Purification and characterization of Erythroid Differentiation Factor(EDF) isolated from human leukemia cell line THP-1

Eto, Yuzuru; Tsuji, Tomoko; Takezawa, Misako; Takano, Satoshi; Yokogawa, Yasunori; Shibai, Hiroshiro

doi:10.1016/0006-291x(87)91528-2

Cited by 411 publications

(123 citation statements)

References 6 publications

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“…This line di erentiates into erythrocytes in response to activin (Ikawa et al, 1976;Eto et al, 1987). Untransfected or vector-transfected F5-5 cells, treated or untreated with activin, did not express gsc mRNA (data not shown).…”

Section: Ectopic Expression Of Goosecoid (Gsc) In the Erythroblast Cementioning

confidence: 83%

“…We expressed GSC in the erythroblastic cell line, F5-5 (Ikawa et al, 1976), a line that di erentiates into hemoglobin producing cells in response to activin (Eto et al, 1987). Although F5-5 cells do not express gsc mRNA, even following activin treatment (data not shown), forced expression of gsc via stable transfection inhibited activin-induced di erentiation.…”

Section: Discussionmentioning

confidence: 96%

“…Vector transfected (Vector) and four individual clones (gsc74-1 ± 4) were cultured in the presence or absence of activin (100 ng/ml) for 6 days at 1610 3 cells/100 ml/well in a 96-well microplate. After 6 days, cultures were stained with dianisidine to detect hemoglobin positive cells (Eto et al, 1987) ets family protein PU.1 (Klemsz et al, 1990;Hagemeier et al, 1993) with a molecular weight between 36 and 46 kDa (Schuetze et al, 1992;Scott et al, 1994). To investigate a possible interaction of PU.1 and GSC, lysates from metabolically labeled F5-5 cells from both untreated and activin stimulated cultures were subjected to sequential a nity chromatography on GST-GSC beads, followed by immunoprecipitation of eluted material with an anti-PU.1 antibody.…”

Section: Ectopic Expression Of Goosecoid (Gsc) In the Erythroblast Cementioning

confidence: 99%

“…An activin high responder subclone was supplied by Dr Yuzuru Eto (Central Research Laboratories, Ajinomoto Co., Inc.; Eto et al, 1987). This subclone was grown in F12 (F12 Nutrient Mixture, Gibco BRL) supplemented with 8% fetal calf serum.…”

Section: Cell Linesmentioning

confidence: 99%

“…The TGFb-like signaling molecule activin has also been studied as an erythrocyte di erentiation factor, based on its ability to induce red blood cell maturation (Eto et al, 1987;Yu et al, 1987). In order to investigate the suppression of erythroid di erentiation by goosecoid further, we ectopically expressed gsc in an erythroblastic cell line.…”

Section: Introductionmentioning

confidence: 99%

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GOOSECOID inhibits erythrocyte differentiation by competing with Rb for PU.1 binding in murine cells

Konishi¹,

Tominaga²,

Watanabe³

et al. 1999

Oncogene

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Section: Ectopic Expression Of Goosecoid (Gsc) In the Erythroblast Cementioning

confidence: 83%

Section: Discussionmentioning

confidence: 96%

Section: Ectopic Expression Of Goosecoid (Gsc) In the Erythroblast Cementioning

confidence: 99%

Section: Cell Linesmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

GOOSECOID inhibits erythrocyte differentiation by competing with Rb for PU.1 binding in murine cells

Konishi¹,

Tominaga²,

Watanabe³

et al. 1999

Oncogene

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Analysis of activin A gene expression in human bone marrow stromal cells

et al. 1998

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Activin A, a member of the TGF-beta superfamily, plays roles in differentiation and development, including hematopoiesis. Our previous studies indicated that the expression of activin A by human bone marrow cells and monocytes is highly regulated by inflammatory cytokines and glucocorticoids. The present study was undertaken to investigate the regulation of activin A gene expression in the human bone marrow stromal cell lines L87/4 and HS-5, as well as in primary stromal cells. Northern blots demonstrated that, like primary stromal cells, the cell lines expressed four activin A RNA transcripts (6.4, 4.0, 2.8, and 1.6 kb), although distribution of the RNA among the four sizes varied. The locations of the 5' ends of the RNAs were investigated by Northern blots and RNase protection assays. The results identified a transcription start site at 212 nucleotides upstream of the translation start codon. In addition, luciferase expression assays of a series of deletion constructs were used to identify regulatory sequences upstream of the activin A gene. A 58 bp upstream sequence exhibits promoter activity. However, severalfold higher expression requires a positive element consisting of an additional 71 bp of the upstream region. Promoter activity was also identified between 2.5 and 3.6 kb upstream of the start codon. These findings suggest that expression of activin A at the transcriptional level follows complex patterns of regulation.

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Truncated activin type II receptor inhibits erythroid differentiation in K562 cells

Liu¹,

Shao²,

Yu³

2000

J. Cell. Biochem.

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Two receptor serine/threonine kinases (types I and II) have been identified as signaling transducing activin receptors. We studied the possibility of inhibiting activin A-dependent differentiation in K562 cells, using a dominant negative mutant of type II receptor. A vector was constructed expressing activin type II truncated receptor (ActRIIa) that lacks the cytoplasmic kinase domain. Since activin type I and II receptors form heteromeric complexes for signaling, the mutant receptors compete for binding to endogenous receptors, hence acting in a dominant negative fashion. K562 cells were stably transfected with ActRIIa, and independent clones were expanded. The truncated cDNA was integrated into the genome of the transfectants, as shown by polymerase chain reaction; and the surface expression of truncated receptors was shown by affinity cross-linking with (125)I-activin A. In wild-type K562 cells, activin A induced erythroid differentiation and cells started to express hemoglobins. In transfected cells expressing ActRIIa, the induction of erythroid differentiation was abrogated and less than 10% of cells were hemoglobin-containing cells after culture with activin A. Further transfection with wild-type type II receptors rescued the mutant phenotype of these transfectants, indicating that the effect of ActRIIa is dominant negative. In addition, phosphorylation of the cytoplasmic kinase domain of the type II receptor in vitro confirms the autophosphorylation of this portion of the receptor. Therefore, induction of erythroid differentiation in vitro is mediated through the cell surface activin receptor, and interference with this receptor signaling inhibits this process of differentiation in K562 cells.

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Purification and characterization of Erythroid Differentiation Factor(EDF) isolated from human leukemia cell line THP-1

Cited by 411 publications

References 6 publications

GOOSECOID inhibits erythrocyte differentiation by competing with Rb for PU.1 binding in murine cells

GOOSECOID inhibits erythrocyte differentiation by competing with Rb for PU.1 binding in murine cells

Analysis of activin A gene expression in human bone marrow stromal cells

Truncated activin type II receptor inhibits erythroid differentiation in K562 cells

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