Bomalaski J S, Baker D, Resurreccion N V, Clark M A
V.A. Medical Center, Medical College of Pennsylvania, University of Pennsylvania, Philadelphia 19104.
Agents Actions. 1989 Jun;27(3-4):425-7. doi: 10.1007/BF01972841.
Rheumatoid arthritis is characterized by excessive eicosanoid production, and phospholipase enzymes are the rate limiting step in eicosanoid synthesis. We have shown previously that cells from patients with rheumatoid arthritis express enhanced phospholipase A2 enzyme activities. Recently, we have isolated a phospholipase A2 activating protein termed PLAP from rheumatoid synovial fluid. This novel human protein shares biochemical and antigenic similarities with melittin, a bee venom phospholipase activating protein. Because melittin has been shown to induce neutrophil degranulation and superoxide formation, and because exuberent release of lysosomal enzymes and superoxide have been implicated in the pathogenesis of rheumatoid arthritis, we examined the role of PLAP on inducing these neutrophil functions.
类风湿性关节炎的特征是类花生酸生成过多，而磷脂酶是类花生酸合成的限速步骤。我们之前已经表明，类风湿性关节炎患者的细胞表达增强的磷脂酶A2酶活性。最近，我们从类风湿性滑液中分离出一种称为PLAP的磷脂酶A2激活蛋白。这种新型人类蛋白与蜂毒磷脂酶激活蛋白蜂毒肽在生化和抗原方面具有相似性。由于蜂毒肽已被证明可诱导中性粒细胞脱颗粒和超氧化物形成，并且由于溶酶体酶和超氧化物的过度释放与类风湿性关节炎的发病机制有关，我们研究了PLAP在诱导这些中性粒细胞功能中的作用。
