Literature DB >> 3390148

Haem inhibits iron uptake subsequent to endocytosis of transferrin in reticulocytes.

P Ponka1, H M Schulman, J Martinez-Medellin.   

Abstract

Haem controls the rate of haem synthesis in erythroid cells by inhibiting iron incorporation from transferrin. The present results indicate that haem primarily inhibits the release of iron from transferrin subsequent to transferrin endocytosis and that the inhibition of transferrin endocytosis caused by relatively high concentrations of haem is a secondary effect. Low concentrations of haem (10-25 microM) significantly inhibit reticulocyte iron uptake and to a greater extent its incorporation into haem, but do not inhibit either the initial rate of transferrin uptake or its internalization by the cells.

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Year:  1988        PMID: 3390148      PMCID: PMC1148969          DOI: 10.1042/bj2510105

Source DB:  PubMed          Journal:  Biochem J        ISSN: 0264-6021            Impact factor:   3.857


  27 in total

1.  Evidence supporting a physiological role for the hemin-controlled translational repressor of globin synthesis in reticulocytes.

Authors:  H M Schulman
Journal:  Biochim Biophys Acta       Date:  1975-12-04

2.  The oxidation state of newly synthesized hemoglobin.

Authors:  H M Schulman; J Martinez-Medellin; R Sidloi
Journal:  Biochem Biophys Res Commun       Date:  1974-01       Impact factor: 3.575

3.  The reticulocyte-mediated release of iron and bicarbonate from transferrin: effect of metabolic inhibitors.

Authors:  H M Schulman; J Martinez-Medellin; R Sidloi
Journal:  Biochim Biophys Acta       Date:  1974-05-24

4.  The role of heme in the release of iron from transferrin in reticulocytes.

Authors:  P Ponka; J Neuwirt; J Borová
Journal:  Enzyme       Date:  1974

5.  The preparation, properties, and metabolism of 14C-bicarbonate-labelled transferrin.

Authors:  J Martinez-Medellin; H M Schulman
Journal:  Biochem Biophys Res Commun       Date:  1973-07-02       Impact factor: 3.575

6.  The kinetics of iron and transferrin incorporation into rabbit erythroid cells and the nature of stromal-bound iron.

Authors:  J Martinez-Medellin; H M Schulman
Journal:  Biochim Biophys Acta       Date:  1972-04-21

7.  The effect of plasma and transferrin on the hemin inhibition of iron uptake by reticulocytes.

Authors:  P Ponka; J Neuwirt
Journal:  Experientia       Date:  1972-02-15

8.  Solid state lactoperoxidase: a highly stable enzyme for simple, gentle iodination of proteins.

Authors:  G S David
Journal:  Biochem Biophys Res Commun       Date:  1972-07-25       Impact factor: 3.575

9.  Regulation of iron entry into reticulocytes. I. Feedback inhibitory effect of heme on iron entry into reticulocytes and on heme synthesis.

Authors:  P Ponka; J Neuwirt
Journal:  Blood       Date:  1969-05       Impact factor: 22.113

10.  The role of heme in the maturation of erythroblasts: the effects of inhibition of pyridoxine metabolism.

Authors:  L M Hoffman; J Ross
Journal:  Blood       Date:  1980-05       Impact factor: 22.113

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  2 in total

1.  Human erythroid 5-aminolevulinate synthase: promoter analysis and identification of an iron-responsive element in the mRNA.

Authors:  T C Cox; M J Bawden; A Martin; B K May
Journal:  EMBO J       Date:  1991-07       Impact factor: 11.598

2.  Extracellular glycine is necessary for optimal hemoglobinization of erythroid cells.

Authors:  Daniel Garcia-Santos; Matthias Schranzhofer; Richard Bergeron; Alex D Sheftel; Prem Ponka
Journal:  Haematologica       Date:  2017-05-11       Impact factor: 9.941

  2 in total

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