Regulation of phospholipase D2 by H2O2 in PC12 cells

被引:26
作者
Oh, SO
Hong, JH
Kim, YR
Yoo, HS
Lee, SH
Lim, K
Hwang, BD
Exton, JH
Park, SK
机构
[1] Chungnam Natl Univ, Coll Med, Dept Biochem, Taejon, South Korea
[2] Chungnam Natl Univ, Coll Med, Dept Pharmacol, Taejon, South Korea
[3] Korea Res Inst Biol & Biotechnol, Taejon, South Korea
[4] Pusan Natl Univ, Coll Med, Dept Physiol, Pusan 609735, South Korea
[5] Vanderbilt Univ, Sch Med, Howard Hughes Med Inst, Dept Mol Physiol & Biophys, Nashville, TN 37212 USA
关键词
phospholipase D2; hydrogen peroxide; PC12; cells; protein kinase C; calcium;
D O I
10.1046/j.1471-4159.2000.0752445.x
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Phospholipase D2 (PLD2) is expressed in brain and inhibited by synuclein, which is involved in Parkinson's and Alzheimer's diseases. However, the activation mechanism of PLD2 in neuronal cells has not been defined clearly. Hydrogen peroxide (H2O2) plays roles in the neurodegenerative diseases and also acts as a second messenger of various molecules such as nerve growth factor. To study regulation mechanisms of PLD2 by H2O2 in neuronal cells, we have made stable PC12 cell lines expressing PLD2 (PLD2-PC12 cells). H2O2 treatment stimulated PLD activity in PLD2-PC12 cells in a dose- and time-dependent manner. This activation was inhibited by the treatment with protein kinase C (PKC) inhibitors or by depletion of PKC alpha, -delta, and -epsilon. Phorbol ester markedly activated PLD2, Go-treatment with phorbol ester and H2O2 did not show an additive effect. Chelation of extracellular calcium substantially blocked the H2O2-induced activation of PLD2, A calcium ionophore induced PLD2 activation in a PKC-dependent manner. Protein-tyrosine kinase inhibitors inhibited H2O2-induced PLD activation slightly. These data indicate that H2O2 can activate PLD2 in PC12 cells and that this activation is largely dependent on PKC and Ca2+ ions and minimally dependent on tyrosine phosphorylation.
引用
收藏
页码:2445 / 2454
页数:10
相关论文
共 48 条
[1]   Epidermal growth factor (EGF)-induced generation of hydrogen peroxide - Role in EGF receptor-mediated tyrosine phosphorylation [J].
Bae, YS ;
Kang, SW ;
Seo, MS ;
Baines, IC ;
Tekle, E ;
Chock, PB ;
Rhee, SG .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1997, 272 (01) :217-221
[2]   PHOSPHOLIPASE D ACTIVATION BY THE MITOGENS PLATELET-DERIVED GROWTH-FACTOR AND 12-O-TETRADECANOYLPHORBOL 13-ACETATE IN NIH-3T3 CELLS [J].
BENAV, P ;
LISCOVITCH, M .
FEBS LETTERS, 1989, 259 (01) :64-66
[3]   THE REGULATION AND CELLULAR FUNCTIONS OF PHOSPHATIDYLCHOLINE HYDROLYSIS [J].
BILLAH, MM ;
ANTHES, JC .
BIOCHEMICAL JOURNAL, 1990, 269 (02) :281-291
[4]  
BOCCKINO SB, 1987, J BIOL CHEM, V262, P15309
[5]  
BOURGOIN S, 1992, J BIOL CHEM, V267, P11908
[6]   Synaptojanin inhibition of phospholipase D activity by hydrolysis of phosphatidylinositol 4,5-bisphosphate [J].
Chung, JK ;
Sekiya, F ;
Kang, HS ;
Lee, CH ;
Han, JS ;
Kim, SR ;
Bae, YS ;
Morris, AJ ;
Rhee, SG .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1997, 272 (25) :15980-15985
[7]   Phospholipase D2, a distinct phospholipase D isoform with novel regulatory properties that provokes cytoskeletal reorganization [J].
Colley, WC ;
Sung, TC ;
Roll, R ;
Jenco, J ;
Hammond, SM ;
Altshuller, Y ;
BarSagi, D ;
Morris, AJ ;
Frohman, MA .
CURRENT BIOLOGY, 1997, 7 (03) :191-201
[8]   EPIDERMAL GROWTH-FACTOR INCREASES SN-1,2-DIACYLGLYCEROL LEVELS AND ACTIVATES PHOSPHOLIPASE D-CATALYZED PHOSPHATIDYLCHOLINE BREAKDOWN IN SWISS 3T3 CELLS IN THE ABSENCE OF INOSITOL-LIPID HYDROLYSIS [J].
COOK, SJ ;
WAKELAM, MJO .
BIOCHEMICAL JOURNAL, 1992, 285 :247-253
[9]   PHOSPHOLIPASE-D ACTIVITY IN PHAGOCYTIC LEUKOCYTES IS SYNERGISTICALLY REGULATED BY G-PROTEIN-BASED AND TYROSINE KINASE-BASED MECHANISMS [J].
DUBYAK, GR ;
SCHOMISCH, SJ ;
KUSNER, DJ ;
XIE, MS .
BIOCHEMICAL JOURNAL, 1993, 292 :121-128
[10]   Messenger functions of phosphatidic acid [J].
English, D ;
Cui, Y ;
Siddiqui, RA .
CHEMISTRY AND PHYSICS OF LIPIDS, 1996, 80 (1-2) :117-132