Open AccessBreakdown of Phosphatidylinositol during the Elicitation of Phytoalexin Production in Cultured Carrot Cells
Author(s) -
Fumiya Kurosaki,
Yutaka Tsurusawa,
Arasuke Nishi
Publication year - 1987
Publication title -
plant physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.554
H-Index - 312
eISSN - 1532-2548
pISSN - 0032-0889
DOI - 10.1104/pp.85.3.601
Subject(s) - elicitor , phytoalexin , phosphatidylinositol , diacylglycerol kinase , second messenger system , protein kinase c , biochemistry , inositol trisphosphate , phospholipase c , inositol , calmodulin , biology , phospholipase , protein kinase a , trifluoperazine , diglyceride , gq alpha subunit , phospholipase a2 , kinase , signal transduction , enzyme , g protein , receptor , resveratrol
Elicitor-induced production of the phytoalexin, 6-methoxymellein, in cultured carrot cells was appreciably depressed by the calmodulin inhibitors N-(6-aminohexyl)-5-chloro-1-naphthalenesulfonamide and trifluoperazine. An inhibitor of Ca(2+)-phospholipid dependent protein kinase (protein kinase C), 1-(5-isoquinolinesulfonyl)-2-methylpiperazine, also inhibited the phytoalexin production in carrot. Both phorbol ester and synthetic diacylglycerol, activators of protein kinase C, showed an ability to induce 6-methoxymellein production even in the absence of elicitor. Phosphatidylinositol-degrading phospholipase activity increased in elicitor-treated carrot cells without a notable lag, and a product of this reaction, inositol trisphosphate, appeared to increase in parallel with the phospholipase activity. These results suggest that breakdown of phosphatidylinositol takes place in the elicitor-treated carrot cells. The messengers liberated from the phospholipid in the plasma membrane may participate in the elicitation process by controlling the activity of protein kinase C-like enzyme(s) and Ca(2+)-mediated processes including calmodulin.