Summary
We have recently shown that activation of protein kinase C by tumour promoting phorbolesters, such as 4β-β-phorbol-12,13-dibutyrate, stimulates adenosine-induced accumulation of cAMP in 7urkat cells, a human T-leukaemia line. Activating the CD3 complex associated with the T-cell receptor by means of the monoclonal antibody OKT3 caused a concentration-dependent accumulation of inositol phosphates and an increase in the phosphorylation of an endogenous protein kinase C substrate. OKT3 also mimicked the previously reported effects of protein kinase C since it potentiated the cAMP stimulation by either an adenosine analogue, NECA, or cholera toxin. Thus, our results indicate that stimulation of a receptor activating phospholipase C and protein kinase C can secondarily enhance the action of agonists that act on adenylate cyclase-coupled receptors.
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Abbreviations
- cAMP:
-
cyclic adenosine-monophosphate
- NECA:
-
5′-N-ethylcarboxyamido adenosine
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The present study was supported by grants from The Swedish Cancer Association, The Swedish Medical Research Council (project no. 2553), by Gustaf V 80 Years Fund, by Nanna Swartz foundation and by Karolinska Institutet
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Kvanta, A., Nordstedt, C., Jondal, M. et al. Activation of protein kinase C via the T-cell receptor complex potentiates cyclic AMP responses in T-cells. Naunyn-Schmiedeberg's Arch Pharmacol 340, 715–717 (1989). https://doi.org/10.1007/BF00169679
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DOI: https://doi.org/10.1007/BF00169679