Comparison of interleukin 2 and 12-O-tetradecanoyl-phorbol 13-acetate as signals for protein kinase C activation in purified human T lymphocytes
✍ Scribed by Yann Mahé; Jean-Pierre Piau; Naomi Wakasugi; Thomas Tursz; Gerard Gacon; Hiro Wakasugi
- Publisher
- John Wiley and Sons
- Year
- 1988
- Tongue
- English
- Weight
- 835 KB
- Volume
- 18
- Category
- Article
- ISSN
- 0014-2980
No coin nor oath required. For personal study only.
✦ Synopsis
Comparison of interleukin 2 and 12-0-tetradecanoyl-phorboll3-acetate as signals for protein kinase C activation in purified human T lymphocytes*
Interleukin 2 (IL 2) and 12-0-tetradecanoylphorbol 13-acetate (TPA) have been compared for their ability to induce translocation of protein kinase C (PKC) in T lymphocytes prestimulated with anti-CD3 monoclonal antibody (mAb), either in the presence or absence of monocytes. TPA alone did not promote purified T cell growth, but it was able to induce a transient, within 30 min, translocation of PKC activity. The profiles of PKC association with the membrane of the T cells under TPA stimulation were quite similar when either the anti-CD3 mAb or the fixed monocytes, or both, were added to the Tcells. The decrease of cytosolic PKC under TPA stimulation was less pronounced for the purified T cells stimulated with anti-CD3 mAb, fixed monocytes alone or both than for unstimulated purified T cells. Even in the absence of monocytes, the addition of exogenous IL2 to the anti-CD3 mAb-treated T cells resulted in PKC translocation, with a transient increase in the PKC activity found in both the particulate and cytosolic fractions. When exogenous IL2 was added to the proliferating T cells, the association of PKC with the membrane was prolonged and the activity did not reach a plateau during the first 2 h after the IL2 stimulation.
In parallel, the level of PKC associated with the membrane was higher in proliferating cells than in resting cells even 4 days after stimulation. These results suggest that activation of PKC by IL2 might be different from the direct activation of PKC by TPA and that a specific activation pathway, at least kinetically distinct from the classical phosphatidyl inositol diphosphate degradation by phospholipase C, might be involved during IL 2 stimulation of T lymphocytes through high-affinity IL 2 receptors.