Activation of phospholipase D induced by hydrogen peroxide in suspension-cultured rice cells.
Activation of phospholipase D induced by hydrogen peroxide in suspension-cultured rice cells.
复制标题
DOI：
10.1093/pcp/pch150
复制
发表时间：
2004-09
影响因子：
4.9
通讯作者：
T. Yamaguchi;Shigeru Tanabe;E. Minami;N. Shibuya
中科院分区：
文献类型：
--
作者：
T. Yamaguchi;Shigeru Tanabe;E. Minami;N. Shibuya
过氧化氢（H₂O₂）（10 - 100微摩尔）可诱导悬浮培养的水稻细胞中磷脂酸（PA）快速且短暂地积累。当在1 - 丁醇（0.1%）存在的条件下，对经H₂O₂处理的水稻细胞制备的细胞提取物组分中的磷脂酶活性进行测定时，观察到磷脂酰丁醇（PtdBut）快速且短暂地生成。因此，得出结论：H₂O₂激活的磷脂酶为磷脂酶D（PLD）。此外，H₂O₂可直接在体外诱导未经H₂O₂处理的细胞溶质组分中的PLD激活。在强效蛋白酪氨酸激酶抑制剂拉文达斯汀A（0.05毫摩尔）存在的情况下，PLD的体外和体内激活均被完全抑制。在H₂O₂（10 - 100微摩尔）存在时，由N - 乙酰壳寡糖激发子诱导的植物抗毒素生物合成增强，而在强效超氧阴离子清除剂铁钛试剂、1 - 丁醇（0.1%）和拉文达斯汀A（0.05毫摩尔）存在时，该生物合成受到抑制。这些结果表明，H₂O₂诱导的PLD激活可增强水稻细胞中导致植物抗毒素生物合成的信号转导。
Hydrogen peroxide (H2O2) (10-100 microM) induced rapid and transient accumulation of phosphatidic acid (PA) in suspension-cultured rice cells. When phospholipase activity in the cellular extract fraction prepared from rice cells treated with H2O2 was assayed in the presence of 1-butanol (0.1%), rapid and transient phosphatidylbutanol (PtdBut) formation was observed. Thus, the H2O2-activated phospholipase was concluded to be phospholipase D (PLD). Furthermore, H2O2 directly induced in vitro PLD activation in the cytosolic fraction without H2O2 treatment. In vitro and in vivo activation of PLD were completely suppressed in the presence of lavendustin A (0.05 mM), a potent inhibitor of protein tyrosine kinase. Phytoalexin biosynthesis induced by N-acetylchitooligosaccharide elicitor was enhanced in the presence of H2O2 (10-100 microM), whereas it was suppressed in the presence of tiron, a potent scavenger of O2-, 1-butanol (0.1%) and lavendustin A (0.05 mM). These results indicate that H2O2-inducible PLD activation enhances signal transduction leading to phytoalexin biosynthesis in rice cells.