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Protein tyrosine phosphorylation and activation of primary response genes by interleukin 11 in B9-TY1 cells.
Cell Growth Differ. 1993 Jul; 4(7):603-9.CG

Abstract

Interleukin (IL) 11 is a multifunctional cytokine derived from bone marrow stromal cells. To understand the mechanisms by which IL-11 exerts its pleiotropic actions, we have analyzed IL-11-mediated signal transduction pathways in IL-11-dependent B9-TY1, which is a subclone of an IL-6-dependent B-cell hybridoma, B9. IL-11 stimulation of B9-TY1 cells resulted in tyrosine phosphorylation of a 97/95 kilodalton cellular protein in a dose-dependent manner, and this effect was inhibited by tyrosine kinase inhibitors genistein and herbimycin A, but not by a serine/threonine kinase inhibitor, H7. We next examined the early nuclear events in the IL-11-triggered intracellular signaling cascade. The data showed that tis11, tis21, and junB early response genes were rapidly activated following IL-11 treatment. The kinetic studies indicated that activation of tis11 and junB genes peaked at 30-60 min and then declined slowly afterward. The tis21 gene was constitutively expressed, and the level of tis21 mRNA was significantly increased and maintained at the elevated level following IL-11 stimulation. Inhibitor studies with genistein, herbimycin A, and H7 revealed that tyrosine kinases and H7-sensitive serine/threonine kinases are required for the IL-11-mediated activation of tis11, tis21, and junB genes. Using a variety of known protein kinase inhibitors or activators, we have demonstrated that H7-sensitive protein kinases activated by IL-11 are distinct from those of well-characterized protein kinase-second messenger systems.(

ABSTRACT

TRUNCATED AT 250 WORDS)

Authors+Show Affiliations

Department of Medicine (Hematology/Oncology), Indiana University School of Medicine, Indianapolis 46202.No affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, P.H.S.

Language

eng

PubMed ID

8398901

Citation

Yin, T, and Y C. Yang. "Protein Tyrosine Phosphorylation and Activation of Primary Response Genes By Interleukin 11 in B9-TY1 Cells." Cell Growth & Differentiation : the Molecular Biology Journal of the American Association for Cancer Research, vol. 4, no. 7, 1993, pp. 603-9.
Yin T, Yang YC. Protein tyrosine phosphorylation and activation of primary response genes by interleukin 11 in B9-TY1 cells. Cell Growth Differ. 1993;4(7):603-9.
Yin, T., & Yang, Y. C. (1993). Protein tyrosine phosphorylation and activation of primary response genes by interleukin 11 in B9-TY1 cells. Cell Growth & Differentiation : the Molecular Biology Journal of the American Association for Cancer Research, 4(7), 603-9.
Yin T, Yang YC. Protein Tyrosine Phosphorylation and Activation of Primary Response Genes By Interleukin 11 in B9-TY1 Cells. Cell Growth Differ. 1993;4(7):603-9. PubMed PMID: 8398901.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Protein tyrosine phosphorylation and activation of primary response genes by interleukin 11 in B9-TY1 cells. AU - Yin,T, AU - Yang,Y C, PY - 1993/7/1/pubmed PY - 1993/7/1/medline PY - 1993/7/1/entrez SP - 603 EP - 9 JF - Cell growth & differentiation : the molecular biology journal of the American Association for Cancer Research JO - Cell Growth Differ VL - 4 IS - 7 N2 - Interleukin (IL) 11 is a multifunctional cytokine derived from bone marrow stromal cells. To understand the mechanisms by which IL-11 exerts its pleiotropic actions, we have analyzed IL-11-mediated signal transduction pathways in IL-11-dependent B9-TY1, which is a subclone of an IL-6-dependent B-cell hybridoma, B9. IL-11 stimulation of B9-TY1 cells resulted in tyrosine phosphorylation of a 97/95 kilodalton cellular protein in a dose-dependent manner, and this effect was inhibited by tyrosine kinase inhibitors genistein and herbimycin A, but not by a serine/threonine kinase inhibitor, H7. We next examined the early nuclear events in the IL-11-triggered intracellular signaling cascade. The data showed that tis11, tis21, and junB early response genes were rapidly activated following IL-11 treatment. The kinetic studies indicated that activation of tis11 and junB genes peaked at 30-60 min and then declined slowly afterward. The tis21 gene was constitutively expressed, and the level of tis21 mRNA was significantly increased and maintained at the elevated level following IL-11 stimulation. Inhibitor studies with genistein, herbimycin A, and H7 revealed that tyrosine kinases and H7-sensitive serine/threonine kinases are required for the IL-11-mediated activation of tis11, tis21, and junB genes. Using a variety of known protein kinase inhibitors or activators, we have demonstrated that H7-sensitive protein kinases activated by IL-11 are distinct from those of well-characterized protein kinase-second messenger systems.(ABSTRACT TRUNCATED AT 250 WORDS) SN - 1044-9523 UR - https://www.unboundmedicine.com/medline/citation/8398901/Protein_tyrosine_phosphorylation_and_activation_of_primary_response_genes_by_interleukin_11_in_B9_TY1_cells_ L2 - http://cgd.aacrjournals.org/cgi/pmidlookup?view=long&pmid=8398901 DB - PRIME DP - Unbound Medicine ER -