Sphingosylphosphorylcholine generates reactive oxygen species through calcium-, protein kinase C delta- and phospholipase D-dependent pathways
SCIE
SCOPUS
- Title
- Sphingosylphosphorylcholine generates reactive oxygen species through calcium-, protein kinase C delta- and phospholipase D-dependent pathways
- Authors
- Jeon, ES; Kang, YJ; Song, HY; Im, DS; Kim, HS; Ryu, SH; Kim, YK; Kim, JH
- Date Issued
- 2005-06
- Publisher
- ELSEVIER SCIENCE INC
- Abstract
- Sphingosylphosphorylcholine (SPC) is a bioactive lipid molecule involved in numerous biological processes. Treatment of MS1 pancreatic islet endothelial cells with SPC increased phospholipase D (PLD) activity in a time- and dose-dependent manner. In addition, treatment of the MS1 cells with 10 mu M SPC induced stimulation of phospholipase C (PLC) activity and transient elevation of intracellular Ca2+. The SPC-induced PLD activation was prevented by pretreatment of the NISI cells with a PLC inhibitor, U73122, and an intracellular Ca2+ -chelating agent, BAPTA-AM. This suggests that PLC-dependent elevation of intracellular Ca2+ is involved in the SPC-induced activation of PLD. The SPC-dependent PLD activity was also almost completely prevented by pretreatment with pan-specific PKC inhibitors, GF109203X and RO31-8220, and with a PKC delta-specific inhibitor, rottlerin, but not by pretreatment with GO6976, a conventional PKC isozymes-specific inhibitor. Adenoviral overexpression of a kinase-deficient mutant of PKC delta attenuated the SPC-induced PLD activity. These results suggest that PKC delta plays a crucial role for the SPC-induced PLD activation. The SPC-induced PLD activation was preferentially potentiated in COS-7 cells transfected with PLD2 but not with PLD1, suggesting a specific implication of PLD2 in the SPC-induced PLD activation. SPC treatment induced phosphorylation of PLD2 in COS-7 cells, and overexpression of the kinase-deficient mutant of PKC delta prevented the SPC-induced phosphorylation of PLD2. Furthermore, SPC treatment generated reactive oxygen species (ROS) in MS1 cells and the SPC induced production of ROS was inhibited by pretreatment with U73122, BAPTA-AM, and rottlerin. In addition, pretreatment with a PLD inhibitor 1-butanol and overexpression of a lipase-inactive mutant of PLD2 but not PLD1 attenuated the SPC-induced generation of ROS. These results suggest that PLC-, Ca2+-, PKC delta-, and PLD2-dependent pathways are essentially required for the SPC induced ROS generation. (c) 2004 Elsevier Inc. All rights reserved.
- Keywords
- PLD; PKC delta; calcium; ROS; SPC; ADP-RIBOSYLATION FACTOR; SMOOTH-MUSCLE-CELLS; BRONCHIAL EPITHELIAL-CELLS; ANGIOTENSIN-II; NADPH OXIDASE; GROWTH-FACTOR; HUMAN NEUTROPHILS; COUPLED RECEPTOR; PC12 CELLS; ACTIVATION
- URI
- https://oasis.postech.ac.kr/handle/2014.oak/24723
- DOI
- 10.1016/j.cellsig.2004.11.004
- ISSN
- 0898-6568
- Article Type
- Article
- Citation
- CELLULAR SIGNALLING, vol. 17, no. 6, page. 777 - 787, 2005-06
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- There are no files associated with this item.
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