scholarly journals Characterization of cellular receptors for erythroid differentiation factor on murine erythroleukemia cells

1989 ◽  
Vol 264 (17) ◽  
pp. 10309-10314
Author(s):  
M Hino ◽  
A Tojo ◽  
K Miyazono ◽  
Y Miura ◽  
S Chiba ◽  
...  
Keyword(s):  
Erythroid Differentiation ◽  
Cellular Receptors ◽  
Differentiation Factor ◽  
Erythroleukemia Cells ◽  
Murine Erythroleukemia ◽  
Erythroid Differentiation Factor ◽  
Murine Erythroleukemia Cells

scholarly journals The identification and characterization of a novel human differentiation-inhibiting protein that selectively blocks erythroid differentiation

Blood ◽  
1992 ◽  
Vol 79 (5) ◽  
pp. 1161-1171
Author(s):  
JP Durkin ◽  
JM Biquard ◽  
JF Whitfield ◽  
N Morardet ◽  
J Royer ◽  
...  
Keyword(s):  
Culture Medium ◽  
Erythroid Differentiation ◽  
Pure Red Cell Aplasia ◽  
Red Cell ◽  
Erythroleukemia Cells ◽  
Inhibiting Protein ◽  
Murine Erythroleukemia ◽  
Identification And Characterization ◽  
Murine Erythroleukemia Cells

We have isolated a novel inhibitor of erythropoietic differentiation from the plasma of a patient suffering from idiopathic pure red cell aplasia. This differentiation-inhibiting protein (DIP) specifically blocked the differentiation of human burst-forming unit-erythroid (BFU- E), but not colony-forming unit-erythroid (CFU-E) cells. DIP also blocked the maturation of murine BFU-E cells, but not CFU-E or CFU- granulocyte-macrophage cells, and it inhibited the dimethyl sulfoxide (DMSO)-induced differentiation of Friend murine erythroleukemia cells (FLC) at levels between 10(-10) and 10(-12) mol/L. DIP activity was not detectable in the plasma of normal, healthy subjects. Unlike other known inhibitors of hematopoiesis, DIP appears to directly inhibit erythropoietic differentiation, because it did not affect the proliferation of untreated FLC and it effectively blocked FLC hemoglobinization without affecting the ability of the blocked cells to proliferate. DIP blocked FLC differentiation only when added to the culture medium within 1 hour of inducing the cells with DMSO, suggesting that the protein inhibited an early, but critical, DMSO- induced cellular process. DIP appears to be at least partially responsible for the patient's anemia, and its unique activity suggests a role in the early development of some erythroleukemias.

scholarly journals The identification and characterization of a novel human differentiation-inhibiting protein that selectively blocks erythroid differentiation

Blood ◽  
1992 ◽  
Vol 79 (5) ◽  
pp. 1161-1171 ◽  
Author(s):  
JP Durkin ◽  
JM Biquard ◽  
JF Whitfield ◽  
N Morardet ◽  
J Royer ◽  
...  
Keyword(s):  
Culture Medium ◽  
Erythroid Differentiation ◽  
Pure Red Cell Aplasia ◽  
Red Cell ◽  
Erythroleukemia Cells ◽  
Inhibiting Protein ◽  
Murine Erythroleukemia ◽  
Identification And Characterization ◽  
Murine Erythroleukemia Cells

Abstract We have isolated a novel inhibitor of erythropoietic differentiation from the plasma of a patient suffering from idiopathic pure red cell aplasia. This differentiation-inhibiting protein (DIP) specifically blocked the differentiation of human burst-forming unit-erythroid (BFU- E), but not colony-forming unit-erythroid (CFU-E) cells. DIP also blocked the maturation of murine BFU-E cells, but not CFU-E or CFU- granulocyte-macrophage cells, and it inhibited the dimethyl sulfoxide (DMSO)-induced differentiation of Friend murine erythroleukemia cells (FLC) at levels between 10(-10) and 10(-12) mol/L. DIP activity was not detectable in the plasma of normal, healthy subjects. Unlike other known inhibitors of hematopoiesis, DIP appears to directly inhibit erythropoietic differentiation, because it did not affect the proliferation of untreated FLC and it effectively blocked FLC hemoglobinization without affecting the ability of the blocked cells to proliferate. DIP blocked FLC differentiation only when added to the culture medium within 1 hour of inducing the cells with DMSO, suggesting that the protein inhibited an early, but critical, DMSO- induced cellular process. DIP appears to be at least partially responsible for the patient's anemia, and its unique activity suggests a role in the early development of some erythroleukemias.

scholarly journals Stability of alpha and beta globin messenger RNA during induced differentiation of mouse erythroleukemia cells

Blood ◽  
1979 ◽  
Vol 54 (4) ◽  
pp. 933-939
Author(s):  
R Gambari ◽  
RA Rifkind ◽  
PA Marks
Keyword(s):  
Messenger Rna ◽  
Erythroid Differentiation ◽  
Beta Globin ◽  
Globin Mrna ◽  
Induced Differentiation ◽  
Hexamethylene Bisacetamide ◽  
Erythroleukemia Cells ◽  
Mrna Content ◽  
Murine Erythroleukemia ◽  
Murine Erythroleukemia Cells

Murine erythroleukemia cells (MELC) are induced to express erythroid differentiation when cultured with hexamethylene bisacetamide (HMBA). Newly synthesized alpha and beta globin mRNA are both relatively stable, half-life (t1/2) greater than 50 hr, early in the course of induced differentiation. In fully induced cells there is a decrease in stability of both newly synthesized alpha and beta globin mRNA. The decay of alpha mRNA is faster, (t 1/2, 10--12 hr) than beta globin mRNA (t1/2, 20--22 hr). Thus, differences in stability of alpha and beta globin mRNA plays a role in determining the ratio of alpha to beta mRNA content in differentiated erythroid cells.

Mechanism of erythropoietin action on the erythroid progenitor cells induced from murine erythroleukemia cells (TSA8)

Development ◽  
1989 ◽  
Vol 105 (1) ◽  
pp. 109-114 ◽  
Author(s):  
H. Fukumoto ◽  
Y. Matsui ◽  
M. Obinata
Keyword(s):  
Progenitor Cells ◽  
Phosphodiesterase Inhibitor ◽  
Second Messenger ◽  
Erythroid Differentiation ◽  
Camp Level ◽  
Erythropoietin Receptor ◽  
Erythroid Progenitor ◽  
Erythroleukemia Cells ◽  
Murine Erythroleukemia ◽  
Murine Erythroleukemia Cells

Erythropoietin is a well-known erythroid differentiation and growth factor, but the mechanism of its action is not well understood. In this work, we have examined its mechanism of action on the erythropoietin-responsive murine erythroleukemia cells (TSA8). TSA8 cells become responsive to erythropoietin after induction with DMSO. Stimulatory effects on erythropoietin response are observed with the addition of compounds affecting the cAMP level such as forskolin, phosphodiesterase inhibitor and cholera toxin only in the presence of erythropoietin. cAMP analogues themselves show no stimulatory effect on TSA8 cells, nor does erythropoietin increase cAMP level in the cells. Thus, it is suggested that cAMP does not act as a direct second messenger for signal transduction through erythropoietin receptors, but as a stimulator of the erythropoietin receptor pathway and/or as a second messenger in combination with the receptor pathway. The mechanism for acquisition of responsiveness to growth and differentiation factors of progenitor cells is discussed.

scholarly journals Calcium influx in induced differentiation of murine erythroleukemia cells

Blood ◽  
1993 ◽  
Vol 81 (3) ◽  
pp. 783-792 ◽  
Author(s):  
B Gillo ◽  
YS Ma ◽  
AR Marks
Keyword(s):  
Calcium Channel ◽  
Calcium Influx ◽  
Cdna Probe ◽  
Erythroid Differentiation ◽  
Early Event ◽  
Induced Differentiation ◽  
Erythroleukemia Cells ◽  
Murine Erythroleukemia ◽  
Murine Erythroleukemia Cells

Abstract Murine erythroleukemia cells (MELC) have served as a model for examining the regulation of erythroid differentiation. However, the role of Ca2+ in the signal transduction pathways regulating differentiation remains unclear. To begin to address this uncertainty we have characterized the regulation of cytoplasmic Ca2+ and the possible role of calcium channels during induced differentiation in MELC. MELC can be induced to terminal differentiation using the polar/apolar compound hexamethylene bisacetamide (HMBA). We found that HMBA stimulated Ca2+ influx within 3 to 6 minutes and that Ca2+ entry was required but not sufficient for MELC growth and differentiation. Nifedipine (1 to 10 mumol/L), a calcium channel antagonist, blocked HMBA-induced Ca2+ influx and inhibited differentiation by approximately 60%. Depolarization of the MELC membrane did not induce Ca2+ influx and whole-cell patch-clamp recordings failed to detect a voltage-activated Ca2+ current, suggesting that MELC do not express detectable levels of a functional voltage-dependent calcium channel (VDCC). However, a cDNA probe encoding a portion of the alpha 1 subunit of the cardiac VDCC detected an approximately 8-kb mRNA on Northern blots of total MELC RNA. Taken together, these data show that Ca2+ influx is an early event associated with HMBA-induced differentiation in MELC, blockade of this calcium influx inhibits induced differentiation, and a voltage- insensitive dihydropyridine-sensitive calcium channel may be involved in Ca2+ influx in MELC.

Sign in / Sign up

Export Citation Format

Share Document