These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: Hemin inhibits internalization of transferrin by reticulocytes and promotes phosphorylation of the membrane transferrin receptor.
    Author: Cox TM, O'Donnell MW, Aisen P, London IM.
    Journal: Proc Natl Acad Sci U S A; 1985 Aug; 82(15):5170-4. PubMed ID: 2991909.
    Abstract:
    Addition of hemin to reticulocytes inhibits incorporation of iron from transferrin [Ponka, P. & Neuwirt, J. (1969) Blood 33, 609-707]. Heme also regulates protein synthesis in immature erythroid cells through its effects on phosphorylation of the initiation factor eIF-2. We have therefore examined its effects on endocytosis of iron-transferrin and phosphorylation of the transferrin receptor. Hemin (10-50 microM) reduced iron transport but increased cell-associated transferrin. When intracellular iron delivery was inhibited by NH4Cl, no such increase in cell-associated transferrin was seen. During uptake of 125I-labeled transferrin in the steady state, the use of a washing technique to dissociate bound transferrin on the cell membrane showed that radioligand accumulated on the surface of hemin-treated cells. Hemin reduced the initial influx of transferrin, thereby diminishing incorporation of iron. Receptor phosphorylation was investigated by immunoprecipitation of reticulocyte extracts after metabolic labeling with [32P]Pi. In the absence of ligand, phosphorylated receptor was chiefly localized on cell stroma. Exposure to transferrin increased cytosolic phosphorylated receptor from 15-30% to approximately 50% of the total, an effect overcome by hemin treatment. Addition of hemin in the presence of transferrin enhanced net phosphorylated receptor in the reticulocyte in association with a redistribution of phosphorylated receptor to stromal membranes. The findings suggest a possible relationship of phosphorylation to endocytosis of the transferrin receptor in reticulocytes.
    [Abstract] [Full Text] [Related] [New Search]