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KMID : 0614019990150010238
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Journal of Pharmaceutical Sciences (C.N.U.)
1999 Volume.15 No. 1 p.238 ~ p.243
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Conversion of Glycosylphosphatidylinositol (GPI)-Anchored Alkaline Phosphatase by GPI-PLD
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Moon Young-Girl
Lee Hyun-Jeong
Kim Mee-Ree
Myung Pyung-Keun
Park Soo-Young
Sok Dai-Eun
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Abstract
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Enzymatic conversion of brain glycosylphosphatidylinositol-linked alkaline phosphatase (GPI-AP), amphiphilic was examined. When GPI-AP was incubated with glycosylphosphatidylinositol-specific phospholipase D (GPI-PLD), a negligible conversion of GPI-AP to hydrophilic form was observed. The inclusion of monoacylglycerols enhanced the enymatic conversion, although the action of monoacylglycerols differed greatly according to the size of acyl group the enzymatic conversion was enhanced considerably in the presence of monoacylglycerols possessing acyl group of longer chain length (C_10-C_18), while monoacylglycerols with acyl moiety of shorter length (C_4-C_8) did fail to augment the enzymatic conversion. Noteworthy, monooleovlglycerol was much more effective than the other monoacylglycerols in promoting the enzymatic conversion, indicating a beneficial role of the unsaturation in acyl chain Meanwhile, ionic amphiphiles such as monohexadecyllysophosphabdylcholine and palmitaylcarnitine decreased the enzymatic conversion of GPI-AP in a concentration-dependent manner, with monohexadecyllysophosphatidylcholine being more inhibitory than palmitoylcarnitine.
Separately, when GPI-AP was exposed to various oxidants prior to the incubation with GPI-PLD, a remarkable decrease of the enzymatic conversion was observed with hypochlorite and peroxynitrite generators, but not H_2O_2. In further study, hypochlorite was found to inactivate GPI-PLD at low concentrations (3-100μM). From these results, it is suggested that the enzymatic conversion of GPI-AP by GPI-PLD may be regulated in vivo system.
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KEYWORD
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GPI-PLD, Phosphatase, Enhancement, Inhibition, Inactivation
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