scholarly journals Different signalling pathways are used in the commitment of murine erythroleukemia cells (TSA 8) to differentiate, and in the erythropoietin action on progenitor cells.

1989 ◽  
Vol 14 (2) ◽  
pp. 231-239
Author(s):  
Hiroaki Fukumoto ◽  
Yasuhisa Matsui ◽  
Masuo Obinata
Keyword(s):  
Progenitor Cells ◽  
Signalling Pathways ◽  
Erythroleukemia Cells ◽  
Murine Erythroleukemia ◽  
Murine Erythroleukemia 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.

Cell cycle analysis of p53-induced cell death in murine erythroleukemia cells

1993 ◽  
Vol 13 (1) ◽  
pp. 711-719
Author(s):  
J J Ryan ◽  
R Danish ◽  
C A Gottlieb ◽  
M F Clarke
Keyword(s):  
Cell Death ◽  
G1 Arrest ◽  
Wild Type ◽  
Transfected Cells ◽  
Endogenous Expression ◽  
Erythroleukemia Cells ◽  
Wild Type P53 ◽  
G1 Cells ◽  
Murine Erythroleukemia ◽  
Murine Erythroleukemia Cells

A temperature-sensitive mutant of murine p53 (p53Val-135) was transfected by electroporation into murine erythroleukemia cells (DP16-1) lacking endogenous expression of p53. While the transfected cells grew normally in the presence of mutant p53 (37.5 degrees C), wild-type p53 (32.5 degrees C) was associated with a rapid loss of cell viability. Genomic DNA extracted at 32.5 degrees C was seen to be fragmented into a characteristic ladder consistent with cell death due to apoptosis. Following synchronization by density arrest, transfected cells released into G1 at 32.5 degrees C were found to lose viability more rapidly than did randomly growing cultures. Following release into G1, cells became irreversibly committed to cell death after 4 h at 32.5 degrees C. Commitment to cell death correlated with the first appearance of fragmented DNA. Synchronized cells allowed to pass out of G1 prior to being placed at 32.5 degrees C continued to cycle until subsequently arrested in G1; loss of viability occurred following G1 arrest. In contrast to cells in G1, cells cultured at 32.5 degrees C for prolonged periods during S phase and G2/M, and then returned to 37.5 degrees C, did not become committed to cell death. G1 arrest at 37.5 degrees C, utilizing either mimosine or isoleucine deprivation, does not lead to rapid cell death. Upon transfer to 32.5 degrees C, these G1 synchronized cell populations quickly lost viability. Cells that were kept density arrested at 32.5 degrees C (G0) lost viability at a much slower rate than did cells released into G1. Taken together, these results indicate that wild-type p53 induces cell death in murine erythroleukemia cells and that this effect occurs predominantly in the G1 phase of actively cycling cells.

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