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KMID : 0043319990220030249
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Archives of Pharmacal Research
1999 Volume.22 No. 3 p.249 ~ p.254
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Conversion of Gycosylphosphatidylinositol (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 enzymatic 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 (), which monoacylglycerols with acyl moiety of shorter length () did fail to augment the enzymatic conversion. Noteworthy, monooleoylglycerol 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 monohexadecyllysophosphatidylcholoine and palmitoyl-carnitine decreased the enzymatic conversion of GPI-AP in a concentration-dependent manner, with monohexadecyllysophosphatidylcholine and palmitoyl-carnitine deceased the enzymatic conversion of GPI-AP in a concentration-dependent manner, with monohexadecyllysophosphatidylcholoine 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 peroynitrite generators, but not . In further study, hypochlorite was found to inactivate GPI-PLD at low concentrations (). 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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