Scara5 is a ferritin receptor mediating non-transferrin iron delivery.
Dev Cell
; 16(1): 35-46, 2009 Jan.
Article
de En
| MEDLINE
| ID: mdl-19154717
ABSTRACT
Developing organs require iron for a myriad of functions, but embryos deleted of the major adult transport proteins, transferrin or its receptor transferrin receptor1 (TfR1(-/-)), still initiate organogenesis, suggesting that non-transferrin pathways are important. To examine these pathways, we developed chimeras composed of fluorescence-tagged TfR1(-/-) cells and untagged wild-type cells. In the kidney, TfR1(-/-) cells populated capsule and stroma, mesenchyme and nephron, but were underrepresented in ureteric bud tips. Consistently, TfR1 provided transferrin to the ureteric bud, but not to the capsule or the stroma. Instead of transferrin, we found that the capsule internalized ferritin. Since the capsule expressed a novel receptor called Scara5, we tested its role in ferritin uptake and found that Scara5 bound serum ferritin and then stimulated its endocytosis from the cell surface with consequent iron delivery. These data implicate cell type-specific mechanisms of iron traffic in organogenesis, which alternatively utilize transferrin or non-transferrin iron delivery pathways.
Texte intégral:
1
Collection:
01-internacional
Base de données:
MEDLINE
Sujet principal:
Récepteurs à la transferrine
/
Transferrine
/
Récepteurs de surface cellulaire
/
Protéines de liaison au fer
/
Récepteurs éboueurs de classe A
/
Ferritines
/
Fer
Limites:
Animals
Langue:
En
Journal:
Dev Cell
Sujet du journal:
EMBRIOLOGIA
Année:
2009
Type de document:
Article
Pays d'affiliation:
États-Unis d'Amérique
Pays de publication:
EEUU
/
ESTADOS UNIDOS
/
ESTADOS UNIDOS DA AMERICA
/
EUA
/
UNITED STATES
/
UNITED STATES OF AMERICA
/
US
/
USA