CATABOLISM OF PLATELET-ACTIVATING-FACTOR AND ITS ACYL ANALOG - DIFFERENTIATION OF THE ACTIVITIES OF LYSOPHOSPHOLIPASE AND PLATELET-ACTIVATING-FACTOR ACETYLHYDROLASE

被引:41
作者
AARSMAN, AJ [1 ]
NEYS, FW [1 ]
VANDENBOSCH, H [1 ]
机构
[1] STATE UNIV UTRECHT,CTR BIOMEMBRANES & LIPID ENZYMOL,PADUALAAN 8,POB 80054,3508 TB UTRECHT,NETHERLANDS
来源
EUROPEAN JOURNAL OF BIOCHEMISTRY | 1991年 / 200卷 / 01期
关键词
D O I
10.1111/j.1432-1033.1991.tb21066.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
Recent investigations have shown the presence of 1-acyl-2-acetyl-sn-glycero-3-phospholine, i.e. the acyl analog of platelet-activating factor (PAF), in unstimulated tissues as well as its formation along with platelet-activating factor upon stimulation of a variety of cells. We demonstrate here that this acyl analog of PAF can be catabolized by purified lysophospholipases I and II from bovine liver with near stoichiometric formation of 2-acetyl-sn-glycero-3-phosphocholine. Lysophospholipase II also deacetylated PAF to lysoPAF and evidence is presented to show that this is an intrinsic activity of this enzyme. This suggested that some lysophospholipases may contribute to intracellular inactivation of PAF by deacetylation. Anion-exchange chromatography of rat liver cytosol confirmed this possibility. However, similar experiments with rat kidney cytosol and rat and human platelet cytosol clearly separated lysophospholipase activities without PAF acetylhydrolase activity from specific PAF acetylhydrolases not having lysophospholipase activity. Thus, lysophospholipases are clearly involved in the metabolism of the acyl analog of PAF and in some tissues, such as liver, may even contribute to abolishing the biological activity of PAF through deacetylation.
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页码:187 / 193
页数:7
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