RELEASE OF PLATELET-ACTIVATING FACTOR IN SYSTEMIC LUPUS-ERYTHEMATOSUS
RELEASE OF PLATELET-ACTIVATING FACTOR IN SYSTEMIC LUPUS-ERYTHEMATOSUS
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DOI：
10.1159/000235124
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发表时间：
1990-03-01
期刊：
影响因子：
--
通讯作者：
CAMUSSI, G
中科院分区：
文献类型：
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作者：
TETTA, C;BUSSOLINO, F;CAMUSSI, G
具有生物活性的1- o -烷基-2-乙酰基- cn -甘油-3-磷酸胆碱（血小板活化因子；PAF）在血浆中主要被一种特异性的PAF乙酰水解酶（1-烷基-2-乙酰基- cn -甘油-3-磷酸胆碱乙酰水解酶；EC 3.1.1.48）灭活。在本研究中，PAF以可检测的量（5.4 +-）释放。2.9 ng / ml;的意思。+ -。在系统性红斑狼疮（SLE）最活跃的阶段，10例患者中有8例血浆中含有1 SD)。在非活动性SLE患者或健康受试者的血浆中从未检测到PAF。10例活动性SLE患者血清PAF乙酰水解酶活性明显低于7例非活动性SLE患者、16例类风湿性关节炎（RA）患者、5例肾病综合征（NS）患者和15例健康受试者。活动性SLE患者的酶动力学研究表明，酶的整体活性降低，而不是内在缺陷。活动性SLE患者血清中PAF乙酰水解酶与健康人具有相同的底物特异性、对酶和化学物理治疗的敏感性以及与血浆中作为PAF乙酰水解酶载体的低密度脂蛋白（LDL）的相关性。然而，与非活动性SLE、RA和NS患者以及健康受试者相比，活动性SLE患者的LDL蛋白浓度显著降低，从而提示活动性SLE患者PAF乙酰水解酶活性的降低可能至少部分归因于与疾病活动性相关的载体缺陷。此外，将活动期SLE患者血清与健康人血清以不同组合混合的实验表明，SLE患者体内不存在抑制PAF乙酰水解酶活性的因素。
The biologically active 1-O-alkyl-2-acetyl-sn-glyceryl-3-phosphorylcholine (platelet-activating factor; PAF) is inactivated in plasma mainly by a specific PAF acetylhydrolase (1-alkyl-2-acetyl-sn-glyceryl-3-phosphorylcholine acetylhydrolase; EC 3.1.1.48). In the present study, PAF was released in detectable amounts (5.4 .+-. 2.9 ng/ml; mean .+-. 1 SD) in the plasma of 8 out of 10 patients with systemic lupus erythematosus (SLE) during the most active phases of the disease. PAF was never detectable in the plasma of patients with inactive SLE or of healthy subjects. PAF acetylhydrolase activity was markedly reduced in sera of 10 patients with active SLE as compared to 7 patients with inactive SLE, 16 patients with rheumatoid arthritis (RA), 5 patients with nephrotic syndrome (NS) and 15 healthy subjects. A kinetic study of the enzyme in patients with active SLE suggested an overall reduced activity rather than an intrinsic defect of the enzyme. PAF acetylhydrolase in sera of patients with active SLE shared with that of healthy subjects the same substrate specificity, sensitivity to enzymatic and chemicophysical treatments and association to low-density lipoprotein (LDL), acting as carrier of PAF acetylhydrolase in plasma. However, the protein concentration of LDL was significantly reduced in patients with active SLE as compared to patients with inactive SLE, RA and NS and to healthy subjects, thereby suggesting that the reduction of PAF acetylhydrolase activity in active SLE might be due at least in part to a carrier defect related to the activity of the disease. In addition, experiments in which serum of patients with active SLE and serum of healthy subjects were mixed in different combinations indicated the absence of factors inhibiting PAF acetylhydrolase activity in SLE patients.