hosp, Div Hematol, Boston, MA 02115 USA Brigham & Womens Hosp Boston MA USA 02115 v Hematol, Boston, MA 02115 USA Brigham & Womens Hosp, Dept Pathol, Boston, MA 02115 USA Brigham & Womens Hosp Boston MA USA 02115 pt Pathol, Boston, MA 02115 USA Harvard Univ, Sch Med, Dept Med, Boston, MA 02115 USA Harvard Univ BostonMA USA 02115 Sch Med, Dept Med, Boston, MA 02115 USA Harvard Univ, Sch Med, Dept Pediat, Boston, MA 02115 USA Harvard Univ Boston MA USA 02115 h Med, Dept Pediat, Boston, MA 02115 USA
Titolo Testata:
NATURE GENETICS
fascicolo: 4, volume: 21, anno: 1999,
pagine: 396 - 399
SICI:
1061-4036(199904)21:4<396:TRINFD>2.0.ZU;2-O
Fonte:
ISI
Lingua:
ENG
Soggetto:
IRON UPTAKE; MOUSE; CELLS; MICE; ATRANSFERRINEMIA; HEMOCHROMATOSIS; PRECURSORS; LACKING; DEFECT; GENE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
21
Recensione:
Indirizzi per estratti:
Indirizzo: Andrews, NC Childrens Hosp, Div Hematol Oncol, Boston, MA 02115 USA Childrens Hosp Boston MA USA 02115 ncol, Boston, MA 02115 USA
Citazione:
J.E. Levy et al., "Transferrin receptor is necessary for development of erythrocytes and the nervous system", NAT GENET, 21(4), 1999, pp. 396-399

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 metaltransporter 1 (DMT1, formerly Nramp2), a transmembrane iron transporter that functions only at low pH (ref. 1). 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 (refs 2,3). 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(3,4). 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.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 21/09/20 alle ore 05:20:45