Erythroid �Differentiation � of Friend Cells

2015 ◽  
pp. 273-274
Author(s):  
Mitsuru Furusawa
Keyword(s):  
Erythroid Differentiation ◽  
Friend Cells

Decreased deoxy-d-glucose transport in Friend cells during exposure to inducers of erythroid differentiation

1977 ◽  
Vol 110 (2) ◽  
pp. 375-385 ◽  
Author(s):  
Ralph J. Germinario ◽  
Lawrence Kleiman ◽  
Susan Peters ◽  
Maureen Oliveira
Keyword(s):  
Glucose Transport ◽  
Erythroid Differentiation ◽  
Friend Cells

Opposite effects of murine interferons on erythroid differentiation of friend cells

Virology ◽  
1988 ◽  
Vol 167 (1) ◽  
pp. 185-193 ◽  
Author(s):  
Elisabetta Affabris ◽  
Maurizio Federico ◽  
Giovanna Romeo ◽  
Eliana M. Coccia ◽  
Giovanni B. Rossi
Keyword(s):  
Erythroid Differentiation ◽  
Friend Cells

Erythroid differentiation and protoporphyrin IX down-regulate frataxin expression in Friend cells: characterization of frataxin expression compared to molecules involved in iron metabolism and hemoglobinization

Blood ◽  
2002 ◽  
Vol 99 (10) ◽  
pp. 3813-3822 ◽  
Author(s):  
Erika M. Becker ◽  
Judith M. Greer ◽  
Prem Ponka ◽  
Des R. Richardson
Keyword(s):  
Friedreich Ataxia ◽  
Protoporphyrin Ix ◽  
Erythroid Differentiation ◽  
Ammonium Citrate ◽  
Ferric Ammonium Citrate ◽  
Mrna Levels ◽  
Synthesis Inhibitor ◽  
Protein Levels ◽  
Friend Cells

Friedreich ataxia (FA) is caused by decreased frataxin expression that results in mitochondrial iron (Fe) overload. However, the role of frataxin in mammalian Fe metabolism remains unclear. In this investigation we examined the function of frataxin in Fe metabolism by implementing a well-characterized model of erythroid differentiation, namely, Friend cells induced using dimethyl sulfoxide (DMSO). We have characterized the changes in frataxin expression compared to molecules that play key roles in Fe metabolism (the transferrin receptor [TfR] and the Fe transporter Nramp2) and hemoglobinization (β-globin). DMSO induction of hemoglobinization results in a marked decrease in frataxin gene (Frda) expression and protein levels. To a lesser extent, Nramp2messenger RNA (mRNA) levels were also decreased on erythroid differentiation, whereas TfR and β-globinmRNA levels increased. Intracellular Fe depletion using desferrioxamine or pyridoxal isonicotinoyl hydrazone, which chelate cytoplasmic or cytoplasmic and mitochondrial Fe pools, respectively, have no effect on frataxin expression. Furthermore, cytoplasmic or mitochondrial Fe loading of induced Friend cells with ferric ammonium citrate, or the heme synthesis inhibitor, succinylacetone, respectively, also had no effect on frataxin expression. Although frataxin has been suggested by others to be a mitochondrial ferritin, the lack of effect of intracellular Fe levels on frataxin expression is not consistent with an Fe storage role. Significantly, protoporphyrin IX down-regulates frataxin protein levels, suggesting a regulatory role of frataxin in Fe or heme metabolism. Because decreased frataxin expression leads to mitochondrial Fe loading in FA, our data suggest that reduced frataxin expression during erythroid differentiation results in mitochondrial Fe sequestration for heme biosynthesis.

An intracellular factor that induces erythroid differentiation in mouse erythroleukemia (Friend) cells

Cell ◽  
1986 ◽  
Vol 44 (4) ◽  
pp. 663-669 ◽  
Author(s):  
Shintaro Nomura ◽  
Satoshi Yamagoe ◽  
Toshikazu Kamiya ◽  
Michio Oishi
Keyword(s):  
Erythroid Differentiation ◽  
Friend Cells ◽  
Mouse Erythroleukemia

Friend erythroleukemia cell membrane transferrin receptors

1980 ◽  
Vol 58 (10) ◽  
pp. 935-940 ◽  
Author(s):  
A. Wilczynska ◽  
H. M. Schulman
Keyword(s):  
Sodium Dodecyl Sulfate ◽  
Sodium Dodecyl ◽  
Erythroid Differentiation ◽  
Binding Activity ◽  
Transferrin Receptors ◽  
Membrane Component ◽  
Erythroleukemia Cells ◽  
Single Protein ◽  
Friend Cells ◽  
Erythroleukemia Cell

We have compared the uptake of transferrin by murine Friend erythroleukemia cells with the uptake of transferrin by murine reticulocytes. Friend cells which had been induced to erythroid differentiation by dimethyl sulfoxide took up transferrin in a manner qualitatively and quantitatively similar to the uptake of transferrin by reticulocytes, while uninduced Friend cells took up only negligible amounts of transferrin. Specific transferrin-binding activity could be demonstrated in detergent extracts of membranes from induced cells and this activity was isolated from membrane extracts by the use of antibody to transferrin. The isolated membrane component(s) with transferrin-binding activity migrated electrophoretically as a single protein on sodium dodecyl sulfate gels and had similar properties to a transferrin-binding protein isolated previously from reticulocytes.

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