## Abstract We have previously shown that HeLa cells express P2Y~2~ and P2Y~6~ receptors endogenously and determined the pathways by which the P2Y~2~ controls proliferation and Na^+^/K^+^ATPase activity. Our objective in this study was to investigate the hypothesis that P2Y~6~ also controls prolife
The role of protein kinase C in the regulation of extracellular signal-regulated kinase by the T cell antigen receptor
โ Scribed by Manolo Izquierdo; Sally J. Leevers; David H. Williams; Chris J. Marshall; Arthur Weiss; Doreen Cantrell
- Publisher
- John Wiley and Sons
- Year
- 1994
- Tongue
- English
- Weight
- 820 KB
- Volume
- 24
- Category
- Article
- ISSN
- 0014-2980
No coin nor oath required. For personal study only.
โฆ Synopsis
The role of protein kinase C in the regulation of extracellular signal-regulated kinase by the T cell antigen receptor
The aim of this study was to explore the role of protein kinase C (PKC) in the activation of mitogen-activated protein kinases (MAPK) in T lymphocytes. The MAPK extracellular signal-regulated kinase-2 (ERK2) is activated in response to phorbol esters which stimulate PKC, by transient expression of a constitutively active ras mutant, by cell activation via the G protein-coupled type 1 muscarinic acetylcholine receptor (HMlR) or in response to triggering of the T cell antigen receptor (TCR). The relative contribution of PKC to TCR and HMlR regulation of ERK2 was explored by examining the effects of a PKC inhibitor (Ro 31-8425) on ERK2 activation. The data demonstrate that phorbol ester and HMlR regulation of ERK2 was prevented by the PKC inhibitor, but that the inhibitor had no effect on ERK2 activation induced by expression of a constitutively active ras mutant p2lv-Ha-ras. Furthermore, the TCR stimulates both PKC and p21ras but TCR regulation of ERK2 was only weakly suppressed by the PKC inhibitor. These data indicate that PKC has a potential but not a predominant role in TCR regulation of ERK2.
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