ArticleProceedings of the National Academy of Sciences of the United States of America1993
Common elements in interleukin 4 and insulin signaling pathways in factor-dependent hematopoietic cells.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1993. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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Who cites it
36 citing papers in PubMed, 173 citations in OpenAlex.
- The Common Cytokine Receptor γ Chain Family of Cytokines.Cold Spring Harbor perspectives in biology · 2018Review
- IL-4 and IL-13 Receptor Signaling From 4PS to Insulin Receptor Substrate 2: There and Back Again, a Historical View.Frontiers in immunology · 2018Review
- The adaptor protein insulin receptor substrate 2 inhibits alternative macrophage activation and allergic lung inflammation.Science signaling · 2016Article
- Irs2 and Irs4 synergize in non-LepRb neurons to control energy balance and glucose homeostasis.Molecular metabolism · 2014Article
- Brain deletion of insulin receptor substrate 2 disrupts hippocampal synaptic plasticity and metaplasticity.PloS one · 2012Article
- Immune-mediated signaling in intestinal goblet cells via PI3-kinase- and AKT-dependent pathways.American journal of physiology. Gastrointestinal and liver physiology · 2008Article
- Insulin receptor substrate (IRS)-1 regulates murine embryonic stem (mES) cells self-renewal.Journal of cellular physiology · 2007Article
- Transient inhibition of interleukin 4 signaling by T cell receptor ligation.The Journal of experimental medicine · 2000Article
- Cross talk of pp125(FAK) and pp59(Lyn) non-receptor tyrosine kinases to insulin-mimetic signaling in adipocytes.Molecular and cellular biology · 2000Article
- Consequences of Stat6 deletion on Sis/PDGF- and IL-4-induced proliferation and transcriptional activation in murine fibroblasts.Oncogene · 1999Article
- Cytokines in asthma.Thorax · 1999Review
- Insulin-like growth factor I synergizes with interleukin 4 for hematopoietic cell proliferation independent of insulin receptor substrate expression.Molecular and cellular biology · 1999Article
- Molecular mechanisms in T helper phenotype development.Springer seminars in immunopathology · 1999Review
- The IRS-signalling system: a network of docking proteins that mediate insulin action.Molecular and cellular biochemistry · 1998Review
- Regulation of interleukin 4-mediated signaling by naturally occurring dominant negative and attenuated forms of human Stat6.Proceedings of the National Academy of Sciences of the United States of America · 1998Article
- The early intracellular signaling pathway for the insulin/insulin-like growth factor receptor family in the mammalian central nervous system.Molecular neurobiology · 1996Review
- Insulin signalling and insulin actions in the muscles and livers of insulin-resistant, insulin receptor substrate 1-deficient mice.Molecular and cellular biology · 1996Article
- Growth inhibition signalled through the interleukin-4/interleukin-13 receptor complex is associated with tyrosine phosphorylation of insulin receptor substrate-1.The Biochemical journal · 1996Article
- The Drosophila insulin receptor activates multiple signaling pathways but requires insulin receptor substrate proteins for DNA synthesis.Molecular and cellular biology · 1996Article
- Modulation of early steps in insulin action in the liver and muscle of epinephrine treated rats.Endocrine · 1995Article
Corrections and comments
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Authors and funding
10 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Interleukin 4 (IL-4), insulin, and insulin-like growth factor I (IGF-I) efficiently induced DNA synthesis in the IL-3-dependent murine myeloid cell lines FDC-P1 and FDC-P2. Although these factors could not individually sustain long-term growth of these lines, a combination of IL-4 with either insulin or IGF-I did support continuous growth. The principal tyrosine-phosphorylated substrate observed in FDC cells stimulated with IL-4, previously designated 4PS, was of the same size (170 kDa) as the major substrate phosphorylated in response to insulin or IGF-I. These substrates had phosphopeptides of the same size when analyzed by digestion with Staphylococcus aureus V8 protease, and each tightly associated with the 85-kDa component of phosphatidylinositol 3-kinase after factor stimulation. IRS-1, the principal substrate phosphorylated in response to insulin or IGF-I stimulation in nonhematopoietic cells, is similar in size to 4PS. However, anti-IRS-1 antibodies failed to efficiently precipitate 4PS, and some phosphopeptides generated by V8 protease digestion of IRS-1 were distinct in size from the phosphopeptides of 4PS. Nevertheless, IL-4, insulin, and IGF-I were capable of stimulating tyrosine phosphorylation of IRS-1 in FDC cells that expressed this substrate as a result of transfection. These findings indicate that (i) IL-4, insulin, and IGF-I use signal transduction pathways in FDC lines that have at least one major feature in common, the rapid tyrosine phosphorylation of 4PS, and (ii) insulin and IGF-I stimulation of hematopoietic cell lines leads to the phosphorylation of a substrate that may be related to but is not identical to IRS-1.
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