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Diacylglycerol breakdown in plasma membrane of rat intestinal epithelial cells Effect of E. coli heat‐stable toxin
Author(s) -
Banik Nupur Dey,
Ganguly Uma
Publication year - 1989
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(89)80720-3
Subject(s) - triolein , lipase , diacylglycerol lipase , chemistry , biochemistry , enzyme , diacylglycerol kinase , phospholipase , phospholipase c , glycerol , monoacylglycerol lipase , phospholipase d , glyceride , fatty acid , protein kinase c , endocannabinoid system , receptor
Rat intestinal epithelial cells were isolated and the activity of the enzyme diacylglycerol lipase (DG lipase, EC 3.1.1.3) was investigated. When cells were treated with Escherichia coli heat‐stable toxin (ST) liberation of endogenous glycerol and fatty acids was observed. The enzyme responsible for this effect could be demonstrated to be a DG lipase by using specific substrates. It was found that the activity of DG lipase was increased 5–6‐fold with the substrates diolein and 1,2‐dioleyl‐ rac ‐glycerol and triolein being neutral lipid insensitive to DG lipase. ST had no direct effect on the DG lipase. The enzyme DG lipase was activated via a chain reaction due to the hydrolysis of phosphatidylinositol (PI) by the enzyme PI‐specific phospholipase C stimulated by ST.