Characterization of a cyclosporin A-sensitive activation pathway in cultured T and natural killer cells

C. Cantoni, A. Cambiaggi, S. Sforzini, A. Poggi, M. Viale, R. Biassoni, S. Ferrini

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Previously, the authors have described a molecule, identified by the LD6 monoclonal antibody (MoAb), present at the cell surface of long-term cultured T and Natural Killer (NK) cells which is involved in cell triggering. In the study described here the authors used biotin surface labelling and immunoprecipitation to show that LD6 MoAb recognizes a surface protein of approximately 65 kDa. In combination with submitogenic concentrations of phorbol esters (PMA), LD6 MoAb was able to induce accumulation of mRNA specific for GM-CSF, γ-IFN and TNF-α and release of these cytokines by LD6+ T-cell lines. Both lymphokine production and lymphokine-specific mRNA accumulation induced by the LD6 MoAb were blocked totally by Cyclosporin A (CsA). To investigate the mechanism(s) of signal transduction through this activatory pathway, the authors performed Ca++ mobilization experiments. The results of these experiments suggested a role for Ca++ in signal transduction. The Ca++ mobilization induced by LD6 MoAb cross-linking could be inhibited totally by the use of pertussis toxin, indicating a possible role for G proteins in signalling through the LD6 MoAb-reactive molecule. Western blot analysis performed with an anti-phosphotyrosine antibody did not suggest that tyrosine kinase activation has a role.

Original languageEnglish
Pages (from-to)373-379
Number of pages7
JournalScandinavian Journal of Immunology
Issue number4
Publication statusPublished - 1994

ASJC Scopus subject areas

  • Immunology


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