caa a22 4500 397556330 CHVBK 20180308164803.0 cr unu---uuuuu 161202e199609 xx s 000 0 eng 10.1093/oxfordjournals.jbchem.a021457 doi (NATIONALLICENCE)oxford-10.1093/oxfordjournals.jbchem.a021457 Importance of the Phospholipase D-Initiated Sequential Pathway for Arachidonic Acid Release and Prostaglandin D2 Generation by Rat Peritoneal Mast Cells [Elektronische Daten] [Tsuyoshi Ishimoto, Satoshi Akiba, Takashi Sato] The association of prostaglandin D2 (PGD2) production as well as arachidonic acid release with the phospholipase D (PLD)-linked mechanism was studied in rat peritoneal mast cells. Stimulation of mast cells with cross-linking of the high-affinity Fc receptor for IgE caused increases in the release of arachidonic acid and PGD2, which are suppressed almost completely by ethanol or RHC 80267, a diacylglycerol lipase inhibitor. Ethanol did not influence inositol phosphate release in response to an antigen. An increase in diacylglycerol, that is inhibited by propranolol, was observed, with a peak within 1 min. Antigen stimulation induced little production of lysophosphatidylcholine, while ionomycin as a control markedly induced the production. However, the phospholipase A2 (PLA2) activity in the cytosol of antigen-stimulated cells increased to the level in ionomycin-stimulated cells. The addition of the ADP-ribosylation factor-containing fraction prepared from bovine brain, that is known to specifically activate PLD, to permeabilized mast cells in the presence of GTPγS, apparently increased arachidonic acid and PGD2 release, but not in the presence of ethanol. Furthermore, arachidonic acid release by an antigen was enhanced by melittin, that activates PLA2, but PGD2 production was not. These results suggest that antigen-stimulated PGD2 production as well as arachidonic acid release are strongly associated with the sequential PLD-linked pathway. © 1996 BY THE JOURNAL OF BIOCHEMISTRY Regular Papers nationallicence arachidonic acid nationallicence mast cell nationallicence phospholipase A2 nationallicence phospholipase D nationallicence prostaglandin D2 nationallicence Ishimoto Tsuyoshi Department of Pathological Biochemistry, Kyoto Pharmaceutical University, Misasagi, Yamashina-ku, Kyoto, Kyoto 607 aut Akiba Satoshi Department of Pathological Biochemistry, Kyoto Pharmaceutical University, Misasagi, Yamashina-ku, Kyoto, Kyoto 607 aut Sato Takashi Department of Pathological Biochemistry, Kyoto Pharmaceutical University, Misasagi, Yamashina-ku, Kyoto, Kyoto 607 aut The Journal of Biochemistry Oxford University Press 120/3(1996-09), 616-623 0021-924X 120:3<616 1996 120 jbchem https://doi.org/10.1093/oxfordjournals.jbchem.a021457 text/html Onlinezugriff via DOI 1 other jats NATIONALLICENCE 856 40 https://doi.org/10.1093/oxfordjournals.jbchem.a021457 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Ishimoto Tsuyoshi Department of Pathological Biochemistry, Kyoto Pharmaceutical University, Misasagi, Yamashina-ku, Kyoto, Kyoto 607 aut NATIONALLICENCE 700 1- Akiba Satoshi Department of Pathological Biochemistry, Kyoto Pharmaceutical University, Misasagi, Yamashina-ku, Kyoto, Kyoto 607 aut NATIONALLICENCE 700 1- Sato Takashi Department of Pathological Biochemistry, Kyoto Pharmaceutical University, Misasagi, Yamashina-ku, Kyoto, Kyoto 607 aut NATIONALLICENCE 773 0- The Journal of Biochemistry Oxford University Press 120/3(1996-09), 616-623 0021-924X 120:3<616 1996 120 jbchem Metadata rights reserved CC BY-NC-4.0 http://creativecommons.org/licenses/by-nc/4.0 nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-oxford