Gene expression of divalent metal transporter 1 and transferrin receptor in duodenum of Belgrade rats
| Autor: | Matthew J. Callow, Phillip S. Oates, Elizabeth Freitas, Evan H. Morgan, Carla Thomas |
|---|---|
| Rok vydání: | 2000 |
| Předmět: |
Male
Duodenum Physiology Enterocyte Iron Crypt Gene Expression Transferrin receptor Biology Iron-Binding Proteins Physiology (medical) Receptors Transferrin medicine Animals RNA Messenger Rats Wistar Cation Transport Proteins chemistry.chemical_classification Hepatology Osmolar Concentration digestive oral and skin physiology Transferrin Gastroenterology Rats Inbred Strains Transporter Iron deficiency DMT1 medicine.disease Molecular biology Small intestine Rats medicine.anatomical_structure chemistry Biochemistry biology.protein Carrier Proteins |
| Zdroj: | American Journal of Physiology-Gastrointestinal and Liver Physiology. 278:G930-G936 |
| ISSN: | 1522-1547 0193-1857 |
| Popis: | Regulation of iron absorption is thought to be mediated by the amount of iron taken up by duodenal crypt cells via the transferrin receptor (TfR)-transferrin cycle and the activity of the divalent metal transporter (DMT1), although DMT1 cannot be detected morphologically in crypt cells. We investigated the uptake of transferrin-bound iron by duodenal enterocytes in Wistar rats fed different levels of iron and Belgrade (b/b) rats in which iron uptake by the transferrin cycle is defective because of a mutation in DMT1. We showed that DMT1 in our colony of b/b rats contains the G185R mutation, which in enterocytes results in reduced cellular iron content and increased DMT1 gene expression similar to levels in iron deficiency of normal rats. In all groups the uptake of transferrin-bound iron by crypt cells was directly proportional to plasma iron concentration, being highest in iron-loaded Wistar rats and b/b rats. We conclude that the uptake of transferrin-bound iron by developing enterocytes is largely independent of DMT1. |
| Databáze: | OpenAIRE |
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