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KMID : 0614019990150010244
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Journal of Pharmaceutical Sciences (C.N.U.)
1999 Volume.15 No. 1 p.244 ~ p.250
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Regulation of Brain Glycosylphosphatidylinositol-Specific Phospholipase D by Natural Amphiphiles
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Lee Ji-Yeon
Lee Hyun-Jeong
Kim Mee-Ree
Myung Pyung-Keun
Sok Dai-Eun
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Abstract
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Brain glycosylphosphatidylinositol-specific phospholipase D (GPI-PLD)-catalyzed conversion of amphiphilic form of Zn^2+ -glycerophosphocholine cholinephosphodieterase (Amp-GPC PDE) into hydrophilic form was investigated in the presence of natural amphiphiles. Monoacylglycerols enhanced considerably the conversion by GPI-PLD of Amp-GPC PDE to hydrophilic form, with the enhancing effect of monoacylglycerols being dependent on the size of acyl group (C_8-C_18). Whereas the maximal enhancement of GPI-PLD action was the greatest with monodecanoylglycerol, the concentration (EC_50) required to achieve 50% maximal effect was the smallest for monomyristoyl- or monopalmitoylglycerol. In addition, monolaurylglycerol or its alkyl analogue, monododecylglycerol, showed a remarkable decrease in enhancing effect at high concentrations (>mM). Presence of double bond in acyl chain, as exemplified by monooleoylglycerol or mono-11-eicosenoin, further enhanced the conversion by GPI-PLD. Meanwhile, lysophosphatidylcholine (IC_50 25μM) and phosphatidic acid (IC_50 > 100 μM), ionic amphiphiles, inhibited the GPI-PLD activity, which was determined in the presence of monooleoyglycerol as a detergent. From these results, it is suggested that the activity of GPI-PLD in vivo system may be regulated by natural amphiphiles.
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KEYWORD
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GPI-PLD, regulation, glycerophosphocholine, phosphodiesterase, monoacylglycerols, lysophosphatidylcholine
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