scholarly journals Fusion of the erythropoietin receptor and the Friend spleen focus-forming virus gp55 glycoprotein transforms a factor-dependent hematopoietic cell line.

1993 ◽  
Vol 13 (2) ◽  
pp. 739-748 ◽  
Author(s):  
M O Showers ◽  
J C DeMartino ◽  
Y Saito ◽  
A D D'Andrea
Keyword(s):  
Cell Line ◽  
Fusion Proteins ◽  
Transmembrane Domain ◽  
Specific Interaction ◽  
Erythropoietin Receptor ◽  
Hematopoietic Cell ◽  
Wild Type ◽  
Hematopoietic Cell Line ◽  
Transforming Activity ◽  
Fusion Polypeptides

The Friend spleen focus-forming virus (SFFV) gp55 glycoprotein binds to the erythropoietin receptor (EPO-R), causing constitutive receptor signaling and the first stage of Friend erythroleukemia. We have used three independent strategies to further define this transforming molecular interaction. First, using a retroviral selection strategy, we have isolated the cDNAs encoding three fusion polypeptides containing regions of both EPO-R and gp55. These fusion proteins, like full-length gp55, transformed the Ba/F3 factor-dependent hematopoietic cell line and localized the transforming activity of gp55 to its transmembrane domain. Second, we have isolated a mutant of gp55 (F-gp55-M1) which binds, but fails to activate, EPO-R. We have compared the transforming activity of this gp55 mutant with the EPO-R-gp55 fusion proteins and with other variants of gp55, including wild-type polycythemia Friend gp55 and Rauscher gp55. All of the fusion polypeptides and mutant gp55 polypeptides were expressed at comparable levels, and all coimmunoprecipitated with wild-type EPO-R, but only the Friend gp55 and the EPO-R-gp55 fusion proteins constitutively activated wild-type EPO-R. Third, we have examined the specificity of the EPO-R-gp55 interaction by comparing the differential activation of murine and human EPO-R by gp55. Wild-type gp55 had a highly specific interaction with murine EPO-R; gp55 bound, but did not activate, human EPO-R.

Fusion of the erythropoietin receptor and the Friend spleen focus-forming virus gp55 glycoprotein transforms a factor-dependent hematopoietic cell line

1993 ◽  
Vol 13 (2) ◽  
pp. 739-748
Author(s):  
M O Showers ◽  
J C DeMartino ◽  
Y Saito ◽  
A D D'Andrea
Keyword(s):  
Cell Line ◽  
Fusion Proteins ◽  
Transmembrane Domain ◽  
Specific Interaction ◽  
Erythropoietin Receptor ◽  
Hematopoietic Cell ◽  
Wild Type ◽  
Hematopoietic Cell Line ◽  
Transforming Activity ◽  
Fusion Polypeptides

The Friend spleen focus-forming virus (SFFV) gp55 glycoprotein binds to the erythropoietin receptor (EPO-R), causing constitutive receptor signaling and the first stage of Friend erythroleukemia. We have used three independent strategies to further define this transforming molecular interaction. First, using a retroviral selection strategy, we have isolated the cDNAs encoding three fusion polypeptides containing regions of both EPO-R and gp55. These fusion proteins, like full-length gp55, transformed the Ba/F3 factor-dependent hematopoietic cell line and localized the transforming activity of gp55 to its transmembrane domain. Second, we have isolated a mutant of gp55 (F-gp55-M1) which binds, but fails to activate, EPO-R. We have compared the transforming activity of this gp55 mutant with the EPO-R-gp55 fusion proteins and with other variants of gp55, including wild-type polycythemia Friend gp55 and Rauscher gp55. All of the fusion polypeptides and mutant gp55 polypeptides were expressed at comparable levels, and all coimmunoprecipitated with wild-type EPO-R, but only the Friend gp55 and the EPO-R-gp55 fusion proteins constitutively activated wild-type EPO-R. Third, we have examined the specificity of the EPO-R-gp55 interaction by comparing the differential activation of murine and human EPO-R by gp55. Wild-type gp55 had a highly specific interaction with murine EPO-R; gp55 bound, but did not activate, human EPO-R.

scholarly journals Tcf7 Is an Important Regulator of the Switch of Self-Renewal and Differentiation in a Multipotential Hematopoietic Cell Line

PLoS Genetics ◽  
2012 ◽  
Vol 8 (3) ◽  
pp. e1002565 ◽  
Author(s):  
Jia Qian Wu ◽  
Montrell Seay ◽  
Vincent P. Schulz ◽  
Manoj Hariharan ◽  
David Tuck ◽  
...  
Keyword(s):  
Cell Line ◽  
Hematopoietic Cell ◽  
Self Renewal ◽  
Hematopoietic Cell Line ◽  
Important Regulator

scholarly journals Retinoic acid inhibits interleukin-6-induced macrophage differentiation and apoptosis in a murine hematopoietic cell line, Y6

Blood ◽  
1992 ◽  
Vol 80 (9) ◽  
pp. 2298-2305 ◽  
Author(s):  
K Oritani ◽  
T Kaisho ◽  
K Nakajima ◽  
T Hirano
Keyword(s):  
Signal Transduction ◽  
Retinoic Acid ◽  
Cell Line ◽  
Interleukin 6 ◽  
Signal Transduction Pathway ◽  
Inhibitory Effect ◽  
Hematopoietic Cell ◽  
Transduction Pathway ◽  
Macrophage Differentiation ◽  
Hematopoietic Cell Line

Abstract We established a radiation-induced murine hematopoietic cell line, Y6, that could be induced to differentiate into macrophages by interleukin- 6 (IL-6). IL-6 also induced growth inhibition and apoptosis in Y6 cells. Retinoic acid (RA) inhibited such effects of IL-6 on Y6 cells. The inhibitory effect of RA on the effects of IL-6 was not caused by the downregulation of the IL-6 receptor, because RA neither affected the expression of IL-6 receptor mRNA nor the expression of IL-6 receptor molecule on the cell surface. Furthermore, RA did not inhibit the IL-6-induced expression of junB mRNA, indicating that the expression of functionally active IL-6 receptor and the signal transduction pathway activating the junB gene are not inhibited by RA. IL-6-induced macrophage differentiation of Y6 cells was preceded by the downregulation of the c-myc gene, which was also prevented by RA. Because the inhibitory effect of RA on Y6 cells was reversible and seemed not to require de novo protein synthesis, the RA receptor by itself might be directly involved in the inhibition of the IL-6 signal transduction pathway. The results indicated that the IL-6 signal transduction pathways leading to the induction of macrophage differentiation and junB gene expression can be dissected by RA.

A novel stromal cell-dependent hematopoietic cell line established from temperature-sensitive SV40 T-antigen transgenic mice

1999 ◽  
Vol 27 (6) ◽  
pp. 1087-1096 ◽  
Author(s):  
Nobuaki Yanai ◽  
Naoko Matsui ◽  
Ken-Ichi Matsuda ◽  
Tadashi Furusawa ◽  
Tadashi Okubo ◽  
...  
Keyword(s):  
Transgenic Mice ◽  
Cell Line ◽  
Stromal Cell ◽  
T Antigen ◽  
Hematopoietic Cell ◽  
Temperature Sensitive ◽  
Sv40 T Antigen ◽  
Hematopoietic Cell Line

Identification of a vascular endothelial growth factor (VEGF) antagonist, sFlt-1, from a human hematopoietic cell line NALM-16

FEBS Letters ◽  
2000 ◽  
Vol 469 (1) ◽  
pp. 14-18 ◽  
Author(s):  
Toshiya Inoue ◽  
Keiko Kibata ◽  
Motoyuki Suzuki ◽  
Shuji Nakamura ◽  
Ryuichi Motoda ◽  
...  
Keyword(s):  
Vascular Endothelial Growth Factor ◽  
Growth Factor ◽  
Cell Line ◽  
Hematopoietic Cell ◽  
Vascular Endothelial ◽  
Hematopoietic Cell Line ◽  
Endothelial Growth Factor

scholarly journals Biological effects induced by variable levels of BCR-ABL protein in the pluripotent hematopoietic cell line UT-7

Leukemia ◽  
2000 ◽  
Vol 14 (4) ◽  
pp. 662-670 ◽  
Author(s):  
C Issaad ◽  
M Ahmed ◽  
S Novault ◽  
ML Bonnet ◽  
T Bennardo ◽  
...  
Keyword(s):  
Cell Line ◽  
Biological Effects ◽  
Hematopoietic Cell ◽  
Hematopoietic Cell Line
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