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IL-2 signaling in human monocytes involves the phosphorylation and activation of p59(hck)

  1. Author:
    Bosco, M. C.
    Curiel, R. E.
    Zea, A. H.
    Malabarba, M. G.
    Ortaldo, J. R.
    Espinoza-Delgado, I.

  2. Author Address

    Espinoza-Delgado I Louisiana State Univ, Med Ctr, Dept Med 1542 Tulane Ave,Suite 604K New Orleans, LA 70112 USA Louisiana State Univ, Med Ctr, Dept Med New Orleans, LA 70112 USA Louisiana State Univ, Med Ctr, Dept Microbiol New Orleans, LA 70112 USA Louisiana State Univ, Med Ctr, Stanley S Scott Canc Ctr New Orleans, LA 70112 USA Ist Giannina Gaslini, Mol Biol Lab I-16148 Genoa Italy NCI, Frederick Canc Res & Dev Ctr, Cytokines Mol Mech Sect, Frederick Canc Res & Dev Ctr Frederick, MD 21702 USA
    1. Year: 2000
  2. Journal: Journal of Immunology
    1. 164
    2. 9
    3. Pages: 4575-4585
  4. Type of Article: Article
  1. Abstract:

    The activating properties of IL-2 and the structure of the IL-2R on human monocytes are web characterized. However, relatively little is known about the biochemical mechanisms involved in IL-2 signal transduction in these cells. We investigated the role of protein tyrosine kinases (PTKs) in the activation of monocytes by IL-2. Incubation of monocytes with the PTK inhibitor herbimycin A (HA) resulted in the dose-dependent suppression of IL-2-induced monocyte tumoricidal activity. This inhibition was rather potent, as a concentration of HA as low as 0.5 mu M caused a complete abrogation of cytolytic activity. Furthermore, HA markedly suppressed the ability of IL-2 to induce IL-1 beta, TNF-alpha, IL-6, and IL-8 mRNA expression and protein secretion by monocytes. Anti-phosphotyrosine immunoblotting demonstrated that IL-2 induced a rapid and time-dependent increase in tyrosine phosphorylation of several cellular proteins of molecular masses ranging from 35 to 180 kDa. Interestingly, IL-2 caused a significant up-regulation of the constitutive levels of hck PTK mRNA and protein relative to medium-treated cells as well as an increase in p59(hck) tyrosine phosphorylation. Finally, we demonstrated by in vitro kinase assay that the specific activity of p59(hck) PTK was also induced by IL-2 in monocytes. Thus, these data show that the activation of PTKs is required for the triggering of monocyte effector and secretory functions by IL-2 and strongly suggest that p59(hck) is a key participant in IL-2 signaling ih human monocytes. The Journal of Immunology, 2000, 164: 4575-4585. [References: 62]

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