• 主题
高级搜索  >
历史搜索 清空历史
首页> 外文OA文献 >Phospholipase D1 is threonine-phosphorylated in human-airway epithelial cells stimulated by sphingosine-1-phosphate by a mechanism involving Src tyrosine kinase and protein kinase Cdelta.
【2h】

Phospholipase D1 is threonine-phosphorylated in human-airway epithelial cells stimulated by sphingosine-1-phosphate by a mechanism involving Src tyrosine kinase and protein kinase Cdelta.

机译：磷脂酶D1在Src酪氨酸激酶和蛋白激酶Cdelta的作用机制下，在1磷酸鞘氨醇刺激的人道上皮细胞中被苏氨酸磷酸化。

代理获取
本网站仅为用户提供外文OA文献查询和代理获取服务，本网站没有原文。下单后我们将采用程序或人工为您竭诚获取高质量的原文，但由于OA文献来源多样且变更频繁，仍可能出现获取不到、文献不完整或与标题不符等情况，如果获取不到我们将提供退款服务。请知悉。
页面导航
  • 摘要
  • 著录项
  • 相似文献
  • 相关主题

摘要

The regulatory role of protein kinase C (PKC) delta isoform in the stimulation of phospholipase D (PLD) by sphingosine-1-phosphate (SPP) in a human-airway epithelial cell line (CFNPE9o(-)) was revealed by using antisense oligodeoxynucleotide to PKCdelta, in combination with the specific inhibitor rottlerin. Cell treatment with antisense oligodeoxynucleotide, but not with sense oligodeoxynucleotide, completely eliminated PKCdelta expression and resulted in the strong inhibition of SPP-stimulated phosphatidic acid formation. Indeed, among the PKCalpha, beta, delta, epsilon and zeta isoforms expressed in these cells, only PKCdelta was activated on cell stimulation with SPP, as indicated by translocation into the membrane fraction. Furthermore, pertussis toxin and genistein eliminated both PKCdelta translocation and PLD activation. In particular, a significant reduction in phosphatidylbutanol formation by SPP was observed in the presence of 4-amino-5-(4-methylphenyl)-7-(t-butyl) pyrazolo [3,4-d] pyrimidine (PP1), an inhibitor of Src tyrosine kinase. Furthermore, the activity of Src kinase was slightly increased by SPP and inhibited by PP1. However, the level of PKCdelta tyrosine phosphorylation was not increased in SPP-stimulated cells, suggesting that Src did not directly phosphorylate PKCdelta. Finally, the level of serine phosphorylation of PLD1 and PLD2 isoforms was not changed, whereas the PLD1 isoform alone was threonine-phosphorylated in SPP-treated cells. PLD1 threonine phosphorylation was strongly inhibited by rottlerin, by anti-PKCdelta oligodeoxynucleotide and by PP1. In conclusion, in CFNPE9o(-) cells, SPP interacts with a membrane receptor linked to a G(i) type of G-protein, leading to activation of PLD, probably the PLD1 isoform, by a signalling pathway involving Src and PKCdelta.
机译：通过使用反义寡脱氧核苷酸揭示了蛋白激酶C（PKC）δ亚型在鞘氨醇-1-磷酸（SPP）在人气道上皮细胞系（CFNPE9o（-））刺激磷脂酶D（PLD）中的调控作用。 PKCdelta联合特异性抑制剂rottlerin。用反义寡聚脱氧核苷酸而不是有义寡聚脱氧核苷酸进行细胞处理，完全消除了PKCdelta表达，并强烈抑制了SPP刺激的磷脂酸的形成。实际上，在这些细胞中表达的PKCalpha，β，δ，ε和zeta同工型中，只有PKCdelta在用SPP刺激细胞后才被激活，如易位到膜级分中所示。此外，百日咳毒素和金雀异黄素消除了PKCdelta易位和PLD激活。特别地，在存在4-氨基-5-（4-甲基苯基）-7-（叔丁基）吡唑并[3,4-d]嘧啶（PP1）的存在下，通过SPP可以明显减少磷脂酰丁醇形成。 Src酪氨酸激酶抑制剂。此外，Src激酶的活性被SPP略微增加，而被PP1抑制。但是，在SPP刺激的细胞中PKCdelta酪氨酸磷酸化水平并未增加，这表明Src不能直接磷酸化PKCdelta。最后，PLD1和PLD2同工型的丝氨酸磷酸化水平没有改变，而单独的PLD1同工型在经SPP处理的细胞中被苏氨酸磷酸化。 Rottlerin，抗PKCdelta寡脱氧核苷酸和PP1强烈抑制了PLD1苏氨酸的磷酸化。总之，在CFNPE9o（-）细胞中，SPP与与G（i）型G蛋白连接的膜受体相互作用，从而通过涉及Src和PKCdelta的信号传导途径激活PLD（可能是PLD1亚型）。

著录项

相似文献

  • 外文文献
  • 中文文献
  • 专利
代理获取

客服邮箱：kefu@zhangqiaokeyan.com

京公网安备：11010802029741号 ICP备案号：京ICP备15016152号-6 六维联合信息科技 (北京) 有限公司©版权所有

  • 客服微信

  • 服务号