Interleukin (IL)‐2 activation of p21ras in murine myeloid cells transfected with human IL‐2 receptor β chain

Manuel Izquierdo (Lead / Corresponding author), Julian Downward, Hiroki Otani, Warren J. Leonard, Doreen A. Cantrell

    Research output: Contribution to journalArticle

    26 Citations (Scopus)

    Abstract

    The T cell growth factor interleukin‐2 (IL‐2) induces p21ras activation in T lymphocytes. To determine whether the IL‐2 receptor (IL‐2R) can regulate p21ras when expressed in a non‐T cell environment we have examined the ability of IL‐2 to activate p21ras in 32D murine myeloid progenitor cells transduced with human IL‐2R β chains. These cells are denoted β53 cells. 32D cells normally proliferate in response to IL‐3 but the expression of the IL‐2R β chain confers IL‐2 responsiveness to the cells. Our data show that IL‐3 is able to activate p21ras in the parental 32D cells and both IL‐2 and IL‐3 can stimulate p21ras in the IL‐2R‐expressing β53 clone of 32D. In T lymphocytes, activation of protein kinase C (PKC) with phorbol esters is sufficient to stimulate p21ras. However, in 32D and β53 cells activation of PKC with phorbol esters does not result in p21ras activation even though these cells express functional PKC. It appears, therefore, that a PKC‐mediated pathway for p21ras regulation exists in T lymphocytes but not in 32D cells. The IL‐2R can couple to p21ras independently of the concomitant presence of the PKC pathway for p21ras regulation. These data imply that multiple intracellular mechanisms may exist to regulate p21ras and that cells of different lineages may differ with regard to p21ras regulation.

    Original languageEnglish
    Pages (from-to)817-821
    Number of pages5
    JournalEuropean Journal of Immunology
    Volume22
    Issue number3
    DOIs
    Publication statusPublished - Mar 1992

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