Activation of Phospholipase D in Chinese Hamster Ovary Cells Expressing Platelet-Activating Factor Receptor

阅读量：

作者：

B, Liu，S, Nakashima，H, Kanoh，T, Takano，T, Shimizu，Y, Nozawa

展开

摘要：

Platelet-activating factor (PAF) activated phospholipase D (PLD) in WT-H cells, CHO cells stably expressing cloned guinea-pig PAF receptor. The PLD activation was found to be dependent on extracellular Ca2+, protein kinase C (PKC), and a currently unidentified protein tyrosine kinase (PTK). PTK inhibitors ST-638 and genistein inhibited PLD activation induced by PAF as well as phorbol myristate acetate, indicating that PTK acts downstream of PKC. Furthermore, activation of MAP (mitogen-activated protein) kinases, as assessed by their phosphorylation, was also dependent on Ca2+, PKC, and PTK. The correlation between PLD activity and MAP kinase activation, together with the previously observed MAP kinase activation associated with arachidonic acid release by cPLA2 [Honda et al. (1994) J. Biol. Chem. 269, 2307-2315], led us to examine the involvement of MAP kinase in PLD activation. The results indicate that PLD and MAP kinases are activated through the common pathway consisting of Ca2+, PKC, and the unidentified PTK, which act in parallel, but not in a linear sequence.

展开

关键词：

MAP KINASE PHOSPHOLIPASE D PLATELET-ACTIVATING FACTOR PROTEIN KINASE C

DOI：

10.1093/oxfordjournals.jbchem.a124611

被引量：

年份：

1994