Abstract
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 language | English |
|---|---|
| Pages (from-to) | 373-379 |
| Number of pages | 7 |
| Journal | Scandinavian Journal of Immunology |
| Volume | 39 |
| Issue number | 4 |
| DOIs | |
| Publication status | Published - 1994 |
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ASJC Scopus subject areas
- Immunology
Cite this
Characterization of a cyclosporin A-sensitive activation pathway in cultured T and natural killer cells. / Cantoni, C.; Cambiaggi, A.; Sforzini, S.; Poggi, A.; Viale, M.; Biassoni, R.; Ferrini, S.
In: Scandinavian Journal of Immunology, Vol. 39, No. 4, 1994, p. 373-379.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Characterization of a cyclosporin A-sensitive activation pathway in cultured T and natural killer cells
AU - Cantoni, C.
AU - Cambiaggi, A.
AU - Sforzini, S.
AU - Poggi, A.
AU - Viale, M.
AU - Biassoni, R.
AU - Ferrini, S.
PY - 1994
Y1 - 1994
N2 - 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.
AB - 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.
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UR - http://www.scopus.com/inward/citedby.url?scp=0028244503&partnerID=8YFLogxK
U2 - 10.1111/j.1365-3083.1994.tb03388.x
DO - 10.1111/j.1365-3083.1994.tb03388.x
M3 - Article
C2 - 8146596
AN - SCOPUS:0028244503
VL - 39
SP - 373
EP - 379
JO - Scandinavian Journal of Immunology
JF - Scandinavian Journal of Immunology
SN - 0300-9475
IS - 4
ER -