一种丝氨酸酯酶参与肺内皮细胞中氧化剂介导的磷脂酶A2激活过程。
Involvement of a serine esterase in oxidant-mediated activation of phospholipase A2 in pulmonary endothelium.
作者信息
Chakraborti S, Michael J R
机构信息
Department of Biochemistry and Biophysics, University of Kalyani, India.
出版信息
FEBS Lett. 1991 Apr 9;281(1-2):185-7. doi: 10.1016/0014-5793(91)80389-k.
Exposure of bovine pulmonary arterial endothelial cells to 1 mM H2O2 stimulated associated TAME-esterase and PLA2 activities. Pretreatment with the serine esterase inhibitors: PMSF (1 mM), DFP (1 mM), and alpha 1-PI (1 mg/ml) inhibited H2O2-induced stimulation of TAME-esterase and PLA2 activities. The TAME-esterase and PLA2 activities under H2O2 exposure were determined to be linearly correlated. Affinity labelling of the endothelial cell membrane with [3H]DFP demonstrated that the serine esterase resides in a protein having molecular weight of 29,000 daltons (29 kDa) which is similar to that of elastase. Treatment of the endothelial cell homogenate with trypsin (1 microgram/ml) also stimulated PLA2 activity.
将牛肺动脉内皮细胞暴露于1 mM过氧化氢中会刺激相关的TAME酯酶和磷脂酶A2活性。用丝氨酸酯酶抑制剂进行预处理：苯甲基磺酰氟（PMSF，1 mM）、二异丙基氟磷酸（DFP，1 mM）和α1-抗胰蛋白酶（α1-PI，1 mg/ml）可抑制过氧化氢诱导的TAME酯酶和磷脂酶A2活性刺激。经测定，过氧化氢暴露下的TAME酯酶和磷脂酶A2活性呈线性相关。用[3H]DFP对内皮细胞膜进行亲和标记表明，丝氨酸酯酶存在于一种分子量为29000道尔顿（29 kDa）的蛋白质中，该蛋白质与弹性蛋白酶相似。用胰蛋白酶（1微克/毫升）处理内皮细胞匀浆也会刺激磷脂酶A2活性。
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