Gene interactions and pathways from curated databases and text-mining

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EPO — IL2

Text-mined interactions from Literome

Bryl et al., Artif Organs 1999 (Chronic Disease...) : Recombinant human erythropoietin stimulates production of interleukin 2 by whole blood cell cultures of hemodialysis patients
Hoenstein et al., Cell Immunol 2001 (Hypersensitivity, Immediate) : A significant increase of EPO release was induced by IL-2 , IFN-gamma, and GM-CSF after 18 h in culture
Fandrey et al., Ann N Y Acad Sci 1991 (Carcinoma, Hepatocellular...) : A dose dependent decrease of up to 60 % in Epo production was induced by interleukin-1 beta, interleukin-1 alpha, and tumor necrosis factor-alpha ( in that order of potency )
Ghinassi et al., Exp Hematol 2007 : These results suggest that interleukin-3 and erythropoietin cooperate to establish the lineage-specific transcription factor milieu of erythroid cells : interleukin-3 regulates mainly gene transcription and erythropoietin consistently increases mRNA and protein stability
Lifshitz et al., Haematologica 2010 : The macrophages derived in-vitro from bone marrow cells expressed erythropoietin receptor transcripts, and in-vitro stimulation with erythropoietin activated multiple signaling pathways, including signal transducer and activator of transcription ( STAT ) 1 and 5, mitogen activated protein kinase, phosphatidylinositol 3-kinase and nuclear factor kappa B. In-vitro erythropoietin treatment of these cells up-regulated their surface expression of CD11b, F4/80 and CD80, enhanced their phagocytic activity and nitric oxide secretion, and also led to augmented interleukin 12 secretion and decreased interleukin 10 secretion in response to lipopolysaccharide
Barber et al., Mol Cell Biol 1994 : Immune complex kinase assays confirmed that IL-2 and IL-4 activated JAK1 and EPO activated JAK2
Chiba et al., Nature 1993 : Interleukin-3 and erythropoietin , however, induce transient tyrosine phosphorylation of a common set of proteins as a growth signal, and interleukin-2 induces phosphorylation of an overlapping but distinct set of proteins