Abstract
Interleukin-9 (IL-9) stimulation results in JAK, STAT and IRS1/2 phosphorylation. The role of IRS adaptor proteins in IL-9 signaling is not clear. We show that IL-9 induces IRS2 phosphorylation and association with phosphatidylinositol-3 kinase (PI 3-K) p85 subunit in TS1 cells and BaF/9R cells, which proliferate upon IL-9 stimulation. We observed a PI 3-K-dependent phosphorylation of protein kinase B (PKB) in TS1 cells, but not in BaF/9R, nor in other IL-9-dependent cell lines. Finally, 32D cells that were transfected with the IL-9 receptor but lack IRS expression survived in the presence of IL-9. Ectopic IRS1 expression allowed for IL-9-induced proliferation, in the absence of significant PKB phosphorylation.
Publication types
-
Research Support, Non-U.S. Gov't
MeSH terms
-
Animals
-
Cell Division / physiology*
-
Cells, Cultured
-
Extracellular Matrix Proteins / metabolism
-
Humans
-
Insulin Receptor Substrate Proteins
-
Interleukin-9 / physiology*
-
Intracellular Signaling Peptides and Proteins
-
Mice
-
Phosphatidylinositol 3-Kinases / metabolism
-
Phosphoproteins / biosynthesis
-
Phosphoproteins / physiology*
-
Phosphorylation
-
Protein Serine-Threonine Kinases*
-
Proto-Oncogene Proteins / metabolism
-
Proto-Oncogene Proteins c-akt
Substances
-
ECM1 protein, human
-
Ecm1 protein, mouse
-
Extracellular Matrix Proteins
-
IRS2 protein, human
-
Insulin Receptor Substrate Proteins
-
Interleukin-9
-
Intracellular Signaling Peptides and Proteins
-
Irs2 protein, mouse
-
Phosphoproteins
-
Proto-Oncogene Proteins
-
Protein Serine-Threonine Kinases
-
Proto-Oncogene Proteins c-akt