Hemin inhibits internalization of transferrin by reticulocytes and promotes phosphorylation of the membrane transferrin receptor
Journal Article
·
· Proc. Natl. Acad. Sci. U.S.A.; (United States)
Addition of hemin to reticulocytes inhibits incorporation of iron from transferrin. Heme also regulates protein synthesis in immature erythroid cells through its effects on phosphorylation of the initiation factor eIF-2. The authors have examined its effects on endocytosis of iron-transferrin and phosphorylation of the transferrin receptor. Hemin reduced iron transport but increased cell-associated transferrin. During uptake of SVI-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. Receptor phosphorylation was investigated by immunoprecipitation of reticulocyte extracts after metabolic labeling with (TSP)P/sub i/. 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. The findings suggest a possible relationship of phosphorylation to endocytosis of the transferrin receptor in reticulocytes.
- Research Organization:
- Massachusetts Institute of Technology, Cambridge
- OSTI ID:
- 6085399
- Journal Information:
- Proc. Natl. Acad. Sci. U.S.A.; (United States), Journal Name: Proc. Natl. Acad. Sci. U.S.A.; (United States) Vol. 82:15; ISSN PNASA
- Country of Publication:
- United States
- Language:
- English
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Related Subjects
550301* -- Cytology-- Tracer Techniques
59 BASIC BIOLOGICAL SCIENCES
ANIMALS
BETA DECAY RADIOISOTOPES
BETA-MINUS DECAY RADIOISOTOPES
BIOLOGICAL MATERIALS
BLOOD
BLOOD CELLS
BLOOD FORMATION
BODY FLUIDS
CARBOXYLIC ACIDS
CELL CONSTITUENTS
CELL MEMBRANES
CHEMICAL REACTIONS
DAYS LIVING RADIOISOTOPES
ELECTRON CAPTURE RADIOISOTOPES
ERYTHROCYTES
ERYTHROPOIESIS
EVEN-ODD NUCLEI
GLOBULINS
GLOBULINS-BETA
HEME
HETEROCYCLIC ACIDS
HETEROCYCLIC COMPOUNDS
INHIBITION
INTERMEDIATE MASS NUCLEI
IODINE 125
IODINE ISOTOPES
IRON 59
IRON ISOTOPES
ISOTOPES
LIGHT NUCLEI
MAMMALS
MATERIALS
MEMBRANE TRANSPORT
MEMBRANES
METALLOPROTEINS
NUCLEI
ODD-EVEN NUCLEI
ODD-ODD NUCLEI
ORGANIC ACIDS
ORGANIC COMPOUNDS
ORGANIC NITROGEN COMPOUNDS
PHAGOCYTOSIS
PHOSPHORUS 32
PHOSPHORUS ISOTOPES
PHOSPHORYLATION
PIGMENTS
PORPHYRINS
PROTEINS
RABBITS
RADIOISOTOPES
RECEPTORS
RETICULOCYTES
TRANSFERRIN
VERTEBRATES
59 BASIC BIOLOGICAL SCIENCES
ANIMALS
BETA DECAY RADIOISOTOPES
BETA-MINUS DECAY RADIOISOTOPES
BIOLOGICAL MATERIALS
BLOOD
BLOOD CELLS
BLOOD FORMATION
BODY FLUIDS
CARBOXYLIC ACIDS
CELL CONSTITUENTS
CELL MEMBRANES
CHEMICAL REACTIONS
DAYS LIVING RADIOISOTOPES
ELECTRON CAPTURE RADIOISOTOPES
ERYTHROCYTES
ERYTHROPOIESIS
EVEN-ODD NUCLEI
GLOBULINS
GLOBULINS-BETA
HEME
HETEROCYCLIC ACIDS
HETEROCYCLIC COMPOUNDS
INHIBITION
INTERMEDIATE MASS NUCLEI
IODINE 125
IODINE ISOTOPES
IRON 59
IRON ISOTOPES
ISOTOPES
LIGHT NUCLEI
MAMMALS
MATERIALS
MEMBRANE TRANSPORT
MEMBRANES
METALLOPROTEINS
NUCLEI
ODD-EVEN NUCLEI
ODD-ODD NUCLEI
ORGANIC ACIDS
ORGANIC COMPOUNDS
ORGANIC NITROGEN COMPOUNDS
PHAGOCYTOSIS
PHOSPHORUS 32
PHOSPHORUS ISOTOPES
PHOSPHORYLATION
PIGMENTS
PORPHYRINS
PROTEINS
RABBITS
RADIOISOTOPES
RECEPTORS
RETICULOCYTES
TRANSFERRIN
VERTEBRATES