We found a match
Your institution may have access to this item. Find your institution then sign in to continue.
- Title
Activation of phospholipase D induced by hydrogen peroxide in suspension-cultured rice cells.
- Authors
Yamaguchi, Takeshi; Tanabe, Shigeru; Minami, Eiichi; Shibuya, Naoto
- Abstract
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.
- Publication
Plant & cell physiology, 2004, Vol 45, Issue 9, p1261
- ISSN
0032-0781
- Publication type
Journal Article
- DOI
10.1093/pcp/pch150