3 edition of The role of RNA synthesis in erythropoietin induced erythroid differentiation found in the catalog.
The role of RNA synthesis in erythropoietin induced erythroid differentiation
Written in English
|LC Classifications||Microfilm 26029|
|The Physical Object|
|Pagination||ix, 232 l.|
|Number of Pages||232|
|LC Control Number||94895492|
In this chapter we have focused on the major changes in nucleic acids and proteins that occur during terminal erythroid cell development and have Gross, M., and Goldwasser, E., , On the mechanism of erythropoietin-induced differentiation. VII: The relationship Macromolecular Synthesis and Degradation during Terminal Erythroid Cell Cited by: 7. These findings indicate that Src may play a more universal role in EPO-induced erythroid differentiation than Lyn. Recently, Src-induced tyrosine phosphorylation and DNA binding of STAT5 have been Cited by:
differentiation markers was increased under hypoxic conditions, but decreased with RNA interference of HIF1 or GATA1. Flow cytome- try analysis also indicated that hypoxia, desferrioxamine or CoCl 2 induced expression of erythroid surface markers CD71 and CDa,Cited by: Some Studies of Erythroid Differentiation In Vitro epo for erythropoietin, rRNA for ribosomal RNA, tRNA for transfer RNA. mation of ribosomal RNA, transfer RNA, by increased protein synthesis, and the RNA synthesis, while the non-induced. i- CL I - C 0 - .
The regulation of transferrin‐receptor synthesis was studied in J2E erythroid cells induced to differentiate with erythropoietin. Nuclear run‐on assays demonstrated that transcription of the transferrin‐receptor gene rose markedly after erythropoietin by: MAPK (p38) and ERK are involved in erythropoietin-induced erythroid differentiation, we studied their roles using specific inhibitors. p38 inhibitor (SB) prevented CsA-induced hemoglobin synthesis in K cells, although MEK/ERK inhibitor (U) en-hanced it by times in K cells. These results indicate activation of p38 and inacti Cited by:
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Within 1 hr, erythropoietin causes a 2- to 3-fold stimulation of uridine incorporation into RNA by these cells. The types of RNA preferentially stimulated by erythropoietin during the first hour of exposure of the cells to the hormone include ribosomal RNAs and their precursors, as well as S by: Erythropoietin (EPO) is the key hormone responsible for effective erythropoiesis, and iron is the essential mineral required for hemoglobin production.
EPO allows survival and proliferation of erythroid precursor cells by generating intracellular signals resulting in the prevention of : Ajay K. Singh. Erythropoietin (EPO) acts primarily to stimulate erythroid cell production supporting the survival, proliferation and differentiation of erythroid progenitor cells.
In addition to hematopoietic cells, expression of the EPO receptor (EPO-R) and EPO response are observed in other cell types including endothelial and neural cells [ 1 - 4 ].Cited by: We have examined the role of DNA synthesis in the induced differentiation of erythropoietin-responsive cells (ERC) by using cultured marrow cells from plethoric rats.
In such marrow cell populations there are minimal numbers of differentiated erythroid cells permitting the study of erythropoietin action on the non-differentiated primitive by: 9.
If erythropoietin is allowed to act on the cells for 24 h, the further increase in hemoglobin synthesis is no longer affected by actinomycin D, demonstrating a relatively stable messenger RNA in the type of cell which characterizes the erythroid by: Erythropoietin (EPO) is the hormone necessary for production of red blood cells that function primarily to transport oxygen from the lungs to tissues.
EPO is synthesised in the adult kidney and can be induced by anaemia or hypoxic stress to increase the number of red blood cells and oxygen transport. Marrow cells induced toward erythroid differentia- tion by treatment with erythropoietin respond by in- creasing the rates of iron uptake and hemoglobin syn- thesis.
Study of the enzymes of heme biosynthesis dur- ing erythroid differentiation suggests that induction of heme synthesis in these cells is regulated by synthesis of porphobilinogen deaminase.
The activities of &ami. differentiation, including human embryonic stem cells forced to erythroid differentiation, K and UT-7 cells induced to hemoglobin production by chemical compounds, erythropoietin-treated erythroid.
Erythropoietin (Ep) regulates the proliferation and differentiation of erythroid progenitor cells, but whether it functions solely as a survival factor or also acts as a mitogen is unresolved. Activity of the erythroid-specific ALAS isoform (ALAS2) along with erythroid iron uptake have determining regulatory roles in heme biosynthesis [1, 3].
It is, in fact, the coordination between iron acquisition, heme biosynthesis and globin synthesis that makes erythropoiesis possible . Receptors for Erythropoietin Distribution, Structure, and Role in Receptor-Mediated Endocytosis in Erythroid Cells E.,On the mechanism of erythropoietin-induced differentiation.
XII. A cytoplasmatic protein mediating induced nuclear RNA synthesis, Dev. Biol. – and Sawada, K.-I.,The role of erythropoietin in Cited by: Ca2+ may also be involved in the induction of differentiation by erythropoietin.
An increase in RNA synthesis due to activation of transcription is one of the earliest recognized effects of the.
Erythropoietin stimulates the rate of RNA synthesis by fetal mouse liver erythroid cell cultures. This effect is demonstrable prior to hormone-mediated effects on DNA synthesis. Truncated HS1 Inhibits Erythroid Differentiation and Proliferation. Because tHS1 had a major effect on the phenotype of J2E cells, the effect of this mutant on erythroid differentiation was examined.
Strikingly, hemoglobin synthesis was severely repressed in each of the JDs clones studied (Fig.4 A). Production of the oxygen carrier was.
Erythropoietin (EPO) and its receptor, EPOR, were originally named because of their pivotal contribution to hematopoiesis, but over the last ~20 years, their important role also in the nervous Cited by: Harrison, P.
R., Conkie, D. and Paul, J. () Role of cell division and nucleic acid synthesis in erythropoietin-induced maturation of foetal liver cells in vitro.
Brit. Brit. : John Paul. Differentiation of erythroid cells. (A) Erythroid cells differentiate from hematopoietic stem cells (HSC) in the bone marrow. The long-term HSCs successively differentiate into the multipotent progenitors CLP (common lymphoid progenitors) and CMPs (common myeloid progenitors).
The CMPs differentiate. These data indicate for the first time an essential role for lyn in erythropoietin‐initiated differentiation of J2E cells but not in the maintenance of cell viability. Introduction Lyn is a member of the src family of intracellular membrane‐associated tyrosine kinases (Yamanashi et al., ).Cited by: GATA family members GATA-1 and GATA-2 have the opposite activity and promote differentiation along the erythroid lineage.
In the following, the role of transcription factors, chromatin structure alterations, and noncoding RNA during the process of erythroid differentiation will be described. Without erythropoietin (epo), pluripotent stem cells in an erythroid-inductive microenvironment develop into microscopic colonies of apparently undifferentiated cells (4, 8).
In the mouse spleen, erythroid colonies outnumber granulocytic colonies 3 to 1 whereas, in the bone marrow, granulocytic colonies outnumber erythroid colonies 2 to 1 (8).Cited by: 1.
Survival and proliferative roles of erythropoietin beyond the erythroid lineage. Noguchi CT 1, During erythroid differentiation of haematopoietic stem cells, EPO acts through binding of (EPAS-1) by the use of RNA interference: erythropoietin is a HIF-2alpha target gene in Hep3B and Kelly cells.
Faseb J. ; – Exogenous synthetic C2- and C6-ceramide as well as bacterial SMase inhibited erythroid differentiation in erythropoietin-induced (Epo)CD34/HSPCs shown by the analysis of various erythroid by: 4.The erythropoietin receptor (EpoR) is a protein that in humans is encoded by the EPOR gene.
EpoR is a 52kDa peptide with a single carbohydrate chain resulting in a n approximately kDa protein found on the surface of EPO responding cells. It is a member of the cytokine receptor family. EpoR pre-exists as dimers which upon binding of a 30 kDa ligand erythropoietin (Epo), changes its Aliases: EPOR, EPO-R, erythropoietin receptor.